Database of Protein Disorder
Names
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Database of Protein Disorder
metasource: Fairsharing.org
version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
metasource: re3data.org
version: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
DisProt
metasource: Fairsharing.org
version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
metasource: re3data.org
version: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
DisProt - Database of Protein Disorder
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
Database of protein disorder (DisProt)
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:59.960592
disprot
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:59.960592
Names
More detailed information about this field from each metasource.
Database of Protein Disorder
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
metasource: re3data.org
version: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
DisProt
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
metasource: re3data.org
version: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
DisProt - Database of Protein Disorder
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
Database of protein disorder (DisProt)
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:59.960592
disprot
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:59.960592
Other names: DisProt, DisProt - Database of Protein Disorder, Database of protein disorder (DisProt), disprot
Names
More detailed information about this field from each metasource.
Database of Protein Disorder
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
metasource: re3data.org
version: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
DisProt
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
metasource: re3data.org
version: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
DisProt - Database of Protein Disorder
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
Database of protein disorder (DisProt)
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:59.960592
disprot
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:59.960592
The Database of Protein Disorder (DisProt) is a curated database that provides information about intrinsically disordered proteins that lack fixed 3D structure in their putatively native states, either in their entirety or in part. Disordered regions are manually curated from literature. DisProt annotations cover both structural and functional aspects of disorder detected by specific experimental methods.
Description
More detailed information about this field from each metasource.
The Database of Protein Disorder (DisProt) is a curated database that provides information about intrinsically disordered proteins that lack fixed 3D structure in their putatively native states, either in their entirety or in part. Disordered regions are manually curated from literature. DisProt annotations cover both structural and functional aspects of disorder detected by specific experimental methods.
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Information about proteins that lack fixed 3D structure in their native states
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
The Database of Protein Disorder (DisProt) is a curated database that provides information about proteins that lack fixed 3D structure in their putatively native states, either in their entirety or in part. DisProt is a community resource annotating protein sequences for intrinsically disorder regions from the literature. It classifies intrinsic disorder based on experimental methods and three ontologies for molecular function, transition and binding partner.
metasource: re3data.orgversion: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
Database of protein disorder. It is a community resource annotating protein sequences for intrinsically disordered regions from the literature.
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:59.960592
Webpage:
http://www.disprot.org/Webpage
More detailed information about this field from each metasource.
http://www.disprot.org/
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
metasource: re3data.org
version: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:59.960592
http://www.dabi.temple.edu/disprot/
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
Licence:
Name: Creative Commons Attribution 4.0 International (CC BY 4.0)Licence name
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Creative Commons Attribution 4.0 International (CC BY 4.0)
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Copyrights
metasource: re3data.orgversion: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
CC-BY-NC-1.0
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:59.960592
Licence URL
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https://creativecommons.org/licenses/by/4.0/
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
http://www.disprot.org/protein.php?id=DP00747_C002
metasource: re3data.orgversion: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
Publications:
Publications
More detailed information about this field from each metasource.
DisProt: the Database of Disordered Proteins
PMID: 17145717
metasource: Fairsharing.org
version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
DisProt 7.0: a major update of the database of disordered proteins
PMID: 27899601
metasource: Fairsharing.org
version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
DisProt: intrinsic protein disorder annotation in 2020
PMID: 31713636
metasource: Fairsharing.org
version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Corrigendum: DisProt 7.0: a major update of the database of disordered proteins
PMID: 27965415
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:59.960592
http://bioinformatics.oxfordjournals.org/cgi/content/abstract/21/1/137
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
Publications
More detailed information about this field from each metasource.
DisProt: the Database of Disordered Proteins
PMID: 17145717
metasource: Fairsharing.org
version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
DisProt 7.0: a major update of the database of disordered proteins
PMID: 27899601
metasource: Fairsharing.org
version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
DisProt: intrinsic protein disorder annotation in 2020
PMID: 31713636
metasource: Fairsharing.org
version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Corrigendum: DisProt 7.0: a major update of the database of disordered proteins
PMID: 27965415
metasource: bio.tools
version: extracted_at: 2022-11-04T11:24:59.960592
http://bioinformatics.oxfordjournals.org/cgi/content/abstract/21/1/137
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
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DisProt: the Database of Disordered Proteins
PubMed citations: 343.
343 articles citing: DisProt: the Database of Disordered Proteins
Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions. PMID:35883444
Enhancement of the solubility of recombinant proteins by fusion with a short-disordered peptide. PMID:35835960
Predicting Protein Conformational Disorder and Disordered Binding Sites. PMID:35507260
Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. PMID:35454150
In Silico Characterisation of the Late Embryogenesis Abundant (LEA) Protein Families and Their Role in Desiccation Tolerance in Ramonda serbica Panc. PMID:35408906
The aqueous humor proteome is intrinsically disordered. PMID:35128080
Erythropoietin Interacts with Specific S100 Proteins. PMID:35053268
Computational Prediction of Intrinsically Disordered Proteins Based on Protein Sequences and Convolutional Neural Networks. PMID:34992646
Probing ion channel functional architecture and domain recombination compatibility by massively parallel domain insertion profiling. PMID:34880224
Implications derived from S-protein variants of SARS-CoV-2 from six continents. PMID:34571123
On the roles of intrinsically disordered proteins and regions in cell communication and signaling. PMID:34461937
Search for Highly Divergent Tandem Repeats in Amino Acid Sequences. PMID:34281150
Testing the length limit of loop grafting in a helical repeat protein. PMID:34235484
Prediction of secondary structure population and intrinsic disorder of proteins using multitask deep learning. PMID:33936509
Intrinsically Disordered Proteins as Regulators of Transient Biological Processes and as Untapped Drug Targets. PMID:33917117
RELT stains prominently in B-cell lymphomas and binds the hematopoietic transcription factor MDFIC. PMID:33367115
Comparative Assessment of Intrinsic Disorder Predictions with a Focus on Protein and Nucleic Acid-Binding Proteins. PMID:33291838
Bioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein. PMID:33073109
Exploring the sequence fitness landscape of a bridge between protein folds. PMID:33048928
Design principles of gene evolution for niche adaptation through changes in protein-protein interaction networks. PMID:32973219
Structure, dynamics and functions of UBQLNs: at the crossroads of protein quality control machinery. PMID:32965492
Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins. PMID:32867340
Intrinsically disordered proteins of viruses: Involvement in the mechanism of cell regulation and pathogenesis. PMID:32828463
De novo engineering of intracellular condensates using artificial disordered proteins. PMID:32747754
Identification of Intrinsic Disorder in Complexes from the Protein Data Bank. PMID:32743159
A convenient protein library for spectroscopic calibrations. PMID:32728409
Analyzing IDPs in Interactomes. PMID:32696395
ShiftCrypt: a web server to understand and biophysically align proteins through their NMR chemical shift values. PMID:32459331
Entropy, Fluctuations, and Disordered Proteins. PMID:32336912
Mutually exclusive locales for N-linked glycans and disorder in human glycoproteins. PMID:32269229
Hydropathy Patterning Complements Charge Patterning to Describe Conformational Preferences of Disordered Proteins. PMID:32227994
The Order-Disorder Continuum: Linking Predictions of Protein Structure and Disorder through Molecular Simulation. PMID:32034199
Bioinformatics for Renal and Urinary Proteomics: Call for Aggrandization. PMID:32024005
Translation of the intrinsically disordered protein α-synuclein is inhibited by a small molecule targeting its structured mRNA. PMID:31900363
The dark side of Alzheimer's disease: unstructured biology of proteins from the amyloid cascade signaling pathway. PMID:31894361
Modeling beta-sheet peptide-protein interactions: Rosetta FlexPepDock in CAPRI rounds 38-45. PMID:31891416
An intrinsically disordered proteins community for ELIXIR. PMID:31824649
Sequence specificity despite intrinsic disorder: How a disease-associated Val/Met polymorphism rearranges tertiary interactions in a long disordered protein. PMID:31626641
Conservation of Potentially Druggable Cavities in Intrinsically Disordered Proteins. PMID:31458221
An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes. PMID:31342121
Structural Analysis and Conformational Dynamics of STN1 Gene Mutations Involved in Coat Plus Syndrome. PMID:31245382
The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins. PMID:31139867
Structural and functional impact of non-synonymous SNPs in the CST complex subunit TEN1: structural genomics approach. PMID:31028137
Recent Advances in Computational Protocols Addressing Intrinsically Disordered Proteins. PMID:30979035
Quality and bias of protein disorder predictors. PMID:30914747
c.259A>C in the fibrinogen gene of alpha chain (FGA) is a fibrinogen with thrombotic phenotype. PMID:30881084
On the Need to Develop Guidelines for Characterizing and Reporting Intrinsic Disorder in Proteins. PMID:30793871
A new technique for predicting intrinsically disordered regions based on average distance map constructed with inter-residue average distance statistics. PMID:30727987
Understanding the evolutionary trend of intrinsically structural disorders in cancer relevant proteins as probed by Shannon entropy scoring and structure network analysis. PMID:30717651
Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments. PMID:30713842
Misprediction of Structural Disorder in Halophiles. PMID:30699990
The C Terminus of the Ribosomal-Associated Protein LrtA Is an Intrinsically Disordered Oligomer. PMID:30563168
Structural disorder in the proteome and interactome of Alkhurma virus (ALKV). PMID:30443749
Large-Scale Analyses of Site-Specific Evolutionary Rates across Eukaryote Proteomes Reveal Confounding Interactions between Intrinsic Disorder, Secondary Structure, and Functional Domains. PMID:30441862
In silico approach to identify non-synonymous SNPs with highest predicted deleterious effect on protein function in human obesity related gene, neuronal growth regulator 1 (NEGR1). PMID:30402368
Virus discovery in all three major lineages of terrestrial arthropods highlights the diversity of single-stranded DNA viruses associated with invertebrates. PMID:30324030
Zn2+-binding in the glutamate-rich region of the intrinsically disordered protein prothymosin-alpha. PMID:30187212
EDEM1's mannosidase-like domain binds ERAD client proteins in a redox-sensitive manner and possesses catalytic activity. PMID:30021839
Comprehensive in-silico prediction of damage associated SNPs in Human Prolidase gene. PMID:29930383
A novel role of C-terminus in introducing a functionally flexible structure critical for the biological activity of botulinum neurotoxin. PMID:29891845
Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii. PMID:29717210
Grid-based prediction of torsion angle probabilities of protein backbone and its application to discrimination of protein intrinsic disorder regions and selection of model structures. PMID:29390958
Functional Analysis of Human Hub Proteins and Their Interactors Involved in the Intrinsic Disorder-Enriched Interactions. PMID:29257115
Intrinsic Disorder in Proteins with Pathogenic Repeat Expansions. PMID:29186753
Analysis of the interactome of Schistosoma mansoni histone deacetylase 8. PMID:29155817
Structure and function of yeast Atg20, a sorting nexin that facilitates autophagy induction. PMID:29114050
First Experimental Assessment of Protein Intrinsic Disorder Involvement in an RNA Virus Natural Adaptive Process. PMID:29029259
Effects of short indels on protein structure and function in human genomes. PMID:28839204
Polymorphism and structure of style-specific arabinogalactan proteins as determinants of pollen tube growth in Nicotiana. PMID:28797243
An Efficient Method for Estimating the Hydrodynamic Radius of Disordered Protein Conformations. PMID:28793210
Predictions of Backbone Dynamics in Intrinsically Disordered Proteins Using De Novo Fragment-Based Protein Structure Predictions. PMID:28765603
Predicting the functional consequences of non-synonymous single nucleotide polymorphisms in IL8 gene. PMID:28747718
Quantiprot - a Python package for quantitative analysis of protein sequences. PMID:28716000
The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner. PMID:28701465
Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions. PMID:28589442
Designing disorder: Tales of the unexpected tails. PMID:28516025
Distribution and cluster analysis of predicted intrinsically disordered protein Pfam domains. PMID:28516017
The alphabet of intrinsic disorder: II. Various roles of glutamic acid in ordered and intrinsically disordered proteins. PMID:28516010
MFDp2: Accurate predictor of disorder in proteins by fusion of disorder probabilities, content and profiles. PMID:28516009
The alphabet of intrinsic disorder: I. Act like a Pro: On the abundance and roles of proline residues in intrinsically disordered proteins. PMID:28516008
Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions. PMID:28510039
Dissecting physical structure of calreticulin, an intrinsically disordered Ca2+-buffering chaperone from endoplasmic reticulum. PMID:28504081
Phase Separation and Single-Chain Compactness of Charged Disordered Proteins Are Strongly Correlated. PMID:28483149
Opposing Intermolecular Tuning of Ca2+ Affinity for Calmodulin by Neurogranin and CaMKII Peptides. PMID:28355539
Stress-Triggered Phase Separation Is an Adaptive, Evolutionarily Tuned Response. PMID:28283059
Genes encoding intrinsic disorder in Eukaryota have high GC content. PMID:28232902
How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe. PMID:28232901
Understanding the roles of intrinsic disorder in subunits of hemoglobin and the disease process of sickle cell anemia. PMID:28232898
Quarterly intrinsic disorder digest (January-February-March, 2014). PMID:28232896
Paradoxes and wonders of intrinsic disorder: Complexity of simplicity. PMID:28232895
The intrinsic disorder alphabet. III. Dual personality of serine. PMID:28232888
An optimized Npro-based method for the expression and purification of intrinsically disordered proteins for an NMR study. PMID:28232886
Protein Bioinformatics Databases and Resources. PMID:28150231
Regulation of human polλ by ATM-mediated phosphorylation during non-homologous end joining. PMID:28109743
CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins. PMID:28076807
DisProt 7.0: a major update of the database of disordered proteins. PMID:27899601
Intrinsic disorder in proteins involved in amyotrophic lateral sclerosis. PMID:27838743
FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies. PMID:27794553
Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment. PMID:27668217
Structured States of Disordered Proteins from Genomic Sequences. PMID:27662088
Intrinsic Disorder of the C-Terminal Domain of Drosophila Methoprene-Tolerant Protein. PMID:27657508
Large-scale analysis of intrinsic disorder flavors and associated functions in the protein sequence universe. PMID:27636733
Estimation of Position Specific Energy as a Feature of Protein Residues from Sequence Alone for Structural Classification. PMID:27588752
AUCpreD: proteome-level protein disorder prediction by AUC-maximized deep convolutional neural fields. PMID:27587688
Resonance assignment of disordered protein with repetitive and overlapping sequence using combinatorial approach reveals initial structural propensities and local restrictions in the denatured state. PMID:27586017
G23D: Online tool for mapping and visualization of genomic variants on 3D protein structures. PMID:27565432
Order, Disorder, and Everything in Between. PMID:27548131
Structural Basis for Recombinatorial Permissiveness in the Generation of Anaplasma marginale Msp2 Antigenic Variants. PMID:27400719
A collection of intrinsic disorder characterizations from eukaryotic proteomes. PMID:27326998
DFLpred: High-throughput prediction of disordered flexible linker regions in protein sequences. PMID:27307636
Phasins, Multifaceted Polyhydroxyalkanoate Granule-Associated Proteins. PMID:27287326
Computational Framework for Prediction of Peptide Sequences That May Mediate Multiple Protein Interactions in Cancer-Associated Hub Proteins. PMID:27218803
Cryptic sequence features within the disordered protein p27Kip1 regulate cell cycle signaling. PMID:27140628
Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics. PMID:27124275
Tick receptor for outer surface protein A from Ixodes ricinus - the first intrinsically disordered protein involved in vector-microbe recognition. PMID:27112540
Functional Diversification after Gene Duplication: Paralog Specific Regions of Structural Disorder and Phosphorylation in p53, p63, and p73. PMID:27003913
PDP-CON: prediction of domain/linker residues in protein sequences using a consensus approach. PMID:26969678
A transducible nuclear/nucleolar protein, mLLP, regulates neuronal morphogenesis and synaptic transmission. PMID:26961175
Statistical prediction of protein structural, localization and functional properties by the analysis of its fragment mass distributions after proteolytic cleavage. PMID:26924271
Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling. PMID:26922996
There is Diversity in Disorder-"In all Chaos there is a Cosmos, in all Disorder a Secret Order". PMID:26904549
Natural protein sequences are more intrinsically disordered than random sequences. PMID:26801222
Protein unfolding as a switch from self-recognition to high-affinity client binding. PMID:26787517
Discovery, Prevalence, and Persistence of Novel Circular Single-Stranded DNA Viruses in the Ctenophores Mnemiopsis leidyi and Beroe ovata. PMID:26733971
Compartmentalization and Functionality of Nuclear Disorder: Intrinsic Disorder and Protein-Protein Interactions in Intra-Nuclear Compartments. PMID:26712748
Resolving the ambiguity: Making sense of intrinsic disorder when PDB structures disagree. PMID:26683124
Bioinformatical parsing of folding-on-binding proteins reveals their compositional and evolutionary sequence design. PMID:26678310
Experimental detection of short regulatory motifs in eukaryotic proteins: tips for good practice as well as for bad. PMID:26581338
KMAD: knowledge-based multiple sequence alignment for intrinsically disordered proteins. PMID:26568635
Analysis of the native conformation of the LIR/AIM motif in the Atg8/LC3/GABARAP-binding proteins. PMID:26565669
Continuous Distributed Representation of Biological Sequences for Deep Proteomics and Genomics. PMID:26555596
Evolutionarily Conserved Sequence Features Regulate the Formation of the FG Network at the Center of the Nuclear Pore Complex. PMID:26541386
DisPredict: A Predictor of Disordered Protein Using Optimized RBF Kernel. PMID:26517719
Tandem Repeats in Proteins: Prediction Algorithms and Biological Role. PMID:26442257
An Overview of Predictors for Intrinsically Disordered Proteins over 2010-2014. PMID:26426014
New genes drive the evolution of gene interaction networks in the human and mouse genomes. PMID:26424194
Elastin-like polypeptides as models of intrinsically disordered proteins. PMID:26325592
Accurate Ab Initio and Template-Based Prediction of Short Intrinsically-Disordered Regions by Bidirectional Recurrent Neural Networks Trained on Large-Scale Datasets. PMID:26307973
Computational approaches for inferring the functions of intrinsically disordered proteins. PMID:26301226
Structural modeling and in silico analysis of non-synonymous single nucleotide polymorphisms of human 3β-hydroxysteroid dehydrogenase type 2. PMID:26288759
New Insights into the Roles of Nogo-A in CNS Biology and Diseases. PMID:26266872
Unfoldome variation upon plant-pathogen interactions: strawberry infection by Colletotrichum acutatum. PMID:26245354
Protein Folding and Mechanisms of Proteostasis. PMID:26225966
MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data. PMID:26219516
Novel circular single-stranded DNA viruses identified in marine invertebrates reveal high sequence diversity and consistent predicted intrinsic disorder patterns within putative structural proteins. PMID:26217327
Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins. PMID:26216991
An Overview of Practical Applications of Protein Disorder Prediction and Drive for Faster, More Accurate Predictions. PMID:26198229
Conformational Entropy of Intrinsically Disordered Proteins from Amino Acid Triads. PMID:26138206
Highly homologous proteins exert opposite biological activities by using different interaction interfaces. PMID:26130271
High-throughput prediction of RNA, DNA and protein binding regions mediated by intrinsic disorder. PMID:26109352
Post-translationally-modified structures in the autophagy machinery: an integrative perspective. PMID:26108642
DisoMCS: Accurately Predicting Protein Intrinsically Disordered Regions Using a Multi-Class Conservative Score Approach. PMID:26090958
Identifying Similar Patterns of Structural Flexibility in Proteins by Disorder Prediction and Dynamic Programming. PMID:26086829
Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access. PMID:26038108
Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators. PMID:25988147
DisCons: a novel tool to quantify and classify evolutionary conservation of intrinsic protein disorder. PMID:25968230
Relating sequence encoded information to form and function of intrinsically disordered proteins. PMID:25863585
Identification of inhibitors of biological interactions involving intrinsically disordered proteins. PMID:25849651
Intrinsic disorder and metal binding in UreG proteins from Archae hyperthermophiles: GTPase enzymes involved in the activation of Ni(II) dependent urease. PMID:25846143
Conformational frustration in calmodulin-target recognition. PMID:25622562
Binding cavities and druggability of intrinsically disordered proteins. PMID:25611056
Nup98 FG domains from diverse species spontaneously phase-separate into particles with nuclear pore-like permselectivity. PMID:25562883
Improving protein order-disorder classification using charge-hydropathy plots. PMID:25559583
Intrinsically disordered proteins in cellular signalling and regulation. PMID:25531225
TDP-43 N terminus encodes a novel ubiquitin-like fold and its unfolded form in equilibrium that can be shifted by binding to ssDNA. PMID:25503365
Rapid evolution of virus sequences in intrinsically disordered protein regions. PMID:25502394
Protein structure annotation resources. PMID:25502191
Intrinsically disordered and pliable Starmaker-like protein from medaka (Oryzias latipes) controls the formation of calcium carbonate crystals. PMID:25490041
Intrinsic disorder mediates hepatitis C virus core-host cell protein interactions. PMID:25424537
DISOPRED3: precise disordered region predictions with annotated protein-binding activity. PMID:25391399
MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins. PMID:25361972
The dynamics of signal amplification by macromolecular assemblies for the control of chromosome segregation. PMID:25324779
Comparison of amino acids physico-chemical properties and usage of late embryogenesis abundant proteins, hydrophilins and WHy domain. PMID:25296175
Grain setting defect1, encoding a remorin protein, affects the grain setting in rice through regulating plasmodesmatal conductance. PMID:25253885
Discriminating between deleterious and neutral non-frameshifting indels based on protein interaction networks and hybrid properties. PMID:25248637
Hamiltonian Switch Metropolis Monte Carlo Simulations for Improved Conformational Sampling of Intrinsically Disordered Regions Tethered to Ordered Domains of Proteins. PMID:25136274
A phasin with many faces: structural insights on PhaP from Azotobacter sp. FA8. PMID:25077609
Molecular docking simulations provide insights in the substrate binding sites and possible substrates of the ABCC6 transporter. PMID:25062064
iMethyl-PseAAC: identification of protein methylation sites via a pseudo amino acid composition approach. PMID:24977164
A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein. PMID:24976112
Continuous wave W- and D-band EPR spectroscopy offer "sweet-spots" for characterizing conformational changes and dynamics in intrinsically disordered proteins. PMID:24950408
Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life. PMID:24939692
Interaction of Sesbania mosaic virus (SeMV) RNA-dependent RNA polymerase (RdRp) with the p10 domain of polyprotein 2a and its implications in SeMV replication. PMID:24918050
The structural and functional signatures of proteins that undergo multiple events of post-translational modification. PMID:24888500
Identification of Atg3 as an intrinsically disordered polypeptide yields insights into the molecular dynamics of autophagy-related proteins in yeast. PMID:24879155
Ion channel regulation by protein S-acylation. PMID:24821965
Synonymous constraint elements show a tendency to encode intrinsically disordered protein segments. PMID:24809503
Calponin-like Chd64 is partly disordered. PMID:24805353
PredictProtein--an open resource for online prediction of protein structural and functional features. PMID:24799431
Classification of intrinsically disordered regions and proteins. PMID:24773235
Intrinsic disorder in the BK channel and its interactome. PMID:24727949
Disordered proteinaceous machines. PMID:24702702
Association between foldability and aggregation propensity in small disulfide-rich proteins. PMID:24635049
Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins. PMID:24594841
Modelling the yeast interactome. PMID:24589662
The cleverSuite approach for protein characterization: predictions of structural properties, solubility, chaperone requirements and RNA-binding abilities. PMID:24493033
A comparative study of Whi5 and retinoblastoma proteins: from sequence and structure analysis to intracellular networks. PMID:24478706
Conformational flexibility of the oncogenic protein LMO2 primes the formation of the multi-protein transcription complex. PMID:24407558
Comprehensive repertoire of foldable regions within whole genomes. PMID:24204229
IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners. PMID:24178034
pE-DB: a database of structural ensembles of intrinsically disordered and of unfolded proteins. PMID:24174539
On the role of aggregation prone regions in protein evolution, stability, and enzymatic catalysis: insights from diverse analyses. PMID:24146608
The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes. PMID:24055376
On the importance of polar interactions for complexes containing intrinsically disordered proteins. PMID:23990768
Assessment of protein disorder region predictions in CASP10. PMID:23946100
A creature with a hundred waggly tails: intrinsically disordered proteins in the ribosome. PMID:23942625
Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues. PMID:23901099
Ion Mobility Spectrometry-Mass Spectrometry of Intrinsically Unfolded Proteins: Trying to Put Order into Disorder. PMID:23885220
Time window expansion for HDX analysis of an intrinsically disordered protein. PMID:23884631
Did the prion protein become vulnerable to misfolding after an evolutionary divide and conquer event? PMID:23859022
Atg29 phosphorylation regulates coordination of the Atg17-Atg31-Atg29 complex with the Atg11 scaffold during autophagy initiation. PMID:23858448
Analysis and consensus of currently available intrinsic protein disorder annotation sources in the MobiDB database. PMID:23815411
Pan1 is an intrinsically disordered protein with homotypic interactions. PMID:23801378
Modulating the intrinsic disorder in the cytoplasmic domain alters the biological activity of the N-methyl-D-aspartate-sensitive glutamate receptor. PMID:23782697
In silico prediction of a disease-associated STIL mutant and its affect on the recruitment of centromere protein J (CENPJ). PMID:23772360
Resilience of death: intrinsic disorder in proteins involved in the programmed cell death. PMID:23764774
Intrinsically semi-disordered state and its role in induced folding and protein aggregation. PMID:23723000
A novel method of predicting protein disordered regions based on sequence features. PMID:23710446
Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains. PMID:23663289
Malleable ribonucleoprotein machine: protein intrinsic disorder in the Saccharomyces cerevisiae spliceosome. PMID:23638354
The challenge of increasing Pfam coverage of the human proteome. PMID:23603847
Analyses of the general rule on residue pair frequencies in local amino acid sequences of soluble, ordered proteins. PMID:23526551
Are all regions of folded proteins that undergo ligand-dependent order-disorder transitions targets for allosteric peptide mimetics? PMID:23520021
Actinidia DRM1--an intrinsically disordered protein whose mRNA expression is inversely correlated with spring budbreak in kiwifruit. PMID:23516402
All-atom ensemble modeling to analyze small-angle x-ray scattering of glycosylated proteins. PMID:23473666
Inherent relationships among different biophysical prediction methods for intrinsically disordered proteins. PMID:23442871
Regulatory motifs in Chk1. PMID:23422000
Rapid evolutionary dynamics of structural disorder as a potential driving force for biological divergence in flaviviruses. PMID:23418179
The case for intrinsically disordered proteins playing contributory roles in molecular recognition without a stable 3D structure. PMID:23361308
Evolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sites. PMID:23341186
Improving the chemical shift dispersion of multidimensional NMR spectra of intrinsically disordered proteins. PMID:23314728
Assessment of 3D models for allergen research. PMID:23239464
Utilization of protein intrinsic disorder knowledge in structural proteomics. PMID:23232152
D²P²: database of disordered protein predictions. PMID:23203878
An assignment of intrinsically disordered regions of proteins based on NMR structures. PMID:23142703
When a domain is not a domain, and why it is important to properly filter proteins in databases: conflicting definitions and fold classification systems for structural domains make filtering of such databases imperative. PMID:23108912
Hydrogen-exchange mass spectrometry for the study of intrinsic disorder in proteins. PMID:23099262
An N-terminal, 830 residues intrinsically disordered region of the cytoskeleton-regulatory protein supervillin contains Myosin II- and F-actin-binding sites. PMID:23075227
Cell cycle regulation by the intrinsically disordered proteins p21 and p27. PMID:22988851
Virtual interactomics of proteins from biochemical standpoint. PMID:22928109
Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression. PMID:22924672
Computational analysis of position-dependent disorder content in DisProt database. PMID:22917189
Fast association and slow transitions in the interaction between two intrinsically disordered protein domains. PMID:22915588
Evolution of viral proteins originated de novo by overprinting. PMID:22821011
Analysis of conformational variation in macromolecular structural models. PMID:22808083
Structural role of RKS motifs in chromatin interactions: a molecular dynamics study of HP1 bound to a variably modified histone tail. PMID:22768949
Phosphorylation of intrinsically disordered regions in remorin proteins. PMID:22639670
MetaDisorder: a meta-server for the prediction of intrinsic disorder in proteins. PMID:22624656
Computational and statistical analyses of amino acid usage and physico-chemical properties of the twelve late embryogenesis abundant protein classes. PMID:22615859
Direct ubiquitin independent recognition and degradation of a folded protein by the eukaryotic proteasomes-origin of intrinsic degradation signals. PMID:22506054
PrionHome: a database of prions and other sequences relevant to prion phenomena. PMID:22363733
Cells diversify transmembrane signaling through the controlled chaos of protein disorder. PMID:22299058
SPINE-D: accurate prediction of short and long disordered regions by a single neural-network based method. PMID:22208280
Unsupervised Integration of Multiple Protein Disorder Predictors: The Method and Evaluation on CASP7, CASP8 and CASP9 Data. PMID:22166115
Evolution of immunity: no development without risk. PMID:22095544
Disease mutations in disordered regions--exception to the rule? PMID:22080206
IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature. PMID:22067451
Soluble expression, purification and characterization of the full length IS2 Transposase. PMID:22032517
Mechanical unfolding of cardiac myosin binding protein-C by atomic force microscopy. PMID:22004751
Evaluation of disorder predictions in CASP9. PMID:21928402
A comprehensive overview of computational protein disorder prediction methods. PMID:21874190
Differential occurrence of protein intrinsic disorder in the cytoplasmic signaling domains of cell receptors. PMID:21776336
Expanding the proteome: disordered and alternatively folded proteins. PMID:21729349
Novel strategies for drug discovery based on Intrinsically Disordered Proteins (IDPs). PMID:21686180
In-silico prediction of disorder content using hybrid sequence representation. PMID:21682902
CSpritz: accurate prediction of protein disorder segments with annotation for homology, secondary structure and linear motifs. PMID:21646342
Constructing ensembles for intrinsically disordered proteins. PMID:21530234
Evolution and disorder. PMID:21482101
Bioinformatics analysis of disordered proteins in prokaryotes. PMID:21366926
Self-organization and regulation of intrinsically disordered proteins with folded N-termini. PMID:21347241
Effects of HMGN variants on the cellular transcription profile. PMID:21278158
LPS-annotate: complete annotation of compositionally biased regions in the protein knowledgebase. PMID:21216786
Functional role of ribosomal signatures. PMID:21156135
Refining orthologue groups at the transcript level. PMID:21143794
Evolution of structurally disordered proteins promotes neostructuralization. PMID:21037204
Library of disordered patterns in 3D protein structures. PMID:20976197
Subcellular TSC22D4 localization in cerebellum granule neurons of the mouse depends on development and differentiation. PMID:20878296
Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assembly. PMID:20875424
Ways and means of coping with uncertainties of the relationship of the genetic blue print to protein structure and function in the cell. PMID:20849616
Improved sequence-based prediction of disordered regions with multilayer fusion of multiple information sources. PMID:20823312
Reduction in structural disorder and functional complexity in the thermal adaptation of prokaryotes. PMID:20711457
Prediction of deleterious non-synonymous SNPs based on protein interaction network and hybrid properties. PMID:20689580
Intrinsically disordered regions may lower the hydration free energy in proteins: a case study of nudix hydrolase in the bacterium Deinococcus radiodurans. PMID:20657662
Targeting intrinsically disordered proteins in neurodegenerative and protein dysfunction diseases: another illustration of the D(2) concept. PMID:20653509
Functional dissection of an intrinsically disordered protein: understanding the roles of different domains of Knr4 protein in protein-protein interactions. PMID:20506404
SPA: Short peptide analyzer of intrinsic disorder status of short peptides. PMID:20497238
Predictors of natively unfolded proteins: unanimous consensus score to detect a twilight zone between order and disorder in generic datasets. PMID:20409339
Unique physical properties and interactions of the domains of methylated DNA binding protein 2. PMID:20405910
A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins. PMID:20368288
Dual coding in alternative reading frames correlates with intrinsic protein disorder. PMID:20212158
Order and disorder in the domain organization of the plasmid partition protein KorB. PMID:20200158
Parameterization of disorder predictors for large-scale applications requiring high specificity by using an extended benchmark dataset. PMID:20158872
N-terminal domains of DELLA proteins are intrinsically unstructured in the absence of interaction with GID1/gibberellic acid receptors. PMID:20103592
PONDR-FIT: a meta-predictor of intrinsically disordered amino acids. PMID:20100603
In silico functional profiling of human disease-associated and polymorphic amino acid substitutions. PMID:20052762
From protein sequences to 3D-structures and beyond: the example of the UniProt knowledgebase. PMID:20043185
Trade-off between positive and negative design of protein stability: from lattice models to real proteins. PMID:20011105
ComSin: database of protein structures in bound (complex) and unbound (single) states in relation to their intrinsic disorder. PMID:19906708
Intrinsic structural disorder confers cellular viability on oncogenic fusion proteins. PMID:19888473
Intrinsically disordered proteins and their environment: effects of strong denaturants, temperature, pH, counter ions, membranes, binding partners, osmolytes, and macromolecular crowding. PMID:19768526
Disordered plant LEA proteins as molecular chaperones. PMID:19704836
Overlapping genes produce proteins with unusual sequence properties and offer insight into de novo protein creation. PMID:19640978
Susceptibility of p53 unstructured N terminus to 20 S proteasomal degradation programs the stress response. PMID:19617345
Protein disorder in the human diseasome: unfoldomics of human genetic diseases. PMID:19594871
Analysis of structured and intrinsically disordered regions of transmembrane proteins. PMID:19585006
The role of intrinsically unstructured proteins in neurodegenerative diseases. PMID:19440375
Prediction of protein binding regions in disordered proteins. PMID:19412530
The apoptotic machinery as a biological complex system: analysis of its omics and evolution, identification of candidate genes for fourteen major types of cancer, and experimental validation in CML and neuroblastoma. PMID:19402918
Development of an accurate classification system of proteins into structured and unstructured regions that uncovers novel structural domains: its application to human transcription factors. PMID:19402914
Disorder-to-order conformational transitions in protein structure and its relationship to disease. PMID:19357935
CDF it all: consensus prediction of intrinsically disordered proteins based on various cumulative distribution functions. PMID:19351533
At low concentrations, 3,4-dihydroxyphenylacetic acid (DOPAC) binds non-covalently to alpha-synuclein and prevents its fibrillation. PMID:19328209
Nuclear magnetic resonance and circular dichroism study of metastin (Kisspeptin-54) structure in solution. PMID:19308666
CP12 from Chlamydomonas reinhardtii, a permanent specific "chaperone-like" protein of glyceraldehyde-3-phosphate dehydrogenase. PMID:19287002
Order propensity of an intrinsically disordered protein, the cyclin-dependent-kinase inhibitor Sic1. PMID:19280601
Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction. PMID:19251668
Protein ionizable groups: pK values and their contribution to protein stability and solubility. PMID:19164280
Synchronous vs asynchronous chain motion in alpha-synuclein contact dynamics. PMID:19099437
Malleable machines in transcription regulation: the mediator complex. PMID:19096501
Large-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteome. PMID:19067583
Malleable machines take shape in eukaryotic transcriptional regulation. PMID:19008886
TOP-IDP-scale: a new amino acid scale measuring propensity for intrinsic disorder. PMID:18991772
A comparative analysis of viral matrix proteins using disorder predictors. PMID:18947403
The unfoldomics decade: an update on intrinsically disordered proteins. PMID:18831774
An unusual intrinsically disordered protein from the model legume Lotus japonicus stabilizes proteins in vitro. PMID:18779323
Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains. PMID:18713862
Effect of methionine oxidation on the structural properties, conformational stability, and aggregation of immunoglobulin light chain LEN. PMID:18652490
Intrinsic disorder in scaffold proteins: getting more from less. PMID:18619997
Potato virus A genome-linked protein VPg is an intrinsically disordered molten globule-like protein with a hydrophobic core. PMID:18533220
A structural annotation resource for the selection of putative target proteins in the malaria parasite. PMID:18500983
SEQATOMS: a web tool for identifying missing regions in PDB in sequence context. PMID:18463137
A new protein linear motif benchmark for multiple sequence alignment software. PMID:18439277
Prevalence of intrinsic disorder in the intracellular region of human single-pass type I proteins: the case of the notch ligand Delta-4. PMID:18435556
Regulation of Escherichia coli SOS mutagenesis by dimeric intrinsically disordered umuD gene products. PMID:18216271
Expression, purification, and characterization of a structurally disordered and functional C-terminal autoinhibitory domain (AID) of the 70 kDa 40S ribosomal protein S6 kinase-1 (S6K1). PMID:17980619
Protein aggregation processes: In search of the mechanism. PMID:17962399
Structural disorder promotes assembly of protein complexes. PMID:17922903
Optimization of linear disorder predictors yields tight association between crystallographic disorder and hydrophobicity. PMID:17893360
Between order and disorder in protein structures: analysis of "dual personality" fragments in proteins. PMID:17850753
The EM structure of human DNA polymerase gamma reveals a localized contact between the catalytic and accessory subunits. PMID:17762861
Composition Profiler: a tool for discovery and visualization of amino acid composition differences. PMID:17578581
Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions. PMID:17391014
Intrinsic disorder and functional proteomics. PMID:17158572 -
DisProt 7.0: a major update of the database of disordered proteins
PubMed citations: 83.
83 articles citing: DisProt 7.0: a major update of the database of disordered proteins
Enhancement of the solubility of recombinant proteins by fusion with a short-disordered peptide. PMID:35835960
Identification of Intrinsically Disordered Proteins and Regions in a Non-Model Insect Species Ostrinia nubilalis (Hbn.). PMID:35454181
Distribution of Charged Residues Affects the Average Size and Shape of Intrinsically Disordered Proteins. PMID:35454150
MoRF-FUNCpred: Molecular Recognition Feature Function Prediction Based on Multi-Label Learning and Ensemble Learning. PMID:35350759
Identifying Intrinsically Disordered Protein Regions through a Deep Neural Network with Three Novel Sequence Features. PMID:35330096
Tools for Characterizing Proteins: Circular Variance, Mutual Proximity, Chameleon Sequences, and Subsequence Propensities. PMID:35298807
A FRET-Based Biosensor for the Src N-Terminal Regulatory Element. PMID:35200356
Pan-cancer assessment of mutational landscape in intrinsically disordered hotspots reveals potential driver genes. PMID:35061901
The dynamic basis of structural order in proteins. PMID:34981860
Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins. PMID:34710373
ProTG4: A Web Server to Approximate the Sequence of a Generic Protein From an in Silico Library of Translatable G-Quadruplex (TG4)-Mapped Peptides. PMID:34602814
p27Kip1, an Intrinsically Unstructured Protein with Scaffold Properties. PMID:34571903
Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association. PMID:34527192
On the roles of intrinsically disordered proteins and regions in cell communication and signaling. PMID:34461937
flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions. PMID:34290238
Updated SARS-CoV-2 single nucleotide variants and mortality association. PMID:34245452
FG nucleoporins feature unique patterns that distinguish them from other IDPs. PMID:34237287
Online biophysical predictions for SARS-CoV-2 proteins. PMID:33892639
Consistent Force Field Captures Homologue-Resolved HP1 Phase Separation. PMID:33826337
Exploring the conformational dynamics and flexibility of intrinsically disordered HIV-1 Nef protein using molecular dynamic network approaches. PMID:33747706
Tuning intrinsic disorder predictors for virus proteins. PMID:33614158
Comparative Assessment of Intrinsic Disorder Predictions with a Focus on Protein and Nucleic Acid-Binding Proteins. PMID:33291838
Sequence Versus Composition: What Prescribes IDP Biophysical Properties? PMID:33267368
A Suggestion of Converting Protein Intrinsic Disorder to Structural Entropy Using Shannon's Information Theory. PMID:33267305
Liquid-Liquid Phase Separation by Intrinsically Disordered Protein Regions of Viruses: Roles in Viral Life Cycle and Control of Virus-Host Interactions. PMID:33260713
Revealing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment. PMID:33191750
The Anti-Inflammatory Protein TNIP1 Is Intrinsically Disordered with Structural Flexibility Contributed by Its AHD1-UBAN Domain. PMID:33182596
Design principles of gene evolution for niche adaptation through changes in protein-protein interaction networks. PMID:32973219
Protein Databases Related to Liquid-Liquid Phase Separation. PMID:32947964
Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins. PMID:32867340
IDRMutPred: predicting disease-associated germline nonsynonymous single nucleotide variants (nsSNVs) in intrinsically disordered regions. PMID:32756939
Predicting Conformational Properties of Intrinsically Disordered Proteins from Sequence. PMID:32696367
How to Annotate and Submit a Short Linear Motif to the Eukaryotic Linear Motif Resource. PMID:32696353
A Unified De Novo Approach for Predicting the Structures of Ordered and Disordered Proteins. PMID:32525675
SIB Literature Services: RESTful customizable search engines in biomedical literature, enriched with automatically mapped biomedical concepts. PMID:32379317
Physical Chemistry of the Protein Backbone: Enabling the Mechanisms of Intrinsic Protein Disorder. PMID:32349480
SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning. PMID:32173600
RFPR-IDP: reduce the false positive rates for intrinsically disordered protein and region prediction by incorporating both fully ordered proteins and disordered proteins. PMID:32112084
Specific Conformational Dynamics and Expansion Underpin a Multi-Step Mechanism for Specific Binding of p27 with Cdk2/Cyclin A. PMID:32088186
The Order-Disorder Continuum: Linking Predictions of Protein Structure and Disorder through Molecular Simulation. PMID:32034199
Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins. PMID:32020911
Biotin proximity tagging favours unfolded proteins and enables the study of intrinsically disordered regions. PMID:31969649
InterPep2: global peptide-protein docking using interaction surface templates. PMID:31917413
Importance of Fluctuating Amino Acid Residues in Folding and Binding of Proteins. PMID:31908743
LLPSDB: a database of proteins undergoing liquid-liquid phase separation in vitro. PMID:31906602
The dark side of Alzheimer's disease: unstructured biology of proteins from the amyloid cascade signaling pathway. PMID:31894361
An intrinsically disordered proteins community for ELIXIR. PMID:31824649
Maximum Entropy Optimized Force Field for Intrinsically Disordered Proteins. PMID:31756104
Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins. PMID:31724233
ELM-the eukaryotic linear motif resource in 2020. PMID:31680160
Identification and Analysis of Long Repeats of Proteins at the Domain Level. PMID:31649924
DISOselect: Disorder predictor selection at the protein level. PMID:31642118
New insight into the mechanisms protecting bacteria during desiccation. PMID:31559453
Polymer effects modulate binding affinities in disordered proteins. PMID:31488718
An interplay of structure and intrinsic disorder in the functionality of peptidylarginine deiminases, a family of key autoimmunity-related enzymes. PMID:31342121
Disorder Atlas: Web-based software for the proteome-based interpretation of intrinsic disorder predictions. PMID:31326853
Systematic identification of recognition motifs for the hub protein LC8. PMID:31266884
Codon selection reduces GC content bias in nucleic acids encoding for intrinsically disordered proteins. PMID:31175370
The Structural and Functional Diversity of Intrinsically Disordered Regions in Transmembrane Proteins. PMID:31139867
INGA 2.0: improving protein function prediction for the dark proteome. PMID:31073595
Intrinsically Disordered Linkers Impart Processivity on Enzymes by Spatial Confinement of Binding Domains. PMID:31032817
Computational Prediction of MoRFs, Short Disorder-to-order Transitioning Protein Binding Regions. PMID:31007871
Quality and bias of protein disorder predictors. PMID:30914747
On the Need to Develop Guidelines for Characterizing and Reporting Intrinsic Disorder in Proteins. PMID:30793871
Transient Secondary Structures as General Target-Binding Motifs in Intrinsically Disordered Proteins. PMID:30445805
Decision-Tree Based Meta-Strategy Improved Accuracy of Disorder Prediction and Identified Novel Disordered Residues Inside Binding Motifs. PMID:30301243
Zn2+-binding in the glutamate-rich region of the intrinsically disordered protein prothymosin-alpha. PMID:30187212
IDP⁻CRF: Intrinsically Disordered Protein/Region Identification Based on Conditional Random Fields. PMID:30135358
Protein Sequences Recapitulate Genetic Code Evolution. PMID:30002789
IDPpi: Protein-Protein Interaction Analyses of Human Intrinsically Disordered Proteins. PMID:30002402
Thermodynamics of Conformational Transitions in a Disordered Protein Backbone Model. PMID:29925017
IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding. PMID:29860432
Exploring intrinsically disordered proteins in Chlamydomonas reinhardtii. PMID:29717210
Pi-Pi contacts are an overlooked protein feature relevant to phase separation. PMID:29424691
Functional Analysis of Human Hub Proteins and Their Interactors Involved in the Intrinsic Disorder-Enriched Interactions. PMID:29257115
Platelet phosphorylated TDP-43: an exploratory study for a peripheral surrogate biomarker development for Alzheimer's disease. PMID:29134122
Random protein sequences can form defined secondary structures and are well-tolerated in vivo. PMID:29133927
The PROSECCO server for chemical shift predictions in ordered and disordered proteins. PMID:29119515
Prediction of protein disorder based on IUPred. PMID:29076577
MFIB: a repository of protein complexes with mutual folding induced by binding. PMID:29036655
Hotspots of age-related protein degradation: the importance of neighboring residues for the formation of non-disulfide crosslinks derived from cysteine. PMID:28592682
How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe. PMID:28232901
Time, space, and disorder in the expanding proteome universe. PMID:28145059 -
DisProt: intrinsic protein disorder annotation in 2020
PubMed citations: 78.
78 articles citing: DisProt: intrinsic protein disorder annotation in 2020
Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions. PMID:35883444
IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures. PMID:35883018
Discovering molecular features of intrinsically disordered regions by using evolution for contrastive learning. PMID:35767567
Complementarity of the residue-level protein function and structure predictions in human proteins. PMID:35615015
FuzDrop on AlphaFold: visualizing the sequence-dependent propensity of liquid-liquid phase separation and aggregation of proteins. PMID:35610022
AlphaFold2: A Role for Disordered Protein/Region Prediction? PMID:35562983
Predicting Protein Conformational Disorder and Disordered Binding Sites. PMID:35507260
Deep learning in prediction of intrinsic disorder in proteins. PMID:35356546
MoRF-FUNCpred: Molecular Recognition Feature Function Prediction Based on Multi-Label Learning and Ensemble Learning. PMID:35350759
Secretory quality control constrains functional selection-associated protein structure innovation. PMID:35338247
Identifying Intrinsically Disordered Protein Regions through a Deep Neural Network with Three Novel Sequence Features. PMID:35330096
Characterization of intrinsically disordered regions in proteins informed by human genetic diversity. PMID:35275927
Databases for intrinsically disordered proteins. PMID:35102880
Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins. PMID:35054576
Molecular Determinants of Selectivity in Disordered Complexes May Shed Light on Specificity in Protein Condensates. PMID:35053240
A Thermodynamic Atlas of Proteomes Reveals Energetic Innovation across the Tree of Life. PMID:35038744
Current status of PTMs structural databases: applications, limitations and prospects. PMID:35020020
ECO: the Evidence and Conclusion Ontology, an update for 2022. PMID:34986598
The dynamic basis of structural order in proteins. PMID:34981860
DisProt in 2022: improved quality and accessibility of protein intrinsic disorder annotation. PMID:34850135
Intergenic ORFs as elementary structural modules of de novo gene birth and protein evolution. PMID:34810219
Identification of ligand binding sites in intrinsically disordered proteins with a differential binding score. PMID:34799573
FuzDB: a new phase in understanding fuzzy interactions. PMID:34791357
DeepREx-WS: A web server for characterising protein-solvent interaction starting from sequence. PMID:34765094
The Eukaryotic Linear Motif resource: 2022 release. PMID:34718738
Beta turn propensity and a model polymer scaling exponent identify intrinsically disordered phase-separating proteins. PMID:34710373
Advanced Sampling Methods for Multiscale Simulation of Disordered Proteins and Dynamic Interactions. PMID:34680048
In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model. PMID:34638925
ProNAB: database for binding affinities of protein-nucleic acid complexes and their mutants. PMID:34606614
Selective 1 Hα NMR Methods Reveal Functionally Relevant Proline cis/trans Isomers in Intrinsically Disordered Proteins: Characterization of Minor Forms, Effects of Phosphorylation, and Occurrence in Proteome. PMID:34585830
Cryptic amyloidogenic regions in intrinsically disordered proteins: Function and disease association. PMID:34527192
Metapredict: a fast, accurate, and easy-to-use predictor of consensus disorder and structure. PMID:34480923
On the roles of intrinsically disordered proteins and regions in cell communication and signaling. PMID:34461937
Seeing Keratinocyte Proteins through the Looking Glass of Intrinsic Disorder. PMID:34360678
flDPnn: Accurate intrinsic disorder prediction with putative propensities of disorder functions. PMID:34290238
Evolutionary conservation of intrinsically unstructured regions in slit-diaphragm proteins. PMID:34288970
The diversity of molecular interactions involving intrinsically disordered proteins: A molecular modeling perspective. PMID:34285781
Updated SARS-CoV-2 single nucleotide variants and mortality association. PMID:34245452
FG nucleoporins feature unique patterns that distinguish them from other IDPs. PMID:34237287
Pretraining model for biological sequence data. PMID:34050350
IUPred3: prediction of protein disorder enhanced with unambiguous experimental annotation and visualization of evolutionary conservation. PMID:34048569
QUARTERplus: Accurate disorder predictions integrated with interpretable residue-level quality assessment scores. PMID:34025946
Homopeptide and homocodon levels across fungi are coupled to GC/AT-bias and intrinsic disorder, with unique behaviours for some amino acids. PMID:33976321
SeRenDIP-CE: Sequence-based Interface Prediction for Conformational Epitopes. PMID:33974039
Variants in GCNA, X-linked germ-cell genome integrity gene, identified in men with primary spermatogenic failure. PMID:33963445
Searching for universal model of amyloid signaling motifs using probabilistic context-free grammars. PMID:33926372
APICURON: a database to credit and acknowledge the work of biocurators. PMID:33882120
A community effort to bring structure to disorder. PMID:33875888
Critical assessment of protein intrinsic disorder prediction. PMID:33875885
Tuning intrinsic disorder predictors for virus proteins. PMID:33614158
Computational Screening of Phase-separating Proteins. PMID:33610793
The human O-GlcNAcome database and meta-analysis. PMID:33479245
The complexity of protein interactions unravelled from structural disorder. PMID:33417598
Computational design of SARS-CoV-2 spike glycoproteins to increase immunogenicity by T cell epitope engineering. PMID:33398234
APOD: accurate sequence-based predictor of disordered flexible linkers. PMID:33381830
Assessing the low complexity of protein sequences via the low complexity triangle. PMID:33378336
The Role of Protein Disorder in Nuclear Transport and in Its Subversion by Viruses. PMID:33321790
Widespread occurrence of the droplet state of proteins in the human proteome. PMID:33318217
PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins. PMID:33305318
NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences. PMID:33304713
Comparative Assessment of Intrinsic Disorder Predictions with a Focus on Protein and Nucleic Acid-Binding Proteins. PMID:33291838
Liquid-Liquid Phase Separation by Intrinsically Disordered Protein Regions of Viruses: Roles in Viral Life Cycle and Control of Virus-Host Interactions. PMID:33260713
MobiDB: intrinsically disordered proteins in 2021. PMID:33237329
The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes. PMID:33119751
DescribePROT: database of amino acid-level protein structure and function predictions. PMID:33119734
Susceptibility of Protein Methionine Oxidation in Response to Hydrogen Peroxide Treatment-Ex Vivo Versus In Vitro: A Computational Insight. PMID:33066324
A Novel Strategy for the Development of Vaccines for SARS-CoV-2 (COVID-19) and Other Viruses Using AI and Viral Shell Disorder. PMID:33006287
IDPology of the living cell: intrinsic disorder in the subcellular compartments of the human cell. PMID:32997198
Design principles of gene evolution for niche adaptation through changes in protein-protein interaction networks. PMID:32973219
Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins. PMID:32867340
Variable absorption of mutational trends by prion-forming domains during Saccharomycetes evolution. PMID:32844065
DispHred: A Server to Predict pH-Dependent Order-Disorder Transitions in Intrinsically Disordered Proteins. PMID:32823616
Moonlighting Proteins in the Fuzzy Logic of Cellular Metabolism. PMID:32751110
Experimentally Determined Long Intrinsically Disordered Protein Regions Are Now Abundant in the Protein Data Bank. PMID:32599863
The Future of Protein Secondary Structure Prediction Was Invented by Oleg Ptitsyn. PMID:32560074
Genomic Analysis of Intrinsically Disordered Proteins in the Genus Camelus. PMID:32503351
PlaToLoCo: the first web meta-server for visualization and annotation of low complexity regions in proteins. PMID:32421769
Thermodynamic and Evolutionary Coupling between the Native and Amyloid State of Globular Proteins. PMID:32294448 -
Corrigendum: DisProt 7.0: a major update of the database of disordered proteins
PubMed citations: 28.
28 articles citing: Corrigendum: DisProt 7.0: a major update of the database of disordered proteins
Matrin3: Disorder and ALS Pathogenesis. PMID:35083279
Mutations of Intrinsically Disordered Protein Regions Can Drive Cancer but Lack Therapeutic Strategies. PMID:33806614
MobiDB: intrinsically disordered proteins in 2021. PMID:33237329
The E3 ubiquitin-protein ligase MDM2 is a novel interactor of the von Hippel-Lindau tumor suppressor. PMID:32985545
Exploring Protein Intrinsic Disorder with MobiDB. PMID:32696355
Analyzing the Sequences of Intrinsically Disordered Regions with CIDER and localCIDER. PMID:32696354
Experimentally Determined Long Intrinsically Disordered Protein Regions Are Now Abundant in the Protein Data Bank. PMID:32599863
Mutually exclusive locales for N-linked glycans and disorder in human glycoproteins. PMID:32269229
Characterization of an Extensive Interface on Vitronectin for Binding to Plasminogen Activator Inhibitor-1: Adoption of Structure in an Intrinsically Disordered Region. PMID:31793295
DisProt: intrinsic protein disorder annotation in 2020. PMID:31713636
Structural Basis of the Subcellular Topology Landscape of Escherichia coli. PMID:31404336
Identification of Intrinsically Disordered Proteins and Regions by Length-Dependent Predictors Based on Conditional Random Fields. PMID:31307006
Intrinsically disordered domains: Sequence ➔ disorder ➔ function relationships. PMID:31299122
Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins. PMID:30841624
Accelerating annotation of articles via automated approaches: evaluation of the neXtA5 curation-support tool by neXtProt. PMID:30576492
Where differences resemble: sequence-feature analysis in curated databases of intrinsically disordered proteins. PMID:30576490
Robustness by intrinsically disordered C-termini and translational readthrough. PMID:30247639
The OB-fold proteins of the Trypanosoma brucei editosome execute RNA-chaperone activity. PMID:30060205
DIBS: a repository of disordered binding sites mediating interactions with ordered proteins. PMID:29385418
MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins. PMID:29136219
To be disordered or not to be disordered: is that still a question for proteins in the cell? PMID:28612216
Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions. PMID:28589442
Structural models of the different trimers present in the core of phycobilisomes from Gracilaria chilensis based on crystal structures and sequences. PMID:28542288
Pipeline to Identify Hydroxyproline-Rich Glycoproteins. PMID:28446635
Novel interactions of the von Hippel-Lindau (pVHL) tumor suppressor with the CDKN1 family of cell cycle inhibitors. PMID:28425505
Modeling disordered protein interactions from biophysical principles. PMID:28394890
DisBind: A database of classified functional binding sites in disordered and structured regions of intrinsically disordered proteins. PMID:28381244
Conformational diversity analysis reveals three functional mechanisms in proteins. PMID:28192432 - http://bioinformatics.oxfordjournals.org/cgi/content/abstract/21/1/137
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version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
intrinsically disordered proteins
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version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
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version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
protein structure
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version: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
metasource: re3data.org
version: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
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cell biology
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intrinsically disordered proteins idps
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protein disordered structure
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disease
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
intrinsically disordered proteins
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
protein
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
protein structure
metasource: Fairsharing.orgversion: FAIRsharing.org: DisProt; Database of Protein Disorder; DOI: https://doi.org/10.25504/FAIRsharing.dt9z89; Last edited: March 9, 2021, 11:47 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
metasource: re3data.org
version: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
structure databases
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
cell biology
metasource: re3data.orgversion: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
intrinsically disordered proteins idps
metasource: re3data.orgversion: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
molecular biology
metasource: re3data.orgversion: re3data.org: DisProt; editing status 2017-08-24; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3NG75 last accessed: 2022-11-04
protein disordered structure
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:24:59.960592
disease intrinsically disordered proteins protein protein structure structure cell biology intrinsically disordered proteins idps molecular biology protein disordered structure
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