Intrinsically Disordered proteins with Extensive Annotations and Literature
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Intrinsically Disordered proteins with Extensive Annotations and Literature
metasource: Fairsharing.org
version: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
IDEAL
metasource: Fairsharing.org
version: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 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: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
ideal
metasource: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
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Intrinsically Disordered proteins with Extensive Annotations and Literature
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
IDEAL
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 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: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
ideal
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:36:09.791462
Names
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Intrinsically Disordered proteins with Extensive Annotations and Literature
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
IDEAL
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 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: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
ideal
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:36:09.791462
IDEAL (Intrinsically Disordered proteins with Extensive Annotations and Literature) is a collection of experimentally-verified intrinsically disordered proteins (IDPs) that cannot adopt stable globular structures under physiological conditions. IDEAL contains manually curated annotations on IDPs in locations, structures, and functional sites such as protein binding regions and post-translational modification sites together with references and structural domain assignments.
Description
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IDEAL (Intrinsically Disordered proteins with Extensive Annotations and Literature) is a collection of experimentally-verified intrinsically disordered proteins (IDPs) that cannot adopt stable globular structures under physiological conditions. IDEAL contains manually curated annotations on IDPs in locations, structures, and functional sites such as protein binding regions and post-translational modification sites together with references and structural domain assignments.
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Intrinsically Disordered proteins with Extensive Annotations and Literature
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
Collection of experimentally verified intrinsically disordered proteins (IDPs) or intrinsically disordered regions (IDRs). Manually curated annotations on IDPs in locations, structures, and functional sites such as protein binding regions and posttranslational modification sites.
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:36:09.791462
Webpage:
http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/Webpage
More detailed information about this field from each metasource.
http://www.ideal.force.cs.is.nagoya-u.ac.jp/IDEAL/
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 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: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
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: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Licence URL
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https://creativecommons.org/licenses/by/4.0/
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
Publications:
Publications
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IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature
PMID: 22067451
metasource: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners
PMID: 24178034
metasource: Fairsharing.org
version: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
http://dx.doi.org/10.1093/nar/gkt1010
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.
IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature
PMID: 22067451
metasource: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners
PMID: 24178034
metasource: Fairsharing.org
version: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
http://dx.doi.org/10.1093/nar/gkt1010
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
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IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature
PubMed citations: 48.
48 articles citing: IDEAL: Intrinsically Disordered proteins with Extensive Annotations and Literature
IDPsBind: a repository of binding sites for intrinsically disordered proteins complexes with known 3D structures. PMID:35883018
Uses and Abuses of the Atomic Displacement Parameters in Structural Biology. PMID:35507268
Origin of Increased Solvent Accessibility of Peptide Bonds in Mutual Synergetic Folding Proteins. PMID:34948202
Measuring and interpreting pervasive heterogeneity, poikilosis. PMID:34377957
NeProc predicts binding segments in intrinsically disordered regions without learning binding region sequences. PMID:33304713
Presence of intrinsically disordered proteins can inhibit the nucleation phase of amyloid fibril formation of Aβ(1-42) in amino acid sequence independent manner. PMID:32703978
Dynamic conformational flexibility and molecular interactions of intrinsically disordered proteins. PMID:32020911
Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins. PMID:31724233
Sequence and Structure Properties Uncover the Natural Classification of Protein Complexes Formed by Intrinsically Disordered Proteins via Mutual Synergistic Folding. PMID:31683980
Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins. PMID:30841624
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
Large-Scale Analyses of Site-Specific Evolutionary Rates across Eukaryote Proteomes Reveal Confounding Interactions between Intrinsic Disorder, Secondary Structure, and Functional Domains. PMID:30441862
Decision-Tree Based Meta-Strategy Improved Accuracy of Disorder Prediction and Identified Novel Disordered Residues Inside Binding Motifs. PMID:30301243
Using 1 HN amide temperature coefficients to define intrinsically disordered regions: An alternative NMR method. PMID:30098073
Discerning evolutionary trends in post-translational modification and the effect of intrinsic disorder: Analysis of methylation, acetylation and ubiquitination sites in human proteins. PMID:30096183
DIBS: a repository of disordered binding sites mediating interactions with ordered proteins. PMID:29385418
Common TFIIH recruitment mechanism in global genome and transcription-coupled repair subpathways. PMID:29069470
Salt-bridge networks within globular and disordered proteins: characterizing trends for designable interactions. PMID:28626846
Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions. PMID:28589442
DisBind: A database of classified functional binding sites in disordered and structured regions of intrinsically disordered proteins. PMID:28381244
Proteus: a random forest classifier to predict disorder-to-order transitioning binding regions in intrinsically disordered proteins. PMID:28365882
The relationship between relative solvent accessible surface area (rASA) and irregular structures in protean segments (ProSs). PMID:28250616
An optimized Npro-based method for the expression and purification of intrinsically disordered proteins for an NMR study. PMID:28232886
Assessment of virulence potential of uncharacterized Enterococcus faecalis strains using pan genomic approach - Identification of pathogen-specific and habitat-specific genes. PMID:27924951
DisProt 7.0: a major update of the database of disordered proteins. PMID:27899601
Large-scale analysis of intrinsic disorder flavors and associated functions in the protein sequence universe. PMID:27636733
Paralog-Specific Patterns of Structural Disorder and Phosphorylation in the Vertebrate SH3-SH2-Tyrosine Kinase Protein Family. PMID:27519537
Phylogenetic and Structural Analysis of the Pluripotency Factor Sex-Determining Region Y box2 Gene of Camelus dromedarius (cSox2). PMID:27486314
A collection of intrinsic disorder characterizations from eukaryotic proteomes. PMID:27326998
Multiple-Localization and Hub Proteins. PMID:27285823
Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics. PMID:27124275
Functional Diversification after Gene Duplication: Paralog Specific Regions of Structural Disorder and Phosphorylation in p53, p63, and p73. PMID:27003913
Statistical prediction of protein structural, localization and functional properties by the analysis of its fragment mass distributions after proteolytic cleavage. PMID:26924271
Bioinformatical parsing of folding-on-binding proteins reveals their compositional and evolutionary sequence design. PMID:26678310
DisPredict: A Predictor of Disordered Protein Using Optimized RBF Kernel. PMID:26517719
A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR. PMID:26184172
Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators. PMID:25988147
Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins. PMID:24594841
Modelling the yeast interactome. PMID:24589662
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
Assessment of protein disorder region predictions in CASP10. PMID:23946100
Analysis and consensus of currently available intrinsic protein disorder annotation sources in the MobiDB database. PMID:23815411
The challenge of increasing Pfam coverage of the human proteome. PMID:23603847
D²P²: database of disordered protein predictions. PMID:23203878
An assignment of intrinsically disordered regions of proteins based on NMR structures. PMID:23142703 -
IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners
PubMed citations: 47.
47 articles citing: IDEAL in 2014 illustrates interaction networks composed of intrinsically disordered proteins and their binding partners
Compositional Bias of Intrinsically Disordered Proteins and Regions and Their Predictions. PMID:35883444
Predicting Protein Conformational Disorder and Disordered Binding Sites. PMID:35507260
Deep learning in prediction of intrinsic disorder in proteins. PMID:35356546
Characterization of intrinsically disordered regions in proteins informed by human genetic diversity. PMID:35275927
Databases for intrinsically disordered proteins. PMID:35102880
LLPSDB v2.0: an updated database of proteins undergoing liquid-liquid phase separation in vitro. PMID:35025997
IUPred3: prediction of protein disorder enhanced with unambiguous experimental annotation and visualization of evolutionary conservation. PMID:34048569
Critical assessment of protein intrinsic disorder prediction. PMID:33875885
Mutations of Intrinsically Disordered Protein Regions Can Drive Cancer but Lack Therapeutic Strategies. PMID:33806614
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
A Suggestion of Converting Protein Intrinsic Disorder to Structural Entropy Using Shannon's Information Theory. PMID:33267305
MobiDB: intrinsically disordered proteins in 2021. PMID:33237329
Protein Databases Related to Liquid-Liquid Phase Separation. PMID:32947964
ODiNPred: comprehensive prediction of protein order and disorder. PMID:32901090
Presence of intrinsically disordered proteins can inhibit the nucleation phase of amyloid fibril formation of Aβ(1-42) in amino acid sequence independent manner. PMID:32703978
Exploring Protein Intrinsic Disorder with MobiDB. PMID:32696355
Experimentally Determined Long Intrinsically Disordered Protein Regions Are Now Abundant in the Protein Data Bank. PMID:32599863
Genomic Analysis of Intrinsically Disordered Proteins in the Genus Camelus. PMID:32503351
Nonstructural proteins NS7b and NS8 are likely to be phylogenetically associated with evolution of 2019-nCoV. PMID:32142938
LLPSDB: a database of proteins undergoing liquid-liquid phase separation in vitro. PMID:31906602
Protein kinases phosphorylate long disordered regions in intrinsically disordered proteins. PMID:31724233
DISOselect: Disorder predictor selection at the protein level. PMID:31642118
Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins. PMID:30841624
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
Troubleshooting Guide to Expressing Intrinsically Disordered Proteins for Use in NMR Experiments. PMID:30713842
Where differences resemble: sequence-feature analysis in curated databases of intrinsically disordered proteins. PMID:30576490
Using 1 HN amide temperature coefficients to define intrinsically disordered regions: An alternative NMR method. PMID:30098073
Combined treatment of human multiple myeloma cells with bortezomib and doxorubicin alters the interactome of 20S proteasomes. PMID:30009671
Deciphering RNA-Recognition Patterns of Intrinsically Disordered Proteins. PMID:29843482
MobiDB 3.0: more annotations for intrinsic disorder, conformational diversity and interactions in proteins. PMID:29136219
MFIB: a repository of protein complexes with mutual folding induced by binding. PMID:29036655
The relationship between relative solvent accessible surface area (rASA) and irregular structures in protean segments (ProSs). PMID:28250616
How disordered is my protein and what is its disorder for? A guide through the "dark side" of the protein universe. PMID:28232901
Quarterly intrinsic disorder digest (January-February-March, 2014). PMID:28232896
An optimized Npro-based method for the expression and purification of intrinsically disordered proteins for an NMR study. PMID:28232886
FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies. PMID:27794553
A collection of intrinsic disorder characterizations from eukaryotic proteomes. PMID:27326998
Multiple-Localization and Hub Proteins. PMID:27285823
There is Diversity in Disorder-"In all Chaos there is a Cosmos, in all Disorder a Secret Order". PMID:26904549
Bioinformatical parsing of folding-on-binding proteins reveals their compositional and evolutionary sequence design. PMID:26678310
DisPredict: A Predictor of Disordered Protein Using Optimized RBF Kernel. PMID:26517719
A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR. PMID:26184172
Wrecked regulation of intrinsically disordered proteins in diseases: pathogenicity of deregulated regulators. PMID:25988147
MobiDB 2.0: an improved database of intrinsically disordered and mobile proteins. PMID:25361972
Classification of intrinsically disordered regions and proteins. PMID:24773235 - http://dx.doi.org/10.1093/nar/gkt1010
Tags:
Tags
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intrinsically disordered proteins
metasource: Fairsharing.org
version: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
molecular interaction
metasource: Fairsharing.org
version: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
post-translational protein modification
metasource: Fairsharing.org
version: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
structure databases
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
protein structure
metasource: Nucleic Acid Research database catalogue
version: extracted_at: 2022-11-04T11:16:25.468657
protein modifications
metasource: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
protein disordered structure
metasource: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
protein folds and structural domains
metasource: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
proteins
metasource: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
protein binding sites
metasource: bio.tools
version: extracted_at: 2022-11-04T11:36:09.791462
Tags
More detailed information about this field from each metasource.
intrinsically disordered proteins
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
molecular interaction
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
post-translational protein modification
metasource: Fairsharing.orgversion: FAIRsharing.org: IDEAL; Intrinsically Disordered proteins with Extensive Annotations and Literature; DOI: https://doi.org/10.25504/FAIRsharing.h3y42f; Last edited: Jan. 30, 2020, 9:48 a.m.; Last accessed: Jan 03 2022 7:07 p.m.
structure databases
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
protein structure
metasource: Nucleic Acid Research database catalogueversion: extracted_at: 2022-11-04T11:16:25.468657
protein modifications
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:36:09.791462
protein disordered structure
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:36:09.791462
protein folds and structural domains
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:36:09.791462
proteins
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:36:09.791462
protein binding sites
metasource: bio.toolsversion: extracted_at: 2022-11-04T11:36:09.791462
intrinsically disordered proteins molecular interaction post-translational protein modification structure protein structure protein modifications protein disordered structure protein folds and structural domains proteins protein binding sites
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