Protein Lysine Modifications Database

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Protein Lysine Modifications Database

metasource: Fairsharing.org
version: None

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PLMD

metasource: Fairsharing.org
version: None

metasource: re3data.org
version: re3data.org: Protein Lysine Modification Database; editing status 2021-12-15; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3ZW3K last accessed: 2022-11-04

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Protein Lysine Modification Database

metasource: re3data.org
version: re3data.org: Protein Lysine Modification Database; editing status 2021-12-15; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3ZW3K last accessed: 2022-11-04

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Other names: PLMD, Protein Lysine Modification Database

The Protein Lysine Modifications Database (PLMD) is an online data resource specifically designed for protein lysine modifications (PLMs).

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Publications

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PLMD: An updated data resource of protein lysine modifications
PMID: 28529077

metasource: Fairsharing.org
version: None

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• PLMD: An updated data resource of protein lysine modifications PubMed citations: 60.

  60 articles citing: PLMD: An updated data resource of protein lysine modifications

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  On the Prediction of In Vitro Arginine Glycation of Short Peptides Using Artificial Neural Networks. PMID:35890916

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  Mini-review: Recent advances in post-translational modification site prediction based on deep learning. PMID:35860402

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  ProtTrans-Glutar: Incorporating Features From Pre-trained Transformer-Based Models for Predicting Glutarylation Sites. PMID:35711929

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  Systematic Characterization of Lysine Post-translational Modification Sites Using MUscADEL. PMID:35696083

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  Studying Acetylation of Aconitase Isozymes by Genetic Code Expansion. PMID:35402385

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  Proteome-Wide Identification and Functional Analysis of Lysine Crotonylation in Trichophyton rubrum Conidial and Mycelial Stages. PMID:35356433

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  Development of an experiment-split method for benchmarking the generalization of a PTM site predictor: Lysine methylome as an example. PMID:34879076

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  qPTMplants: an integrative database of quantitative post-translational modifications in plants. PMID:34718741

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  CPLM 4.0: an updated database with rich annotations for protein lysine modifications. PMID:34581824

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  PCV2 targets cGAS to inhibit type I interferon induction to promote other DNA virus infection. PMID:34543359

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  STALLION: a stacking-based ensemble learning framework for prokaryotic lysine acetylation site prediction. PMID:34532736

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  Preparation of Affinity Purified Antibodies against ε-Glutaryl-Lysine Residues in Proteins for Investigation of Glutarylated Proteins in Animal Tissues. PMID:34439834

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  Understanding and Exploiting Post-Translational Modifications for Plant Disease Resistance. PMID:34439788

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  Phosphoinositide Recognition Sites Are Blocked by Metabolite Attachment. PMID:34368138

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  MDCAN-Lys: A Model for Predicting Succinylation Sites Based on Multilane Dense Convolutional Attention Network. PMID:34208298

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  LSTMCNNsucc: A Bidirectional LSTM and CNN-Based Deep Learning Method for Predicting Lysine Succinylation Sites. PMID:34159204

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  Molecular dynamics shows complex interplay and long-range effects of post-translational modifications in yeast protein interactions. PMID:33979327

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  A Transfer Learning-Based Approach for Lysine Propionylation Prediction. PMID:33967828

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  predPhogly-Site: Predicting phosphoglycerylation sites by incorporating probabilistic sequence-coupling information into PseAAC and addressing data imbalance. PMID:33793659

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  Global Profiling of the Lysine Crotonylome in Different Pluripotent States. PMID:33746086

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  UbiNet 2.0: a verified, classified, annotated and updated database of E3 ubiquitin ligase-substrate interactions. PMID:33693667

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  Computational Analysis Indicates That PARP1 Acts as a Histone Deacetylases Interactor Sharing Common Lysine Residues for Acetylation, Ubiquitination, and SUMOylation in Alzheimer's and Parkinson's Disease. PMID:33681613

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  Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylated Proteins in Fusarium oxysporum. PMID:33643252

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  Recent Advances in Predicting Protein S-Nitrosylation Sites. PMID:33628788

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  Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in Candida albicans. PMID:33531408

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  Mal-Light: Enhancing Lysine Malonylation Sites Prediction Problem Using Evolutionary-based Features. PMID:33354488

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  iDPGK: characterization and identification of lysine phosphoglycerylation sites based on sequence-based features. PMID:33297954

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  PTMsnp: A Web Server for the Identification of Driver Mutations That Affect Protein Post-translational Modification. PMID:33240890

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  Ubiquitinome Profiling Reveals the Landscape of Ubiquitination Regulation in Rice Young Panicles. PMID:33147495

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  Incorporating Deep Learning With Word Embedding to Identify Plant Ubiquitylation Sites. PMID:33102477

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  Ubiquitomics: An Overview and Future. PMID:33080838

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  Computational methods and next-generation sequencing approaches to analyze epigenetics data: Profiling of methods and applications. PMID:32941995

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  Accurately Predicting Glutarylation Sites Using Sequential Bi-Peptide-Based Evolutionary Features. PMID:32878321

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  HybridSucc: A Hybrid-learning Architecture for General and Species-specific Succinylation Site Prediction. PMID:32861878

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  The PPAR Ω Pocket: Renewed Opportunities for Drug Development. PMID:32695150

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  Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions. PMID:32648529

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  Incorporating hybrid models into lysine malonylation sites prediction on mammalian and plant proteins. PMID:32601280

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  HDACi mediate UNG2 depletion, dysregulated genomic uracil and altered expression of oncoproteins and tumor suppressors in B- and T-cell lines. PMID:32264925

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  An Information Entropy-Based Approach for Computationally Identifying Histone Lysine Butyrylation. PMID:32117407

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  Acetylation of MORC2 by NAT10 regulates cell-cycle checkpoint control and resistance to DNA-damaging chemotherapy and radiotherapy in breast cancer. PMID:32112098

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  Mutational Functional Analysis of the Pseudorabies Virus Nuclear Egress Complex-Nucleocapsid Interaction. PMID:32051272

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  Proteome-Wide Identification of Lysine Propionylation in the Conidial and Mycelial Stages of Trichophyton rubrum. PMID:31798556

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  Cell-Wide Survey of Amide-Bonded Lysine Modifications by Using Deacetylase CobB. PMID:31798349

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  Characterization and Identification of Lysine Succinylation Sites based on Deep Learning Method. PMID:31700141

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  Analysis and prediction of human acetylation using a cascade classifier based on support vector machine. PMID:31208321

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  PRISMOID: a comprehensive 3D structure database for post-translational modifications and mutations with functional impact. PMID:31161204

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  DeepUbi: a deep learning framework for prediction of ubiquitination sites in proteins. PMID:30777029

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  GlyStruct: glycation prediction using structural properties of amino acid residues. PMID:30717650

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  Large-Scale Assessment of Bioinformatics Tools for Lysine Succinylation Sites. PMID:30696115

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  Integration of A Deep Learning Classifier with A Random Forest Approach for Predicting Malonylation Sites. PMID:30639696

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  Construction of a Quantitative Acetylomic Tissue Atlas in Rice (Oryza sativa L.). PMID:30388832

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  Large-scale comparative assessment of computational predictors for lysine post-translational modification sites. PMID:30285084

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  PTMD: A Database of Human Disease-associated Post-translational Modifications. PMID:30244175

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  Effects of Acetylation and Phosphorylation on Subunit Interactions in Three Large Eukaryotic Complexes. PMID:30181345

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  Characterizing Lysine Acetylation of Isocitrate Dehydrogenase in Escherichia coli. PMID:29733852

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  Epigenetic drug discovery: a success story for cofactor interference. PMID:29685973

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  Genetically Incorporating Two Distinct Post-translational Modifications into One Protein Simultaneously. PMID:29301074

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  Glypre: In Silico Prediction of Protein Glycation Sites by Fusing Multiple Features and Support Vector Machine. PMID:29099805

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  Database Resources of the BIG Data Center in 2018. PMID:29036542

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  Biochemical Characterization of the Lysine Acetylation of Tyrosyl-tRNA Synthetase in Escherichia coli. PMID:28741290

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Tags

More detailed information about this field from each metasource. ×

post-translational protein modification

metasource: Fairsharing.org
version: None

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protein modification

metasource: Fairsharing.org
version: None

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protein lysine modifications

metasource: re3data.org
version: re3data.org: Protein Lysine Modification Database; editing status 2021-12-15; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3ZW3K last accessed: 2022-11-04

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zebrafish

metasource: re3data.org
version: re3data.org: Protein Lysine Modification Database; editing status 2021-12-15; re3data.org - Registry of Research Data Repositories. http://doi.org/10.17616/R3ZW3K last accessed: 2022-11-04

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post-translational protein modification protein modification protein lysine modifications zebrafish