CPLA 1.0: an integrated database of protein lysine acetylation - Wikidata - awgldk - TriplyDB

CPLA 1.0: an integrated database of protein lysine acetylation

CPLA 1.0: an integrated database of protein lysine acetylation

http://www.wikidata.org/entity/Q24608175

about

PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse Global analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice (Oryza sativa)Genome-wide analysis of functional sirtuin chromatin targets in yeast.Influence of the sequence environment and properties of neighboring amino acids on amino-acetylation: relevance for structure-function analysis.Accurate in silico identification of species-specific acetylation sites by integrating protein sequence-derived and functional features.Position-specific analysis and prediction for protein lysine acetylation based on multiple features.Chemoproteomic profiling of lysine acetyltransferases highlights an expanded landscape of catalytic acetylation Proteomics analysis of human obesity reveals the epigenetic factor HDAC4 as a potential target for obesity Protein databases on the internet.Improved Species-Specific Lysine Acetylation Site Prediction Based on a Large Variety of Features Set.Mechanisms and Dynamics of Protein Acetylation in Mitochondria.Frequent mutations in acetylation and ubiquitination sites suggest novel driver mechanisms of cancer.SNObase, a database for S-nitrosation modification.CPLM: a database of protein lysine modifications.Post-translational modification: nature's escape from genetic imprisonment and the basis for dynamic information encoding.Rapid development of proteomics in China: from the perspective of the Human Liver Proteome Project and technology development.Posttranslational modifications of lysine and evolving role in heart pathologies-recent developments.First Comprehensive Proteome Analyses of Lysine Acetylation and Succinylation in Seedling Leaves of Brachypodium distachyon L.Protein databases on the internet.Global Proteome Analysis Links Lysine Acetylation to Diverse Functions in Oryza Sativa.Success: evolutionary and structural properties of amino acids prove effective for succinylation site prediction.Sirtuin 1 and 7 mediate resveratrol-induced recovery from hyper-anxiety in high-fructose-fed prediabetic rats.Improving succinylation prediction accuracy by incorporating the secondary structure via helix, strand and coil, and evolutionary information from profile bigrams.

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P2860

CPLA 1.0: an integrated database of protein lysine acetylation

http://www.wikidata.org/entity/Q24608175

description

2011 nî lūn-bûn

@nan

2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

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2011年論文

@zh-hk

2011年論文

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2011年論文

@zh-tw

2011年论文

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name

CPLA 1.0: an integrated database of protein lysine acetylation

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CPLA 1.0: an integrated database of protein lysine acetylation

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CPLA 1.0: an integrated database of protein lysine acetylation

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CPLA 1.0: an integrated database of protein lysine acetylation

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CPLA 1.0: an integrated database of protein lysine acetylation

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CPLA 1.0: an integrated database of protein lysine acetylation

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CPLA 1.0: an integrated database of protein lysine acetylation

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CPLA 1.0: an integrated database of protein lysine acetylation

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Nucleic Acids Research

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CPLA 1.0: an integrated database of protein lysine acetylation

@en

P2093

Jian Ren

http://www.w3.org/2001/XMLSchema#string

Jun Cao

http://www.w3.org/2001/XMLSchema#string

Longping Wen

http://www.w3.org/2001/XMLSchema#string

Xiangjiao Yang

http://www.w3.org/2001/XMLSchema#string

Xinjiao Gao

http://www.w3.org/2001/XMLSchema#string

Xuebiao Yao

http://www.w3.org/2001/XMLSchema#string

Yanhong Zhou

http://www.w3.org/2001/XMLSchema#string

Yu Xue

http://www.w3.org/2001/XMLSchema#string

Zexian Liu

http://www.w3.org/2001/XMLSchema#string

P2860

Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase

Regulation of cellular metabolism by protein lysine acetylation

Stress-dependent regulation of FOXO transcription factors by the SIRT1 deacetylase

Stimulation of GCMa transcriptional activity by cyclic AMP/protein kinase A signaling is attributed to CBP-mediated acetylation of GCMa.

BioGRID: a general repository for interaction datasets

ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS

STRING 8--a global view on proteins and their functional interactions in 630 organisms

MINT: the Molecular INTeraction database

The diversity of acetylated proteins.

Lysine acetylation targets protein complexes and co-regulates major cellular functions

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D1029-34

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scholarly article

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1618981

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10.1093/NAR/GKQ939

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P433

Database issue

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39

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2011-01-01T00:00:00Z

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47717628

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21059677

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3013790

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