PHOSIDA 2011: the posttranslational modification database - Wikidata - wikimedia - TriplyDB

PHOSIDA 2011: the posttranslational modification database

PHOSIDA 2011: the posttranslational modification database

http://www.wikidata.org/entity/Q24611418

about

Classification of intrinsically disordered regions and proteins Phosphorylation at intrinsically disordered regions of PAM2 motif-containing proteins modulates their interactions with PABPC1 and influences mRNA fate PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse Mapping the SUMOylated landscape A perspective on proteomics in cell biology Web resources for mass spectrometry-based proteomics Multidimensional proteomics for cell biology Circumventing embryonic lethality with Lcmt1 deficiency: generation of hypomorphic Lcmt1 mice with reduced protein phosphatase 2A methyltransferase expression and defects in insulin signaling The Functional Significance of Posttranslational Modifications on Polo-Like Kinase 1 Revealed by Chemical Genetic Complementation GTSE1 is a microtubule plus-end tracking protein that regulates EB1-dependent cell migration The CDK9 Tail Determines the Reaction Pathway of Positive Transcription Elongation Factor b Inactivation of mitochondrial aspartate aminotransferase contributes to the respiratory deficit of yeast frataxin-deficient cells.Tale of a multifaceted co-activator, hADA3: from embryogenesis to cancer and beyond Adapting extracellular matrix proteomics for clinical studies on cardiac remodeling post-myocardial infarction Proteomic discovery of host kinase signaling in bacterial infections PhosphoSitePlus, 2014: mutations, PTMs and recalibrations The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination The extracellular signal-regulated kinase 3 (mitogen-activated protein kinase 6 [MAPK6])-MAPK-activated protein kinase 5 signaling complex regulates septin function and dendrite morphology Cancer missense mutations alter binding properties of proteins and their interaction networks The roles of post-translational modifications in the context of protein interaction networks The acquisition of novel N-glycosylation sites in conserved proteins during human evolution Fin whale MDH-1 and MPI allozyme variation is not reflected in the corresponding DNA sequences RNA Polymerase II C-Terminal Domain: Tethering Transcription to Transcript and Template Paralog-Specific Patterns of Structural Disorder and Phosphorylation in the Vertebrate SH3-SH2-Tyrosine Kinase Protein Family.The next level of complexity: crosstalk of posttranslational modifications.Incorporating post-translational modifications and unnatural amino acids into high-throughput modeling of protein structures.What's that gene (or protein)? Online resources for exploring functions of genes, transcripts, and proteins.Navigating the multilayered organization of eukaryotic signaling: a new trend in data integration.Survey of phosphorylation near drug binding sites in the Protein Data Bank (PDB) and their effects.Cross-Species PTM Mapping from Phosphoproteomic Data.An unbiased proteomic screen reveals caspase cleavage is positively and negatively regulated by substrate phosphorylation Transgenic tobacco overexpressing Brassica juncea HMG-CoA synthase 1 shows increased plant growth, pod size and seed yield.Polo-like kinase-dependent phosphorylation of the synaptonemal complex protein SYP-4 regulates double-strand break formation through a negative feedback loop.Mycobacterium tuberculosis supports protein tyrosine phosphorylation A novel regulatory locus of phosphorylation in the C terminus of the potassium chloride cotransporter KCC2 that interferes with N-ethylmaleimide or staurosporine-mediated activation.Effects of IL-6 on pyruvate dehydrogenase regulation in mouse skeletal muscle Accurate in silico identification of species-specific acetylation sites by integrating protein sequence-derived and functional features.Interplay of DNA damage and cell cycle signaling at the level of human replication protein A Structure and regulatory interactions of the cytoplasmic terminal domains of serotonin transporter.The application of selective reaction monitoring confirms dysregulation of glycolysis in a preclinical model of schizophrenia.

P2860

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P2860

PHOSIDA 2011: the posttranslational modification database

http://www.wikidata.org/entity/Q24611418

description

2011 nî lūn-bûn

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2011 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հունվարին հրատարակված գիտական հոդված

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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

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2011年論文

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2011年論文

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2011年论文

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name

PHOSIDA 2011: the posttranslational modification database

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PHOSIDA 2011: the posttranslational modification database

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PHOSIDA 2011: the posttranslational modification database

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type

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PHOSIDA 2011: the posttranslational modification database

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PHOSIDA 2011: the posttranslational modification database

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PHOSIDA 2011: the posttranslational modification database

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PHOSIDA 2011: the posttranslational modification database

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PHOSIDA 2011: the posttranslational modification database

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PHOSIDA 2011: the posttranslational modification database

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P3181

P356

P1433

Nucleic Acids Research

P1476

PHOSIDA 2011: the posttranslational modification database

@en

P2093

Florian Gnad

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

Jeremy Gunawardena

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

Matthias Mann

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

P2860

Gene ontology: tool for the unification of biology

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis

Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif

Ensembl's 10th year

Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs

dbPTM: an information repository of protein post-translational modification

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

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

Sequence and structure-based prediction of eukaryotic protein phosphorylation sites

Assembly of cell regulatory systems through protein interaction domains

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D253-60

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scholarly article

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235402

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10.1093/NAR/GKQ1159

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P433

Database issue

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P478

39

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2011-01-01T00:00:00Z

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47809051

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21081558

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3013726

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