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Evolution of SH2 domains and phosphotyrosine signalling networks

Evolution of SH2 domains and phosphotyrosine signalling networks

http://www.wikidata.org/entity/Q24620411

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SRC Homology 2 Domain Binding Sites in Insulin, IGF-1 and FGF receptor mediated signaling networks reveal an extensive potential interactome The role of small adaptor proteins in the control of oncogenic signalingr driven by tyrosine kinases in human cancer Short linear motifs - ex nihilo evolution of protein regulation SRC-family tyrosine kinases in oogenesis, oocyte maturation and fertilization: an evolutionary perspective Neuroblastoma tyrosine kinase signaling networks involve FYN and LYN in endosomes and lipid rafts Src homology 2 domain containing protein 5 (SH2D5) binds the breakpoint cluster region protein, BCR, and regulates levels of Rac1-GTP 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.Mercury alters B-cell protein phosphorylation profiles.Metazoan-like signaling in a unicellular receptor tyrosine kinase.Contribution of Crk adaptor proteins to host cell and bacteria interactions.Genome-wide transcriptional profiling of skin and dorsal root ganglia after ultraviolet-B-induced inflammation.SH2 Ligand-Like Effects of Second Cytosolic Domain of Na/K-ATPase α1 Subunit on Src Kinase.The Physarum polycephalum Genome Reveals Extensive Use of Prokaryotic Two-Component and Metazoan-Type Tyrosine Kinase Signaling.SH2 Domains Serve as Lipid-Binding Modules for pTyr-Signaling Proteins Identifying Kinase Substrates via a Heavy ATP Kinase Assay and Quantitative Mass Spectrometry.Understanding and applying tyrosine biochemical diversity.Evolution and tinkering: what do a protein kinase, a transcriptional regulator and chromosome segregation/cell division proteins have in common?A novel SH2 recognition mechanism recruits Spt6 to the doubly phosphorylated RNA polymerase II linker at sites of transcription.Introduction: History of SH2 Domains and Their Applications.SHIP2: Structure, Function and Inhibition.Regulation of Src and Csk nonreceptor tyrosine kinases in the filasterean Ministeria vibrans Diversity in peptide recognition by the SH2 domain of SH2B1.Classification and Lineage Tracing of SH2 Domains Throughout Eukaryotes.Hidden Markov Models for Protein Domain Homology Identification and Analysis.Src signaling in a low-complexity unicellular kinome.Phosphotyrosine signalling and the origin of animal multicellularity.

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Evolution of SH2 domains and phosphotyrosine signalling networks

http://www.wikidata.org/entity/Q24620411

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2012 nî lūn-bûn

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2012 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2012 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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Evolution of SH2 domains and phosphotyrosine signalling networks

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Evolution of SH2 domains and phosphotyrosine signalling networks

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Evolution of SH2 domains and phosphotyrosine signalling networks

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Evolution of SH2 domains and phosphotyrosine signalling networks

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Evolution of SH2 domains and phosphotyrosine signalling networks

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Philosophical Transactions of the Royal Society B

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Evolution of SH2 domains and phosphotyrosine signalling networks

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Piers D Nash

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P2860

Gene duplication: the genomic trade in spare parts

The dictyostelium kinome--analysis of the protein kinases from a simple model organism.

Protein family expansions and biological complexity

Creation and disruption of protein features by alternative splicing -- a novel mechanism to modulate function.

The genome of the choanoflagellate Monosiga brevicollis and the origin of metazoans

Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7.

The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and export

Structure of a novel phosphotyrosine-binding domain in Hakai that targets E-cadherin

Loops govern SH2 domain specificity by controlling access to binding pockets

Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.

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10.1098/RSTB.2012.0107

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