Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains. - Wikidata - wikimedia - TriplyDB

Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains.

Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains.

http://www.wikidata.org/entity/Q33226743

about

Proteoglycan form and function: A comprehensive nomenclature of proteoglycans Enhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactome Simultaneous Binding of Two Peptidyl Ligands by a Src Homology 2 Domain Diverse Levels of Sequence Selectivity and Catalytic Efficiency of Protein-Tyrosine Phosphatases An investigation of hierachical protein recruitment to the inhibitory platelet receptor, G6B-b SHP-1 and SHP-2 in T cells: two phosphatases functioning at many levels Completion of proteomic data sets by Kd measurement using cell-free synthesis of site-specifically labeled proteins.Sequence specificity of SHP-1 and SHP-2 Src homology 2 domains. Critical roles of residues beyond the pY+3 position.Defining SH2 domain and PTP specificity by screening combinatorial peptide libraries.Reverse interactomics: decoding protein-protein interactions with combinatorial peptide libraries.Synthesis and screening of a cyclic peptide library: discovery of small-molecule ligands against human prolactin receptor A combinatorial H4 tail library for exploring the histone code.High-throughput sequencing of peptoids and peptide-peptoid hybrids by partial edman degradation and mass spectrometry.On-bead screening of combinatorial libraries: reduction of nonspecific binding by decreasing surface ligand density.Robust production of a peptide library using methodological synchronization The role of Src homology 2 containing protein tyrosine phosphatase 2 in vascular smooth muscle cell migration and proliferation.Determination of the substrate specificity of protein-tyrosine phosphatase TULA-2 and identification of Syk as a TULA-2 substrate.Human-specific evolution and adaptation led to major qualitative differences in the variable receptors of human and chimpanzee natural killer cells HDAC6 and Ubp-M BUZ domains recognize specific C-terminal sequences of proteins.Distinct ligand specificity of the Tiam1 and Tiam2 PDZ domains Substrate specificity of protein tyrosine phosphatases 1B, RPTPα, SHP-1, and SHP-2.In vivo regulation of the allergic response by the IL-4 receptor alpha chain immunoreceptor tyrosine-based inhibitory motif Diverse driving forces underlie the invariant occurrence of the T42A, E139D, I282V and T468M SHP2 amino acid substitutions causing Noonan and LEOPARD syndromes Determination of hemin-binding characteristics of proteins by a combinatorial peptide library approach.SHP-1 is a target of regorafenib in colorectal cancer.Functional requirements for inhibitory signal transmission by the immunomodulatory receptor CD300a.Regulation of hematopoietic cell function by inhibitory immunoglobulin G receptors and their inositol lipid phosphatase effectors.Direct Ras Inhibitors Identified from a Structurally Rigidified Bicyclic Peptide Library.The application of modular protein domains in proteomics Global analysis of peptide cyclization efficiency.Specificity profiling of protein-binding domains using one-bead-one-compound Peptide libraries.Targeting protein tyrosine phosphatases for anticancer drug discovery.Profiling the substrate specificity of protein kinases by on-bead screening of peptide libraries Bacterial effector activates jasmonate signaling by directly targeting JAZ transcriptional repressors.Once phosphorylated, tyrosines in carboxyl terminus of protein-tyrosine kinase Syk interact with signaling proteins, including TULA-2, a negative regulator of mast cell degranulation Deciphering Phosphotyrosine-Dependent Signaling Networks in Cancer by SH2 Profiling SOCS3 drives proteasomal degradation of indoleamine 2,3-dioxygenase (IDO) and antagonizes IDO-dependent tolerogenesis Binding specificity of SH2 domains: insight from free energy simulations.Role of tyrosine phosphatase SHP-1 in the mechanism of endorepellin angiostatic activity.Biophysical assay for tethered signaling reactions reveals tether-controlled activity for the phosphatase SHP-1.

P2860

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P2860

Decoding protein-protein interactions through combinatorial chemistry: sequence specificity of SHP-1, SHP-2, and SHIP SH2 domains.

http://www.wikidata.org/entity/Q33226743

description

2005 nî lūn-bûn

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2005 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2005 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

@zh-hans

2005年学术文章

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2005年学术文章

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2005年學術文章

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name

Decoding protein-protein inter ...... , SHP-2, and SHIP SH2 domains.

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Decoding protein-protein inter ...... , SHP-2, and SHIP SH2 domains.

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type

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Decoding protein-protein inter ...... , SHP-2, and SHIP SH2 domains.

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Decoding protein-protein inter ...... , SHP-2, and SHIP SH2 domains.

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Decoding protein-protein inter ...... , SHP-2, and SHIP SH2 domains.

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Decoding protein-protein inter ...... , SHP-2, and SHIP SH2 domains.

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Decoding protein-protein inter ...... , SHP-2, and SHIP SH2 domains.

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Anne-Sophie Wavreille

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Dehua Pei

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Jonathan P Butchar

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Junguk Park

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Michael C Sweeney

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Susheela Tridandapani

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14932-14947

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scholarly article

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10.1021/BI051408H

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45

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2005-11-01T00:00:00Z

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16274240

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