Common mechanism of ligand recognition by group II/III WW domains: redefining their functional classification. - Wikidata - wikimedia - TriplyDB

Common mechanism of ligand recognition by group II/III WW domains: redefining their functional classification.

Common mechanism of ligand recognition by group II/III WW domains: redefining their functional classification.

http://www.wikidata.org/entity/Q30164094

about

ABL tyrosine kinases: evolution of function, regulation, and specificity Ligand binding to WW tandem domains of YAP2 transcriptional regulator is under negative cooperativity WWP2 promotes degradation of transcription factor OCT4 in human embryonic stem cells Structural basis for polyproline recognition by the FE65 WW domain WW domains provide a platform for the assembly of multiprotein networks Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1 affects its binding activity and deregulates pre-mRNA splicing Structure of the dimeric exonuclease TREX1 in complex with DNA displays a proline-rich binding site for WW Domains Comparative analysis of Saccharomyces cerevisiae WW domains and their interacting proteins.Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction Partially-supervised protein subclass discovery with simultaneous annotation of functional residues.Structure of FBP11 WW1-PL ligand complex reveals the mechanism of proline-rich ligand recognition by group II/III WW domains.Natural-like function in artificial WW domains.GAIA: a gram-based interaction analysis tool--an approach for identifying interacting domains in yeast.Redesign of a WW domain peptide for selective recognition of single-stranded DNA.Recent advances in MeCP2 structure and function.Interaction with polyglutamine-expanded huntingtin alters cellular distribution and RNA processing of huntingtin yeast two-hybrid protein A (HYPA).HECT E3 Ubiquitin Ligase Itch Functions as a Novel Negative Regulator of Gli-Similar 3 (Glis3) Transcriptional Activity.Complete thermodynamic and kinetic characterization of the isomer-specific interaction between Pin1-WW domain and the amyloid precursor protein cytoplasmic tail phosphorylated at Thr668.Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily Signaling from membrane receptors to tumor suppressor WW domain-containing oxidoreductase.Genome-wide analysis of the WW domain-containing protein genes in silkworm and their expansion in eukaryotes.Intrinsic disorder and autonomous domain function in the multifunctional nuclear protein, MeCP2.Structural Basis of Intracellular TGF-β Signaling: Receptors and Smads.Characterization of substrate binding of the WW domains in human WWP2 protein.Peptide-polymer ligands for a tandem WW-domain, an adaptive multivalent protein-protein interaction: lessons on the thermodynamic fitness of flexible ligands.WW domains 2 and 3 of Rsp5p play overlapping roles in binding to the LPKY motif of Spt23p and Mga2p.Survey of rice proteins interacting with OsFCA and OsFY proteins which are homologous to the Arabidopsis flowering time proteins, FCA and FY.

P2860

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P2860

Common mechanism of ligand recognition by group II/III WW domains: redefining their functional classification.

http://www.wikidata.org/entity/Q30164094

description

2004 nî lūn-bûn

@nan

2004 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

Common mechanism of ligand rec ...... eir functional classification.

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Common mechanism of ligand rec ...... eir functional classification.

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type

label

Common mechanism of ligand rec ...... eir functional classification.

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Common mechanism of ligand rec ...... eir functional classification.

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prefLabel

Common mechanism of ligand rec ...... eir functional classification.

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Common mechanism of ligand rec ...... eir functional classification.

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P1433

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P1476

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P698

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P356

P1433

Journal of Biological Chemistry

P1476

Common mechanism of ligand rec ...... heir functional classification

@en

P2093

Juan J Herrero

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

Lubing Lian

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

Marius Sudol

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

Mihoko Takahashi

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

Yusuke Kato

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

P2860

Function of WW domains as phosphoserine- or phosphothreonine-binding modules

Association of two nuclear proteins, Npw38 and NpwBP, via the interaction between the WW domain and a novel proline-rich motif containing glycine and arginine

Interaction of WW domains with hematopoietic transcription factor p45/NF-E2 and RNA polymerase II

The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules

FBP WW domains and the Abl SH3 domain bind to a specific class of proline-rich ligands

WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif

Profilin binds proline-rich ligands in two distinct amide backbone orientations

Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan

Structural basis for phosphoserine-proline recognition by group IV WW domains

Solution structure of a Nedd4 WW domain-ENaC peptide complex

P304

31833-31841

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P31

scholarly article

P356

10.1074/JBC.M404719200

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P407

P433

30

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P478

279

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P50

Masaru Tanokura

P577

2004-05-07T00:00:00Z

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P698

15133021

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