Structural basis for phosphoserine-proline recognition by group IV WW domains
about
Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation.The E3 ubiquitin ligase atrophin interacting protein 4 binds directly to the chemokine receptor CXCR4 via a novel WW domain-mediated interactionSnapshots of the RNA processing factor SCAF8 bound to different phosphorylated forms of the carboxyl-terminal domain of RNA polymerase IIThe ubiquitin-protein ligase Nedd4-2 differentially interacts with and regulates members of the Tweety family of chloride ion channelsStructural basis for polyproline recognition by the FE65 WW domainThreonine 48 in the BIR domain of survivin is critical to its mitotic and anti-apoptotic activities and can be phosphorylated by CK2 in vitroWW domains provide a platform for the assembly of multiprotein networksSolution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1Structure-function-folding relationship in a WW domainFF domains of CA150 bind transcription and splicing factors through multiple weak interactionsStructure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteinsRegulation of p53 localization and transcription by the HECT domain E3 ligase WWP1The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complexMultisite phosphorylation of Pin1-associated mitotic phosphoproteins revealed by monoclonal antibodies MPM-2 and CC-3JNK Signaling: Regulation and Functions Based on Complex Protein-Protein PartnershipsPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Regulation of AU-Rich Element RNA Binding Proteins by Phosphorylation and the Prolyl Isomerase Pin1Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity.1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptidesNMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1Determinants for Dephosphorylation of the RNA Polymerase II C-Terminal Domain by Scp1Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate bindingStructural Basis for High-Affinity Peptide Inhibition of Human Pin1Specificity and Autoregulation of Notch Binding by Tandem WW Domains in Suppressor of DeltexThe plant homeodomain finger of RAG2 recognizes histone H3 methylated at both lysine-4 and arginine-2The Nrd1–Nab3–Sen1 termination complex interacts with the Ser5-phosphorylated RNA polymerase II C-terminal domainIdentification, structure, and functional requirement of the Mediator submodule Med7N/31Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1cis -Proline-mediated Ser(P) 5 Dephosphorylation by the RNA Polymerase II C-terminal Domain Phosphatase Ssu72Structural Insights to How Mammalian Capping Enzyme Reads the CTD CodeEpigallocatechin-gallate Suppresses Tumorigenesis by Directly Targeting Pin1Structure of the Mediator Head module bound to the carboxy-terminal domain of RNA polymerase IIA Reduced-Amide Inhibitor of Pin1 Binds in a Conformation Resembling a Twisted-Amide Transition StateNovel Modifications on C-terminal Domain of RNA Polymerase II Can Fine-tune the Phosphatase Activity of Ssu72Structural and Kinetic Analysis of Prolyl-isomerization/Phosphorylation Cross-Talk in the CTD CodeEvidence for small-molecule-mediated loop stabilization in the structure of the isolated Pin1 WW domainVanishingly low levels of Ess1 prolyl-isomerase activity are sufficient for growth in Saccharomyces cerevisiae.The Ess1 prolyl isomerase is required for transcription termination of small noncoding RNAs via the Nrd1 pathwayPin1 modulates the dephosphorylation of the RNA polymerase II C-terminal domain by yeast Fcp1.
P2860
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P2860
Structural basis for phosphoserine-proline recognition by group IV WW domains
description
2000 nî lūn-bûn
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2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
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2000年论文
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name
Structural basis for phosphoserine-proline recognition by group IV WW domains
@ast
Structural basis for phosphoserine-proline recognition by group IV WW domains
@en
Structural basis for phosphoserine-proline recognition by group IV WW domains
@nl
type
label
Structural basis for phosphoserine-proline recognition by group IV WW domains
@ast
Structural basis for phosphoserine-proline recognition by group IV WW domains
@en
Structural basis for phosphoserine-proline recognition by group IV WW domains
@nl
prefLabel
Structural basis for phosphoserine-proline recognition by group IV WW domains
@ast
Structural basis for phosphoserine-proline recognition by group IV WW domains
@en
Structural basis for phosphoserine-proline recognition by group IV WW domains
@nl
P2093
P3181
P356
P1476
Structural basis for phosphoserine-proline recognition by group IV WW domains
@en
P2093
P304
P3181
P356
10.1038/77929
P407
P577
2000-08-01T00:00:00Z