Structural basis for the activation and inhibition of the UCH37 deubiquitylase. - Test2 - elhamkhani - TriplyDB

Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

http://www.wikidata.org/entity/Q35163646

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Substrate specificity of the ubiquitin and Ubl proteases The business of deubiquitination - location, location, location Molecular architecture of polycomb repressive complexes Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets The BAP1/ASXL2 Histone H2A Deubiquitinase Complex Regulates Cell Proliferation and Is Disrupted in Cancer.Gates, Channels, and Switches: Elements of the Proteasome Machine Isolation and Characterization of RNA Aptamers against a Proteasome-Associated Deubiquitylating Enzyme UCH37.Using protein motion to read, write, and erase ubiquitin signals.The Proteasome Ubiquitin Receptor hRpn13 and Its Interacting Deubiquitinating Enzyme Uch37 Are Required for Proper Cell Cycle Progression Ubiquitin C-terminal hydrolase37 regulates Tcf7 DNA binding for the activation of Wnt signalling.Entropic stabilization of a deubiquitinase provides conformational plasticity and slow unfolding kinetics beneficial for functioning on the proteasome Structural disorder and its role in proteasomal degradation.Mechanisms of regulation and diversification of deubiquitylating enzyme function.BAP1/ASXL1 recruitment and activation for H2A deubiquitination.Ubiquitin recognition by the proteasome.Protein Degradation Systems as Antimalarial Therapeutic Targets.The role of ubiquitin-dependent segregase p97 (VCP or Cdc48) in chromatin dynamics after DNA double strand breaks.Identification of deubiquitinase targets of isothiocyanates using SILAC-assisted quantitative mass spectrometry.SGTA interacts with the proteasomal ubiquitin receptor Rpn13 via a carboxylate clamp mechanism.Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome.Ubiquitin recognition of BAP1: understanding its enzymatic function.Meddling with Fate: The Proteasomal Deubiquitinating Enzymes.UCHL5 expression associates with improved survival in lymph-node-positive rectal cancer.Nuclear ubiquitin C-terminal hydrolase L5 expression associates with increased patient survival in pancreatic ductal adenocarcinoma.Ubiquitin carboxyl-terminal hydrolases: involvement in cancer progression and clinical implications.The deubiquitinase UCHL5/UCH37 positively regulates Hedgehog signaling by deubiquitinating Smoothened.Ubiquitin carboxyl-terminal hydrolase isozyme L5 inhibits human glioma cell migration and invasion via downregulating SNRPF.Structure and energetics of pairwise interactions between proteasome subunits RPN2, RPN13, and ubiquitin clarify a substrate recruitment mechanism.A fluorescence polarization-based competition assay for measuring interactions between unlabeled ubiquitin chains and UCH37•RPN13.Positive cytoplasmic UCHL5 tumor expression in gastric cancer is linked to improved prognosis.Monoubiquitination of ASXLs controls the deubiquitinase activity of the tumor suppressor BAP1 A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomes Quantitative Proteomic Analysis Reveals That Arctigenin Alleviates Concanavalin A-Induced Hepatitis Through Suppressing Immune System and Regulating Autophagy

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Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

http://www.wikidata.org/entity/Q35163646

description

2015 nî lūn-bûn

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2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2015 թվականի փետրվարին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

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Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

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type

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Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

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Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

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Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

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Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

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J.MOLCEL.2015.01.016

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Structural basis for the activation and inhibition of the UCH37 deubiquitylase.

@en

P2093

Ada Ndoja

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

Benjamin Schmitt

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

Casey W Hemmis

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

Christopher P Hill

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

Frank G Whitby

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

Howard Robinson

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

Robert E Cohen

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

Ryan T Vander Linden

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Tingting Yao

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P2860

A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair

A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes

Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB

hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37

Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex

Association of C-terminal ubiquitin hydrolase BRCA1-associated protein 1 with cell cycle regulator host cell factor 1

Crystal structure of a deubiquitinating enzyme (human UCH-L3) at 1.8 A resolution

MolProbity: all-atom structure validation for macromolecular crystallography

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Structural basis for the specificity of ubiquitin C-terminal hydrolases

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901-911

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25702872

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