Ubiquitin chain conformation regulates recognition and activity of interacting proteins - Test2 - elhamkhani - TriplyDB

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

http://www.wikidata.org/entity/Q28280440

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OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis Ubiquitin modifications Role of Deubiquitinating Enzymes in DNA Repair Regulation of Met1-linked polyubiquitin signalling by the deubiquitinase OTULIN Optimising methods for the preservation, capture and identification of ubiquitin chains and ubiquitylated proteins by immunoblotting Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating Activity of SARS-CoV Papain-Like Protease Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation New conformations of linear polyubiquitin chains from crystallographic and solution-scattering studies expand the conformational space of polyubiquitin Does antigen masking by ubiquitin chains protect from the development of autoimmune diseases?A New Method for Determining Structure Ensemble: Application to a RNA Binding Di-Domain Protein.Non-degradative Ubiquitination of Protein Kinases.Recovering a representative conformational ensemble from underdetermined macromolecular structural data.Mechanisms of generating polyubiquitin chains of different topology.Assembly and specific recognition of k29- and k33-linked polyubiquitin.Deubiquitinating enzyme specificity for ubiquitin chain topology profiled by di-ubiquitin activity probes The F-box protein FBXO7 positively regulates bone morphogenetic protein-mediated signaling through Lys-63-specific ubiquitination of neurotrophin receptor-interacting MAGE (NRAGE).PolyUbiquitin chain linkage topology selects the functions from the underlying binding landscape SARS hCoV papain-like protease is a unique Lys48 linkage-specific di-distributive deubiquitinating enzyme Substrate degradation by the proteasome: a single-molecule kinetic analysis.The COP9 signalosome and vascular function: intriguing possibilities?VRK1 regulates Cajal body dynamics and protects coilin from proteasomal degradation in cell cycle Comparison of native and non-native ubiquitin oligomers reveals analogous structures and reactivities.Lys63-linked ubiquitin chain adopts multiple conformational states for specific target recognition Using protein motion to read, write, and erase ubiquitin signals.Ensemble structure description of Lys63-linked diubiquitin The Colossus of ubiquitylation: decrypting a cellular code.Recognition of Lys48-Linked Di-ubiquitin and Deubiquitinating Activities of the SARS Coronavirus Papain-like Protease.Measuring activity in the ubiquitin-proteasome system: from large scale discoveries to single cells analysis Lysine 63-linked polyubiquitination is required for EGF receptor degradation.OTUB1-catalyzed deubiquitination of FOXM1 facilitates tumor progression and predicts a poor prognosis in ovarian cancer.A snapshot of ubiquitin chain elongation: lysine 48-tetra-ubiquitin slows down ubiquitination.Deubiquitylases from genes to organism.Ubiquitin-dependent sorting in endocytosis.Discovery of Therapeutic Deubiquitylase Effector Molecules: Current Perspectives.Ubiquitin-binding domains: mechanisms of ubiquitin recognition and use as tools to investigate ubiquitin-modified proteomes.DUBs, the regulation of cell identity and disease.Deciphering the protein-RNA recognition code: combining large-scale quantitative methods with structural biology.Ubiquitin S65 phosphorylation engenders a pH-sensitive conformational switch.Determining Atomistic SAXS Models of Tri-Ubiquitin Chains from Bayesian Analysis of Accelerated Molecular Dynamics Simulations.

P2860

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P2860

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

http://www.wikidata.org/entity/Q28280440

description

2012 nî lūn-bûn

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2012 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի դեկտեմբերին 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

@zh-hk

2012年論文

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2012年論文

@zh-tw

2012年论文

@wuu

name

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

@ast

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

@en

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

@nl

type

label

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

@ast

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

@en

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

@nl

prefLabel

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

@ast

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

@en

Ubiquitin chain conformation regulates recognition and activity of interacting proteins

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Ubiquitin chain conformation regulates recognition and activity of interacting proteins

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Alexander A Zhukov

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

David Komander

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

Georg Blaser

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

Maria J Ruedas-Rama

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

Mathew H Horrocks

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

Shehu Ibrahim

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

Sophie E Jackson

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

Yu Ye

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

P2860

Structural basis and specificity of human otubain 1-mediated deubiquitination

Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains

Recognition of the polyubiquitin proteolytic signal

Structure of a diubiquitin conjugate and a model for interaction with ubiquitin conjugating enzyme (E2)

Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH

Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies

Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains

Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation

Hidden alternative structures of proline isomerase essential for catalysis

Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21

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266-70

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scholarly article

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1083550

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10.1038/NATURE11722

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P433

7428

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492

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David Klenerman

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2012-12-13T00:00:00Z

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233827991

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1046232162

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23201676

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3605796

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