MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes. - Wikidata - awgldk - TriplyDB

MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes.

MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes.

http://www.wikidata.org/entity/Q27934744

about

DUBbing Cancer: Deubiquitylating Enzymes Involved in Epigenetics, DNA Damage and the Cell Cycle As Therapeutic Targets A single MIU motif of MINDY-1 recognizes K48-linked polyubiquitin chains The emerging role of deubiquitinating enzymes in genomic integrity, diseases, and therapeutics Mechanisms of regulation and diversification of deubiquitylating enzyme function.Parkin-phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity.The emerging complexity of ubiquitin architecture.Activity-based probes for the ubiquitin conjugation-deconjugation machinery: new chemistries, new tools, and new insights.Emerging role of DUBs in tumor metastasis and apoptosis: Therapeutic implication.CYLD, A20 and OTULIN deubiquitinases in NF-κB signaling and cell death: so similar, yet so different.Ubiquitin and Parkinson's disease through the looking glass of genetics.Ubiquitin Chains Modified by the Bacterial Ligase SdeA Are Protected from Deubiquitinase Hydrolysis.PLAA Mutations Cause a Lethal Infantile Epileptic Encephalopathy by Disrupting Ubiquitin-Mediated Endolysosomal Degradation of Synaptic Proteins.Regulation of the cell cycle and centrosome biology by deubiquitylases.Ubiquitylation at the crossroads of development and disease.iUUCD 2.0: an update with rich annotations for ubiquitin and ubiquitin-like conjugations.Ubiquitin turnover and endocytic trafficking in yeast are regulated by Ser57 phosphorylation of ubiquitin.Structure-Guided Development of a Potent and Selective Non-covalent Active-Site Inhibitor of USP7.Inhibition of USP10 induces degradation of oncogenic FLT3.The Deubiquitinating Enzymes UBP12 and UBP13 Positively Regulate MYC2 Levels in Jasmonate Responses.Discovery and characterization of highly potent and selective allosteric USP7 inhibitors.Deubiquitinase USP13 dictates MCL1 stability and sensitivity to BH3 mimetic inhibitors.The deubiquitylase USP15 regulates topoisomerase II alpha to maintain genome integrity.Discovery and Characterization of ZUFSP/ZUP1, a Distinct Deubiquitinase Class Important for Genome Stability.Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes.A family of unconventional deubiquitinases with modular chain specificity determinants.Receptor Tyrosine Kinase Ubiquitination and De-Ubiquitination in Signal Transduction and Receptor Trafficking.Integrated Genomic Analysis of the Ubiquitin Pathway across Cancer Types.USP52 acts as a deubiquitinase and promotes histone chaperone ASF1A stabilization.FAM188B enhances cell survival via interaction with USP7.Active site alanine mutations convert deubiquitinases into high-affinity ubiquitin-binding proteins

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P2860

MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes.

http://www.wikidata.org/entity/Q27934744

description

2016 nî lūn-bûn

@nan

2016 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի հուլիսին հրատարակված գիտական հոդված

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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name

MINDY-1 Is a Member of an Evol ...... y of Deubiquitinating Enzymes.

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MINDY-1 Is a Member of an Evol ...... y of Deubiquitinating Enzymes.

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MINDY-1 Is a Member of an Evol ...... y of Deubiquitinating Enzymes.

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MINDY-1 Is a Member of an Evol ...... y of Deubiquitinating Enzymes.

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MINDY-1 Is a Member of an Evol ...... y of Deubiquitinating Enzymes.

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MINDY-1 Is a Member of an Evol ...... y of Deubiquitinating Enzymes.

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MINDY-1 Is a Member of an Evol ...... y of Deubiquitinating Enzymes.

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MINDY-1 Is a Member of an Evol ...... y of Deubiquitinating Enzymes.

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MINDY-1 Is a Member of an Evol ...... y of Deubiquitinating Enzymes.

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J.MOLCEL.2016.05.009

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MINDY-1 Is a Member of an Evol ...... ly of Deubiquitinating Enzymes

@en

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Karim Labib

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Kay Hofmann

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Pedro Junior Nkosi

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Simone Weidlich

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Soo-Youn Choi

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

Syed Arif Abdul Rehman

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Yosua Adi Kristariyanto

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

P2860

OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis

C10ORF97 is a novel tumor-suppressor gene of non-small-cell lung cancer and a functional variant of this gene increases the risk of non-small-cell lung cancer

Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin

Evidence for bidentate substrate binding as the basis for the K48 linkage specificity of otubain 1

Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3

The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module

Recognition of the polyubiquitin proteolytic signal

Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes

Jalview Version 2--a multiple sequence alignment editor and analysis workbench

On Terminal Alkynes That Can React with Active-Site Cysteine Nucleophiles in Proteases

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146-155

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scholarly article

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1004295

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10.1016/J.MOLCEL.2016.05.009

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1

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63

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2016-06-09T00:00:00Z

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27292798

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MINDY lysine 48 deubiquitinase 3

MINDY lysine 48 deubiquitinase 1

MINDY lysine 48 deubiquitinase 2

Lys48-specific deubiquitinase activity

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4942677

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