A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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The strategies for identification and quantification of SUMOylation.Recruitment of a SUMO isopeptidase to rDNA stabilizes silencing complexes by opposing SUMO targeted ubiquitin ligase activity.Identification of SUMO conjugation sites in the budding yeast proteome.

P2860

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P2860

A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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http://www.wikidata.org/entity/Q28551317

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2015 nî lūn-bûn

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2015 թուականին հրատարակուած գիտական յօդուած

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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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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

@ast

A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

@en

A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

@nl

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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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P1476

A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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P2093

Claudio P Albuquerque

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

Eyan Yeung

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

Shawn Ma

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

Ting Fu

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P2860

Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif

Active site remodelling accompanies thioester bond formation in the SUMO E1

Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1

Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover

Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1

Ubc9 sumoylation regulates SUMO target discrimination

Crystal Structure of UBA2ufd-Ubc9: Insights into E1-E2 Interactions in Sumo Pathways

The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.

Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p.

A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization

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e0143810

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scholarly article

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10.1371/JOURNAL.PONE.0143810

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English

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P478

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Kevin D Corbett

Huilin Zhou

P577

2015-01-01T00:00:00Z

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285595284

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26633173

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4669148

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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

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P2860

P2860

A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation

description

name

type

label

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P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P5875

P698

P932