Concepts and Methodologies to Study Protein SUMOylation: An Overview.

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Concepts and Methodologies to Study Protein SUMOylation: An Overview.

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年學術文章

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2016年學術文章

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2016年學術文章

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Concepts and Methodologies to Study Protein SUMOylation: An Overview.

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Concepts and Methodologies to Study Protein SUMOylation: An Overview.

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Concepts and Methodologies to Study Protein SUMOylation: An Overview.

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Concepts and Methodologies to Study Protein SUMOylation: An Overview.

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Concepts and Methodologies to Study Protein SUMOylation: An Overview.

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Concepts and Methodologies to Study Protein SUMOylation: An Overview.

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P1476

Concepts and Methodologies to Study Protein SUMOylation: An Overview

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P2093

Manuel S Rodriguez

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P2860

In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2

Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1

Association of the human SUMO-1 protease SENP2 with the nuclear pore

Ubiquitin-specific protease-like 1 (USPL1) is a SUMO isopeptidase with essential, non-catalytic functions

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

Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics

Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex.

A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex

The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing

SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family

P304

3-22

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scholarly article

P356

10.1007/978-1-4939-6358-4_1

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P407

English

P478

1475

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P50

Michael J. Matunis

P577

2016-01-01T00:00:00Z

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P698

27631794

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