(Q28270616)

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E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer

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title

E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer (English)

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author name string

Ziad M Eletr

series ordinal

1

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Danny T Huang

series ordinal

2

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David M Duda

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3

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Brenda A Schulman

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4

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Brian Kuhlman

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5

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language of work or name

English

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publication date

October 2005

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published in

Nature Structural & Molecular Biology

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volume

12

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issue

10

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page(s)

933-4

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cites work

Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade

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21 April 2017

Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases

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reference URL

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21 April 2017

Structural basis for recruitment of Ubc12 by an E2 binding domain in NEDD8's E1

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21 April 2017

Design of a Novel Globular Protein Fold with Atomic-Level Accuracy

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21 April 2017

Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail

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21 April 2017

The Doc1 subunit is a processivity factor for the anaphase-promoting complex.

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reference URL

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21 April 2017

Ubiquitin: structures, functions, mechanisms

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Crossref

reference URL

https://api.crossref.org/works/10.1038%2FNSMB984

retrieved

21 January 2018

Protein interactions within the N-end rule ubiquitin ligation pathway

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21 January 2018

NEDD8 recruits E2-ubiquitin to SCF E3 ligase.

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21 January 2018

Release of ubiquitin-charged Cdc34-S - Ub from the RING domain is essential for ubiquitination of the SCF(Cdc4)-bound substrate Sic1.

(Q28270616)

E2 conjugating enzymes must disengage from their E1 enzymes before E3-dependent ubiquitin and ubiquitin-like transfer

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