Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases (Q27939287)

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English	Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases	scientific article

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1 December 2016

Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases (English)

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1 December 2016

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GOA release 2020-03-11

author

Aaron Ciechanover

series ordinal

7

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Gunnar Dittmar

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3

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Martin Scheffner

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4

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author name string

Katrin Bagola

series ordinal

1

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Maximilian von Delbrück

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2

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Inbal Ziv

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5

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Michael H Glickman

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6

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Thomas Sommer

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8

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language of work or name

English

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publication date

23 May 2013

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1 December 2016

50

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issue

4

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page(s)

528-39

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cites work

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A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain

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Diverse polyubiquitin interaction properties of ubiquitin-associated domains

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The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site

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Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome.

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DOI

10.1016/J.MOLCEL.2013.04.005

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1 December 2016

ResearchGate publication ID

236691077

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Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases (Q27939287)

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Ubiquitin binding by a CUE domain regulates ubiquitin chain formation by ERAD E3 ligases (Q27939287)

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