Breaking the chains: structure and function of the deubiquitinases (Q28131738)

Nature Reviews Molecular Cell Biology

Europe PubMed Central

title

Breaking the chains: structure and function of the deubiquitinases (English)

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Michael J Clague

2

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Sylvie Urbé

object named as

Sylvie Urbé

series ordinal

3

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David Komander

series ordinal

1

object named as

David Komander

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language of work or name

English

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publication date

August 2009

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published in

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volume

10

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issue

8

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page(s)

550-63

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Multiple associated proteins regulate proteasome structure and function

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Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1.

31 March 2020

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A ubiquitin stress response induces altered proteasome composition.

31 March 2020

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Deubiquitinating enzyme Ubp6 functions noncatalytically to delay proteasomal degradation.

31 March 2020

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31 March 2020

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31 March 2020

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31 March 2020

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A histone H2A deubiquitinase complex coordinating histone acetylation and H1 dissociation in transcriptional regulation

31 March 2020

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Regulation of cell cycle progression and gene expression by H2A deubiquitination

31 March 2020

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31 March 2020

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31 March 2020

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The deubiquitinating enzyme USP1 regulates the Fanconi anemia pathway

31 March 2020

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Deubiquitination of FANCD2 is required for DNA crosslink repair

31 March 2020

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Ubiquitin in NF-kappaB signaling.

31 March 2020

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Deubiquitylation and regulation of the immune response

31 March 2020

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The ubiquitin-modifying enzyme A20 is required for termination of Toll-like receptor responses

31 March 2020

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Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice

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Mutations of multiple genes cause deregulation of NF-kappaB in diffuse large B-cell lymphoma.

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Frequent inactivation of A20 in B-cell lymphomas

31 March 2020

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TNFAIP3 (A20) is a tumor suppressor gene in Hodgkin lymphoma and primary mediastinal B cell lymphoma

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De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-kappaB signalling

31 March 2020

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The E3 ligase Itch negatively regulates inflammatory signaling pathways by controlling the function of the ubiquitin-editing enzyme A20

31 March 2020

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The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling

31 March 2020

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NF-kappaB suppression by the deubiquitinating enzyme Cezanne: a novel negative feedback loop in pro-inflammatory signaling

31 March 2020

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FAM/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination

31 March 2020

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USP17 regulates Ras activation and cell proliferation by blocking RCE1 activity

31 March 2020

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Ab initio protein modelling reveals novel human MIT domains

31 March 2020

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The DUB/USP17 deubiquitinating enzymes, a multigene family within a tandemly repeated sequence

31 March 2020

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Cloning and enzymatic analysis of 22 novel human ubiquitin-specific proteases

31 March 2020

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Structure of a multipartite protein-protein interaction domain in splicing factor prp8 and its link to retinitis pigmentosa

31 March 2020

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Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate

31 March 2020

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Josephin domain of ataxin-3 contains two distinct ubiquitin-binding sites.

31 March 2020

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12 December 2020

Defining the human deubiquitinating enzyme interaction landscape

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Suppression of the deubiquitinating enzyme USP5 causes the accumulation of unanchored polyubiquitin and the activation of p53

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Regulation of monoubiquitinated PCNA by DUB autocleavage

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UAF1 is a subunit of multiple deubiquitinating enzyme complexes

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Dissection of USP catalytic domains reveals five common insertion points

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HAUSP is required for p53 destabilization

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12 December 2020

Identifiers

DOI

10.1038/NRM2731

1 reference

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

100815

1036789873

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100815

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference