Nature Search

Phosphorylation and linear ubiquitin direct A20 inhibition of inflammation

The authors define molecular mechanisms by which distinct domains of the ubiquitin editing enzyme A20 contribute to the regulation of inflammation and cell death.

Ingrid E. Wertz
Kim Newton
Vishva M. Dixit
Research09 Dec 2015
Nature

Volume: 528, P: 370-375
Tumour promoter phorbol-12-myristate-13-acetate induces chromosomal damage via indirect action

Ingrid Emerit
Peter A. Cerutti
Research10 Sept 1981
Nature

Volume: 293, P: 144-146
USP7 small-molecule inhibitors interfere with ubiquitin binding

The development of selective ubiquitin-specific protease-7 (USP7) inhibitors GNE-6640 and GNE-6776, which induce tumour cell death and reveal differential kinetics of Lys-48 and Lys-63-linked ubiquitin chain depolymerization by USP7.

Lorna Kategaya
Paola Di Lello
Ingrid E. Wertz
Research18 Oct 2017
Nature

Volume: 550, P: 534-538
Correction: Corrigendum: Conformational stabilization of ubiquitin yields potent and selective inhibitors of USP7

Yingnan Zhang
Lijuan Zhou
Jacob E Corn
Amendments and Corrections15 Feb 2013
Nature Chemical Biology

Volume: 9, P: 192
Erratum: Sensitivity to antitubulin chemotherapeutics is regulated by MCL1 and FBW7

Ingrid E. Wertz
Saritha Kusam
Vishva M. Dixit
Amendments and Corrections15 Jun 2011
Nature

Volume: 475, P: 122
Erratum: Phosphorylation and linear ubiquitin direct A20 inhibition of inflammation

Ingrid E. Wertz
Kim Newton
Vishva M. Dixit
Amendments and Corrections13 Jan 2016
Nature

Volume: 532, P: 402
Antibody toolkit reveals N-terminally ubiquitinated substrates of UBE2W

UBE2W catalyzes the ubiquitination of protein N-termini but its substrate spectrum is largely unknown. Here, the authors discover mAbs selective for peptides derived from N-terminally ubiquitinated proteins, solve the structure of a peptide-bound mAb and apply the mAbs to map endogenous UBE2W substrates by proteomics.

Christopher W. Davies
Simon E. Vidal
James T. Koerber
ResearchOpen Access29 Jul 2021
Nature Communications

Volume: 12, P: 1-19
Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes

Deubiquitinases are proteases that cleave after the C-terminus of ubiquitin to hydrolyze ubiquitin chains and cleave ubiquitin from substrates. Here the authors describe a reactive-site-centric chemoproteomics approach to studying deubiquitinase activity, and expand the repertoire of known deubiquitinases.

David S. Hewings
Johanna Heideker
Ingrid E. Wertz
ResearchOpen Access21 Mar 2018
Nature Communications

Volume: 9, P: 1-17
Targeted degradation via direct 26S proteasome recruitment

Discovery of macrocyclic ligands to the 19S regulatory particle protein PSMD2 enables the synthesis of heterobifunctional molecules that demonstrate proof-of-concept, targeted degradation of BRD4 through direct engagement of the 26S proteasome.

Charlene Bashore
Sumit Prakash
Erin C. Dueber
ResearchOpen Access28 Dec 2022
Nature Chemical Biology

Volume: 19, P: 55-63
It takes two to tango: a new couple in the family of ubiquitin-editing complexes

Improper termination of inflammatory signals can contribute to tumorigenesis. Cyld and Itch form an ubiquitin-editing complex that cooperatively downregulates the kinase Tak1 and thereby attenuates downstream activation of the transcription factor NF-κB.

Ingrid E Wertz
News & Views16 Nov 2011
Nature Immunology

Volume: 12, P: 1133-1135
Sensitivity to antitubulin chemotherapeutics is regulated by MCL1 and FBW7

Ingrid E. Wertz
Saritha Kusam
Vishva M. Dixit
Research02 Mar 2011
Nature

Volume: 471, P: 110-114
De-ubiquitination and ubiquitin ligase domains of A20 downregulate NF-κB signalling

Ingrid E. Wertz
Karen M. O'Rourke
Vishva M. Dixit
Research18 Jul 2004
Nature

Volume: 430, P: 694-699
The ubiquitin ligase COP1 is a critical negative regulator of p53

David Dornan
Ingrid Wertz
Vishva M. Dixit
Research21 Apr 2004
Nature

Volume: 429, P: 86-92
Bcl10 activates the NF-κB pathway through ubiquitination of NEMO

Honglin Zhou
Ingrid Wertz
Vishva M. Dixit
Research24 Dec 2003
Nature

Volume: 427, P: 167-171
Denisovan, modern human and mouse TNFAIP3 alleles tune A20 phosphorylation and immunity

A20, encoded by TNFAIP3, is a negative-feedback inhibitor of NF-κB. Grey and colleagues identify natural human variants of TNFAIP3, which lower A20 activity and increase autoinflammatory responses. These alleles were inherited by descendants of Denisovans who crossed the Wallace Line to inhabit Oceania.

Nathan W. Zammit
Owen M. Siggs
Shane T. Grey
Research18 Sept 2019
Nature Immunology

Volume: 20, P: 1299-1310
Identifying transcriptional programs underlying cancer drug response with TraCe-seq

Transcriptional mechanisms of drug response are identified with scRNA-seq and molecular barcoding.

Matthew T. Chang
Frances Shanahan
Xin Ye
Research16 Sept 2021
Nature Biotechnology

Volume: 40, P: 86-93
Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death

The regulation of apoptosis is essential for cell homeostasis and the survival of multicellular organisms, and excessive or diminished apopotosis can contribute to various diseases. The post-translational modification of apoptotic proteins by ubiquitylation is a key regulatory mechanism of cell death signalling cascades. Targeting apoptotic regulatory proteins in the ubiquitin proteasome system might afford clinical benefits.

Domagoj Vucic
Vishva M. Dixit
Ingrid E. Wertz
Reviews23 Jun 2011
Nature Reviews Molecular Cell Biology

Volume: 12, P: 439-452
Conformational stabilization of ubiquitin yields potent and selective inhibitors of USP7

Stabilization of ubiquitin's β1-β2 region by computational design and phage display, targeting both buried and surface residues, yields a ubiquitin variant that specifically inhibits the deubiquitinase USP7 in vitro and in cells.

Yingnan Zhang
Lijuan Zhou
Jacob E Corn
Research25 Nov 2012
Nature Chemical Biology

Volume: 9, P: 51-58
A20: from ubiquitin editing to tumour suppression

Recent reports have identified the ubiquitin-editing enzyme A20 as a crucial tumour suppressor in various lymphomas. This Review analyses how deregulation of ubiquitylation in the NF-κB signalling pathway can promote tumorigenesis.

Sarah G. Hymowitz
Ingrid E. Wertz
Reviews12 Apr 2010
Nature Reviews Cancer

Volume: 10, P: 332-341
Rapid, semi-automated protein terminal characterization using ISDetect

Corey E Bakalarski
Yutian Gan
Wendy Sandoval
Correspondence09 Aug 2016
Nature Biotechnology

Volume: 34, P: 811-813
COP1 is a tumour suppressor that causes degradation of ETS transcription factors

Alberto C. Vitari
Kevin G. Leong
Vishva M. Dixit
Research15 May 2011
Nature

Volume: 474, P: 403-406
Loss-of-function mutations in TNFAIP3 leading to A20 haploinsufficiency cause an early-onset autoinflammatory disease

Ivona Aksentijevich and colleagues identify heterozygous loss-of-function mutations in TNFAIP3 (encoding A20) in six unrelated families with early-onset systemic inflammation. Affected individuals exhibit increased expression of NF-κB–mediated proinflammatory cytokines, consistent with the established role of A20 as a potent inhibitor of the NF-κB signaling pathway.

Qing Zhou
Hongying Wang
Ivona Aksentijevich
Research07 Dec 2015
Nature Genetics

Volume: 48, P: 67-73
Ubiquitination in the regulation of inflammatory cell death and cancer

Peter E. Cockram
Matthias Kist
Domagoj Vucic
ReviewsOpen Access11 Jan 2021
Cell Death & Differentiation

Volume: 28, P: 591-605
Regulation of death receptor signaling by the ubiquitin system

I E Wertz
V M Dixit
Reviews06 Nov 2009
Cell Death & Differentiation

Volume: 17, P: 14-24

Search

Phosphorylation and linear ubiquitin direct A20 inhibition of inflammation

Tumour promoter phorbol-12-myristate-13-acetate induces chromosomal damage via indirect action

USP7 small-molecule inhibitors interfere with ubiquitin binding

Correction: Corrigendum: Conformational stabilization of ubiquitin yields potent and selective inhibitors of USP7

Erratum: Sensitivity to antitubulin chemotherapeutics is regulated by MCL1 and FBW7

Erratum: Phosphorylation and linear ubiquitin direct A20 inhibition of inflammation

Antibody toolkit reveals N-terminally ubiquitinated substrates of UBE2W

Reactive-site-centric chemoproteomics identifies a distinct class of deubiquitinase enzymes

Targeted degradation via direct 26S proteasome recruitment

It takes two to tango: a new couple in the family of ubiquitin-editing complexes

Sensitivity to antitubulin chemotherapeutics is regulated by MCL1 and FBW7

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

The ubiquitin ligase COP1 is a critical negative regulator of p53

Bcl10 activates the NF-κB pathway through ubiquitination of NEMO

Denisovan, modern human and mouse TNFAIP3 alleles tune A20 phosphorylation and immunity

Identifying transcriptional programs underlying cancer drug response with TraCe-seq

Ubiquitylation in apoptosis: a post-translational modification at the edge of life and death

Conformational stabilization of ubiquitin yields potent and selective inhibitors of USP7

A20: from ubiquitin editing to tumour suppression

Rapid, semi-automated protein terminal characterization using ISDetect

COP1 is a tumour suppressor that causes degradation of ETS transcription factors

Loss-of-function mutations in TNFAIP3 leading to A20 haploinsufficiency cause an early-onset autoinflammatory disease

Ubiquitination in the regulation of inflammatory cell death and cancer

Regulation of death receptor signaling by the ubiquitin system

Search

Quick links

Search

Filter By:

Search

Quick links