Capzimin is a potent and specific inhibitor of proteasome isopeptidase Rpn11
Published 2017 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Capzimin is a potent and specific inhibitor of proteasome isopeptidase Rpn11
Authors
Keywords
-
Journal
Nature Chemical Biology
Volume 13, Issue 5, Pages 486-493
Publisher
Springer Nature
Online
2017-03-01
DOI
10.1038/nchembio.2326
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- A conserved quality-control pathway that mediates degradation of unassembled ribosomal proteins
- (2016) Min-Kyung Sung et al. eLife
- Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition
- (2016) Corey M Dambacher et al. eLife
- Targeting the AAA ATPase p97 as an Approach to Treat Cancer through Disruption of Protein Homeostasis
- (2015) Daniel J. Anderson et al. CANCER CELL
- A Reversible and Highly Selective Inhibitor of the Proteasomal Ubiquitin Receptor Rpn13 Is Toxic to Multiple Myeloma Cells
- (2015) Darci J. Trader et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- ETD Outperforms CID and HCD in the Analysis of the Ubiquitylated Proteome
- (2015) Tanya R. Porras-Yakushi et al. JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY
- Higher-Order Assembly of BRCC36–KIAA0157 Is Required for DUB Activity and Biological Function
- (2015) Elton Zeqiraj et al. MOLECULAR CELL
- Proteotoxic crisis, the ubiquitin-proteasome system, and cancer therapy
- (2014) Raymond J Deshaies BMC BIOLOGY
- Fluorescent Sensors for Measuring Metal Ions in Living Systems
- (2014) Kyle P. Carter et al. CHEMICAL REVIEWS
- The ubiquitin–proteasome system: opportunities for therapeutic intervention in solid tumors
- (2014) Daniel E Johnson ENDOCRINE-RELATED CANCER
- Current treatment landscape for relapsed and/or refractory multiple myeloma
- (2014) Meletios A. Dimopoulos et al. Nature Reviews Clinical Oncology
- Structure of the Rpn11–Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation
- (2014) Evan J Worden et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11
- (2014) G. R. Pathare et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- p97-dependent retrotranslocation and proteolytic processing govern formation of active Nrf1 upon proteasome inhibition
- (2014) Senthil K Radhakrishnan et al. eLife
- A bis-Benzylidine Piperidone Targeting Proteasome Ubiquitin Receptor RPN13/ADRM1 as a Therapy for Cancer
- (2013) Ravi K. Anchoori et al. CANCER CELL
- Metalloprotein–Inhibitor Binding: Human Carbonic Anhydrase II as a Model for Probing Metal–Ligand Interactions in a Metalloprotein Active Site
- (2013) David P. Martin et al. INORGANIC CHEMISTRY
- Proteasomes Activate Aggresome Disassembly and Clearance by Producing Unanchored Ubiquitin Chains
- (2013) Rui Hao et al. MOLECULAR CELL
- Regulation of Pluripotency and Cellular Reprogramming by the Ubiquitin-Proteasome System
- (2012) Shannon M. Buckley et al. Cell Stem Cell
- Refined Preparation and Use of Anti-diglycine Remnant (K-ε-GG) Antibody Enables Routine Quantification of 10,000s of Ubiquitination Sites in Single Proteomics Experiments
- (2012) Namrata D. Udeshi et al. MOLECULAR & CELLULAR PROTEOMICS
- Using transcriptome sequencing to identify mechanisms of drug action and resistance
- (2012) Sarah A Wacker et al. Nature Chemical Biology
- Chromatin dynamics and the repair of DNA double strand breaks
- (2011) Ye Xu et al. CELL CYCLE
- Emerging trends in metalloprotein inhibition
- (2011) Matthieu Rouffet et al. DALTON TRANSACTIONS
- Quantitative Cell-based Protein Degradation Assays to Identify and Classify Drugs That Target the Ubiquitin-Proteasome System
- (2011) Tsui-Fen Chou et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Dependence of Proteasome Processing Rate on Substrate Unfolding
- (2011) Allen Henderson et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Targeted Mass Spectrometric Approach for Biomarker Discovery and Validation with Nonglycosylated Tryptic Peptides from N-linked Glycoproteins in Human Plasma
- (2011) Ju Yeon Lee et al. MOLECULAR & CELLULAR PROTEOMICS
- FAS and NF-κB signalling modulate dependence of lung cancers on mutant EGFR
- (2011) Trever G. Bivona et al. NATURE
- Inhibition of proteasome deubiquitinating activity as a new cancer therapy
- (2011) Pádraig D'Arcy et al. NATURE MEDICINE
- Reversible inhibitor of p97, DBeQ, impairs both ubiquitin-dependent and autophagic protein clearance pathways
- (2011) T.-F. Chou et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Transcription Factor Nrf1 Mediates the Proteasome Recovery Pathway after Proteasome Inhibition in Mammalian Cells
- (2010) Senthil K. Radhakrishnan et al. MOLECULAR CELL
- Proteasomal Degradation Is Transcriptionally Controlled by TCF11 via an ERAD-Dependent Feedback Loop
- (2010) Janos Steffen et al. MOLECULAR CELL
- Regulators of the Proteasome Pathway, Uch37 and Rpn13, Play Distinct Roles in Mouse Development
- (2010) Amin Al-Shami et al. PLoS One
- Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
- (2009) Daniel Finley Annual Review of Biochemistry
- Boveri revisited: chromosomal instability, aneuploidy and tumorigenesis
- (2009) Andrew J. Holland et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Structural Insights into NEDD8 Activation of Cullin-RING Ligases: Conformational Control of Conjugation
- (2008) David M. Duda et al. CELL
- Structural basis for specific cleavage of Lys 63-linked polyubiquitin chains
- (2008) Yusuke Sato et al. NATURE
- MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
- (2008) Jürgen Cox et al. NATURE BIOTECHNOLOGY
Add your recorded webinar
Do you already have a recorded webinar? Grow your audience and get more views by easily listing your recording on Peeref.
Upload NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started