The complexity of recognition of ubiquitinated substrates by the 26S proteasome (original) (raw)

Proteins containing ubiquitin-like (Ubl) domains not only bind to 26S proteasomes but also induce their activation

Alfred Goldberg

Proceedings of the National Academy of Sciences, 2020

View PDFchevron_right

How the 26S Proteasome Degrades Ubiquitinated Proteins in the Cell

Bernat Coll-Martínez

Biomolecules, 2019

View PDFchevron_right

A New Method of Purification of Proteasome Substrates Reveals Polyubiquitination of 20 S Proteasome Subunits

D. Attaix, Daniel Béchet, Daniel Bechet, Daniel Taillandier

Journal of Biological Chemistry - J BIOL CHEM, 2006

View PDFchevron_right

Transferring substrates to the 26S proteasome

Michael Seeger

Trends in Biochemical Sciences, 2003

View PDFchevron_right

Ubiquitin-independent proteolytic functions of the proteasome

Sherwin Wilk

Archives of Biochemistry and Biophysics, 2003

View PDFchevron_right

ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome that commit to degradation

Alfred Goldberg

Molecular cell, 2010

View PDFchevron_right

A 26 S protease subunit that binds ubiquitin conjugates

Martin Rechsteiner

The Journal of biological chemistry, 1994

View PDFchevron_right

Proteasomes Can Degrade a Significant Proportion of Cellular Proteins Independent of Ubiquitination

Ekaterina Viktorova

Journal of Molecular Biology, 2009

View PDFchevron_right

Proteomics to study the diversity and dynamics of proteasome complexes: from fundamentals to the clinic

Marie-pierre Bousquet-dubouch

Expert Review of Proteomics, 2011

View PDFchevron_right

Localization to the Proteasome Is Sufficient for Degradation

Bernat Crosas Navarro

Journal of Biological Chemistry, 2004

View PDFchevron_right

Ubiquitinated proteasome inhibitor is a component of the 26 S proteasome complex

Joseph Etlinger

Biochemistry, 1992

View PDFchevron_right

A 26S protease subunit that binds ubiquitin conjugates. J Biol Chem

Martin Rechsteiner

Journal of Biological Chemistry

View PDFchevron_right

An ATP-Stabilized Inhibitor of the Proteasome is a Component of the 1500-kDa Ubiquitin Conjugate-Degrading Complex

Judith Frydman, Alfred Goldberg

Proceedings of The National Academy of Sciences, 1992

View PDFchevron_right

Substrate selection by the proteasome during degradation of protein complexes

Andreas Matouschek

Nature chemical biology, 2009

View PDFchevron_right

Session 7: Ubiquitin Proteasomes

Ze'ev Ronai

Toxicologic Pathology, 2004

View PDFchevron_right

Direct Ubiquitin Independent Recognition and Degradation of a Folded Protein by the Eukaryotic Proteasomes-Origin of Intrinsic Degradation Signals

Amit Gautam

PloS one, 2022

View PDFchevron_right

The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag

Andrey Rozenberg

Nature Communications

View PDFchevron_right

Characterization of Two Polyubiquitin Binding Sites in the 26 S Protease Subunit 5a

Martin Rechsteiner

Journal of Biological Chemistry, 1998

View PDFchevron_right

The Proteasome and the Delicate Balance between Destruction and Rescue

Noam Adir

PLoS Biology, 2004

View PDFchevron_right

Ubiquitin Chains Are Remodeled at the Proteasome by Opposing Ubiquitin Ligase and Deubiquitinating Activities

John Hanna

Cell, 2006

View PDFchevron_right

Autoubiquitination of the 26S Proteasome on Rpn13 Regulates Breakdown of Ubiquitin Conjugates

Alfred Goldberg

The EMBO Journal, 2014

View PDFchevron_right

The ubiquitin-proteasome system

Anujith Kumar

Journal of Biosciences, 2006

View PDFchevron_right

Deubiquitination Reactions on the Proteasome for Proteasome Versatility

Nuoc Tran

International Journal of Molecular Sciences

View PDFchevron_right

Placing a Disrupted Degradation Motif at the C Terminus of Proteasome Substrates Attenuates Degradation without Impairing Ubiquitylation

Yuval Reiss

Journal of Biological Chemistry, 2013

View PDFchevron_right

Trimming of Ubiquitin Chains by Proteasome-associated Deubiquitinating Enzymes

John Hanna

Molecular & Cellular Proteomics, 2010

View PDFchevron_right

An unstructured initiation site is required for efficient proteasome-mediated degradation

LIN TIAN

Nature Structural & Molecular Biology, 2004

View PDFchevron_right

RETRACTED: ATP Hydrolysis-Dependent Disassembly of the 26S Proteasome Is Part of the Catalytic Cycle

Tione Buranda

Cell, 2005

View PDFchevron_right

Toward an integrated structural model of the 26S proteasome

S. Nickell

Molecular & cellular proteomics : MCP, 2010

View PDFchevron_right

ATP Hydrolysis-Dependent Disassembly of the 26S Proteasome Is Part of the Catalytic Cycle

Larry Sklar

Cell, 2005

View PDFchevron_right

The ubiquitin-proteasome pathway of intracellular proteolysis

Fergus Doherty

Essays in biochemistry, 2002

View PDFchevron_right

The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates

Kyle Kovary

The Journal of biological chemistry, 2013

View PDFchevron_right

Proteasome substrate degradation requires association plus extended peptide

Philip Coffino

The EMBO Journal, 2007

View PDFchevron_right

Role of Rpn11 metalloprotease in deubiquitination and degradation by the 26S proteasome

L Aravind

Science, 2002

View PDFchevron_right

Mutants of the deubiquitinating enzyme Ubp14 decipher pathway diversity of ubiquitin–proteasome linked protein degradation

Thorsten Pfirrmann

Biochemical and Biophysical Research Communications, 2006

View PDFchevron_right