The size of the proteasomal substrate determines whether its degradation will be mediated by mono- or polyubiquitylation (Q46223379)

20 December 2017

title

The size of the proteasomal substrate determines whether its degradation will be mediated by mono- or polyubiquitylation (English)

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20 December 2017

10

Aaron Ciechanover

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20 December 2017

7

Hilal A Lashuel

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20 December 2017

5

Mahmood Haj-Yahya

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20 December 2017

Yifat Herman-Bachinsky

2

object named as

Yifat Herman-Bachinsky

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20 December 2017

Mirva Hejjaoui

6

object named as

Mirva Hejjaoui

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20 December 2017

Ashraf Brik

9

object named as

Ashraf Brik

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20 December 2017

author name string

Nitzan Shabek

1

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20 December 2017

Samuel Buchsbaum

3

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20 December 2017

Oded Lewinson

4

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20 December 2017

Thomas Sommer

8

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20 December 2017

publication date

16 August 2012

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20 December 2017

published in

Molecular Cell

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20 December 2017

volume

48

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20 December 2017

issue

1

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20 December 2017

page(s)

87-97

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20 December 2017

Occurrence of a polyubiquitin structure in ubiquitin-protein conjugates

cites work

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Regulation of Pax3 by proteasomal degradation of monoubiquitinated protein in skeletal muscle progenitors

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

What genetics tells us about the causes and mechanisms of Parkinson's disease

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Ubiquitin as a degradation signal

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Non-canonical Wnt signaling induces ubiquitination and degradation of Syndecan4

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Proteasome subunit Rpn13 is a novel ubiquitin receptor

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Cell cycle: reaching for a role for the Cks proteins

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Recognition of the polyubiquitin proteolytic signal

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Proteome half-life dynamics in living human cells

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Dependence of phospholipase D1 multi-monoubiquitination on its enzymatic activity and palmitoylation

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Short-lived green fluorescent proteins for quantifying ubiquitin/proteasome-dependent proteolysis in living cells

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Proteasome substrate degradation requires association plus extended peptide

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

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

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

α-Synuclein fate is determined by USP9X-regulated monoubiquitination

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Recognition and processing of ubiquitin-protein conjugates by the proteasome

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Expeditious chemical synthesis of ubiquitinated peptides employing orthogonal protection and native chemical ligation

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

E3 ligase Rad18 promotes monoubiquitination rather than ubiquitin chain formation by E2 enzyme Rad6

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Rad23 escapes degradation because it lacks a proteasome initiation region

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

The Polycomb Protein Ring1B Generates Self Atypical Mixed Ubiquitin Chains Required for Its In Vitro Histone H2A Ligase Activity

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Modification by single ubiquitin moieties rather than polyubiquitination is sufficient for proteasomal processing of the p105 NF-kappaB precursor.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Protein regulation by monoubiquitin

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Methotrexate inhibits proteolysis of dihydrofolate reductase by the N-end rule pathway.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Ubiquitin ligase Nedd4 promotes alpha-synuclein degradation by the endosomal-lysosomal pathway

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Degradation of Monoubiquitinated .alpha.-Globin by 26S Proteasomes

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Degradation of ubiquitin: the fate of the cellular reaper

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Complete subunit architecture of the proteasome regulatory particle

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in Alzheimer's and Down patients

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Minimal length requirement for proteasomal degradation of ubiquitin-dependent substrates

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Towards elucidation of the role of ubiquitination in the pathogenesis of Parkinson's disease with semisynthetic ubiquitinated α-synuclein

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Ferroportin-mediated mobilization of ferritin iron precedes ferritin degradation by the proteasome

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Protein degradation: recognition of ubiquitinylated substrates

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Cyclin-dependent kinase subunit (Cks) 1 or Cks2 overexpression overrides the DNA damage response barrier triggered by activated oncoproteins

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Ubiquitin degradation with its substrate, or as a monomer in a ubiquitination-independent mode, provides clues to proteasome regulation

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Role of the alpha-amino group of protein in ubiquitin-mediated protein breakdown

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Ubiquitin is degraded by the ubiquitin system as a monomer and as part of its conjugated target.

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Defining the geometry of the two-component proteasome degron

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

NORF5/HUG1 is a component of the MEC1-mediated checkpoint response to DNA damage and replication arrest in Saccharomyces cerevisiae

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Degradation of alpha-synuclein by proteasome

1 reference

11 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/J.MOLCEL.2012.07.011

Identifiers

DOI

10.1016/J.MOLCEL.2012.07.011

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20 December 2017

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20 December 2017