ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle (Q27930959)

Dataset for "Continued use of retracted papers: Temporal trends in citations and (lack of) awareness of retractions shown in citation contexts in biomedicine"

1 December 2016

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Continued use of retracted papers: Temporal trends in citations and (lack of) awareness of retractions shown in citation contexts in biomedicine

title

ATP hydrolysis-dependent disassembly of the 26S proteasome is part of the catalytic cycle (English)

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PubMed

retrieved

1 December 2016

author

Hediye Erdjument-Bromage

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Larry A Sklar

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Tione Buranda

object named as

Tione Buranda

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author name string

Shalon E Babbitt

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Alexi Kiss

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Andrew E Deffenbaugh

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Yie-Hwa Chang

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Eric Bailly

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Jennifer Baumler

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Edward Gogol

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Dorota Skowyra

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language of work or name

English

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publication date

20 May 2005

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1 reference

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

retrieved

1 December 2016

volume

121

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issue

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page(s)

553-65

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cites work

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9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

A cryptic protease couples deubiquitination and degradation by the proteasome

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

UFD4 lacking the proteasome-binding region catalyses ubiquitination but is impaired in proteolysis

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9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

The base of the proteasome regulatory particle exhibits chaperone-like activity

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9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

A gated channel into the proteasome core particle

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9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Recruitment of a 19S proteasome subcomplex to an activated promoter

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9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Nanoenzymology of the 20S proteasome: proteasomal actions are controlled by the allosteric transition

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Cyclin-dependent kinase and Cks/Suc1 interact with the proteasome in yeast to control proteolysis of M-phase targets

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Multiple associated proteins regulate proteasome structure and function

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9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Structural basis for the activation of 20S proteasomes by 11S regulators

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

The caspase-like sites of proteasomes, their substrate specificity, new inhibitors and substrates, and allosteric interactions with the trypsin-like sites.

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II.

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

26 S proteasomes function as stable entities

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9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

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

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Selective degradation of ubiquitinated Sic1 by purified 26S proteasome yields active S phase cyclin-Cdk

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9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

ATP-dependent incorporation of 20S protease into the 26S complex that degrades proteins conjugated to ubiquitin

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Functional organization of the yeast proteome by systematic analysis of protein complexes

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Structure of 20S proteasome from yeast at 2.4 A resolution

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Formation of proteasome-PA700 complexes directly correlates with activation of peptidase activity

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

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

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Recognition of the polyubiquitin proteolytic signal

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Release of ubiquitin-charged Cdc34-S - Ub from the RING domain is essential for ubiquitination of the SCF(Cdc4)-bound substrate Sic1.

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Physical association of ubiquitin ligases and the 26S proteasome

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Proteasomes and their kin: proteases in the machine age

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Two-substrate association with the 20S proteasome at single-molecule level

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Isolation and mass spectrometry of transcription factor complexes

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

The 19S complex of the proteasome regulates nucleotide excision repair in yeast.

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Effects of nucleotides on assembly of the 26S proteasome and degradation of ubiquitin conjugates

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

The axial channel of the proteasome core particle is gated by the Rpt2 ATPase and controls both substrate entry and product release

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3.

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system

1 reference

9 February 2024

https://opencitations.net/index/api/v1/references/10.1016/J.CELL.2005.03.028

Identifiers

DOI

10.1016/J.CELL.2005.03.028

0 references

1 reference

stated in

PubMed