Conformational remodeling of proteasomal substrates by PA700, the 19 S regulatory complex of the 26 S proteasome (Q43993763)

28 November 2017

Conformational remodeling of proteasomal substrates by PA700, the 19 S regulatory complex of the 26 S proteasome (English)

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28 November 2017

Chang-Wei Liu

1

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28 November 2017

Linda Millen

2

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28 November 2017

Tracie B Roman

3

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28 November 2017

Hai Xiong

4

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28 November 2017

Hiram F Gilbert

5

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28 November 2017

Robert Noiva

6

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28 November 2017

George N DeMartino

7

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28 November 2017

Philip J Thomas

8

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28 November 2017

language of work or name

English

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publication date

14 May 2002

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Journal of Biological Chemistry

28 November 2017

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28 November 2017

277

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28 November 2017

30

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28 November 2017

26815-26820

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https://api.crossref.org/works/10.1074%2FJBC.M201782200

28 November 2017

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Protein misfolding, evolution and disease

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Defective protein folding as a basis of human disease

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Posttranslational quality control: folding, refolding, and degrading proteins.

21 January 2018

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Structure of 20S proteasome from yeast at 2.4 A resolution

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https://api.crossref.org/works/10.1074%2FJBC.M201782200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Identification, purification, and characterization of a PA700-dependent activator of the proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

The proteasome: paradigm of a self-compartmentalizing protease

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

21 January 2018

1 reference

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The regulatory particle of the Saccharomyces cerevisiae proteasome.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

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.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M201782200

Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Ubiquitin-dependent protein degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Recognition of the polyubiquitin proteolytic signal

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Dynamics of substrate denaturation and translocation by the ClpXP degradation machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

The high molecular weight multicatalytic proteinase, macropain, exists in a latent form in human erythrocytes

21 January 2018

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The molecular chaperone Hsc70 assists the in vitro folding of the N-terminal nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator.

21 January 2018

1 reference

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Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

21 January 2018

1 reference

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pH-dependence of the dithiol-oxidizing activity of DsbA (a periplasmic protein thiol:disulphide oxidoreductase) and protein disulphide-isomerase: studies with a novel simple peptide substrate

21 January 2018

1 reference

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Reductive cleavage of disulfide bridges in ribonuclease

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction

21 January 2018

1 reference

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Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Protein unfolding and the energetics of protein translocation across biological membranes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Chaperonin function: folding by forced unfolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Selective degradation of oxidized calmodulin by the 20 S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Proteolysis of oxidised proteins and cellular senescence

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

A degradation signal located in the C-terminus of p21WAF1/CIP1 is a binding site for the C8 alpha-subunit of the 20S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

Degradation of oxidized proteins by the 20S proteasome.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M201782200

21 January 2018

Identifiers

DOI

10.1074/JBC.M201782200

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28 November 2017

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