Multiubiquitin chain binding and protein degradation are mediated by distinct domains within the 26 S proteasome subunit Mcb1. (Q38340703)

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8 November 2019

title

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

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8 November 2019

4

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8 November 2019

author name string

H Fu

1

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8 November 2019

S Sadis

2

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8 November 2019

D M Rubin

3

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8 November 2019

S van Nocker

5

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8 November 2019

D Finley

6

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8 November 2019

R D Vierstra

7

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8 November 2019

language of work or name

English

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publication date

1 January 1998

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Journal of Biological Chemistry

8 November 2019

published in

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8 November 2019

volume

273

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8 November 2019

issue

4

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8 November 2019

page(s)

1970-1981

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The ubiquitin-proteasome proteolytic pathway

8 November 2019

cites work

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Protein translocation channels in the proteasome and other proteases

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

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Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain

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A ubiquitin mutant with specific defects in DNA repair and multiubiquitination

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A proteolytic pathway that recognizes ubiquitin as a degradation signal

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

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

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Structure of 20S proteasome from yeast at 2.4 A resolution

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Proteolysis: The proteasome: a protein-degrading organelle?

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Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome

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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

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Molecular Cloning and Expression of a Pituitary Gland Protein Modulating Intestinal Fluid Secretion

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Molecular cloning and expression of a multiubiquitin chain binding subunit of the human 26S protease

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Yeast counterparts of subunits S5a and p58 (S3) of the human 26S proteasome are encoded by two multicopy suppressors of nin1-1

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Cloning and Sequencing a Non-ATPase Subunit of the Regulatory Complex of the Drosophila 26S Protease

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Mapping the ubiquitin‐binding domains in the p54 regulatory complex subunit of the Drosophila 26S protease

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Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting

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Inhibition of ubiquitin-mediated proteolysis by the Arabidopsis 26 S protease subunit S5a.

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Structure of tetraubiquitin shows how multiubiquitin chains can be formed

21 January 2018

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Novel Regulation of the Helix-Loop-Helix Protein Id1 by S5a, a Subunit of the 26 S Proteasome

21 January 2018

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p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins

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