Unique proteasome subunit Xrpn10c is a specific receptor for the antiapoptotic ubiquitin-like protein Scythe (Q48109396)

8 February 2018

title

Unique proteasome subunit Xrpn10c is a specific receptor for the antiapoptotic ubiquitin-like protein Scythe (English)

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8 February 2018

author name string

Yuhsuke Kikukawa

1

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8 February 2018

Ryosuke Minami

2

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8 February 2018

Masumi Shimada

3

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8 February 2018

Masami Kobayashi

4

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8 February 2018

Keiji Tanaka

5

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8 February 2018

Hideyoshi Yokosawa

6

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8 February 2018

Hiroyuki Kawahara

7

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8 February 2018

language of work or name

English

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publication date

1 December 2005

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8 February 2018

published in

FEBS Journal

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8 February 2018

volume

272

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8 February 2018

issue

24

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8 February 2018

page(s)

6373-6386

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8 February 2018

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

1 reference

A superfamily of protein tags: ubiquitin, SUMO and related modifiers

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1 reference

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The proteasome: paradigm of a self-compartmentalizing protease

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1 reference

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The proteasome, a novel protease regulated by multiple mechanisms

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1 reference

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The 26S proteasome: a molecular machine designed for controlled proteolysis

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Proteasomes and their kin: proteases in the machine age

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1 reference

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Molecular biology of the proteasome

21 January 2018

1 reference

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

21 January 2018

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https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

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/10.1111%2FJ.1742-4658.2005.05032.X

Proteins containing the UBA domain are able to bind to multi-ubiquitin chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

Characterization of two polyubiquitin binding sites in the 26 S protease subunit 5a

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

A ubiquitin-interacting motif conserved in components of the proteasomal and lysosomal protein degradation systems

21 January 2018

1 reference

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Rad23 links DNA repair to the ubiquitin/proteasome pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

Developmentally regulated, alternative splicing of the Rpn10 gene generates multiple forms of 26S proteasomes

21 January 2018

1 reference

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The cell-death machine

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Programmed cell death during Xenopus development: a spatio-temporal analysis

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Identification of XDRP1; a Xenopus protein related to yeast Dsk2p binds to the N-terminus of cyclin A and inhibits its degradation

21 January 2018

1 reference

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Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

Proteasome subunit Rpn1 binds ubiquitin-like protein domains

21 January 2018

1 reference

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Cloning and functional analysis of BAG-1: a novel Bcl-2-binding protein with anti-cell death activity

21 January 2018

1 reference

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Molecular chaperone targeting and regulation by BAG family proteins

21 January 2018

1 reference

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BAG-1 modulates the chaperone activity of Hsp70/Hsc70.

21 January 2018

1 reference

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The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome

21 January 2018

1 reference

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CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

Protein turnover: a CHIP programmed for proteolysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

Simultaneous binding of PA28 and PA700 activators to 20 S proteasomes

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FJ.1742-4658.2005.05032.X

10.1111/J.1742-4658.2005.05032.X

21 January 2018

Identifiers

DOI

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8 February 2018

1 reference

8 February 2018