Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites. (Q46891027)

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27 December 2019

title

Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites (English)

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27 December 2019

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6

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Jeroen Roelofs

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27 December 2019

Michael H Glickman

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27 December 2019

author name string

Maurits F Kleijnen

1

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27 December 2019

Soyeon Park

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27 December 2019

Nathaniel A Hathaway

4

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Daniel Finley

7

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publication date

18 November 2007

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Nature Structural & Molecular Biology

27 December 2019

published in

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volume

14

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27 December 2019

page(s)

1180-1188

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27 December 2019

issue

12

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https://scigraph.springernature.com/pub.10.1038/nsmb1335

27 December 2019

exact match

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cites work

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31 March 2020

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31 March 2020

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31 March 2020

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Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity

31 March 2020

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Activity probe for in vivo profiling of the specificity of proteasome inhibitor bortezomib

31 March 2020

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Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly

31 March 2020

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Communication between ClpX and ClpP during substrate processing and degradation

31 March 2020

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

31 March 2020

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Characterization of the proteasome using native gel electrophoresis

31 March 2020

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Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms

31 March 2020

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Identification of the yeast 20S proteasome catalytic centers and subunit interactions required for active-site formation

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB1335

1 reference

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27 December 2019

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