NblA, a key protein of phycobilisome degradation, interacts with ClpC, a HSP100 chaperone partner of a cyanobacterial Clp protease (Q42598626)

3 November 2017

title

NblA, a key protein of phycobilisome degradation, interacts with ClpC, a HSP100 chaperone partner of a cyanobacterial Clp protease (English)

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3 November 2017

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Anne Karradt

1

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3 November 2017

Johanna Sobanski

2

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3 November 2017

Jens Mattow

3

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3 November 2017

Wolfgang Lockau

4

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3 November 2017

Kerstin Baier

5

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3 November 2017

language of work or name

English

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publication date

25 September 2008

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Journal of Biological Chemistry

3 November 2017

published in

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3 November 2017

volume

283

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3 November 2017

issue

47

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3 November 2017

page(s)

32394-32403

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Phycobilisomes: structure and dynamics

3 November 2017

cites work

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The structure of ClpP at 2.3 A resolution suggests a model for ATP-dependent proteolysis

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Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease

21 January 2018

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21 January 2018

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ClpS, a substrate modulator of the ClpAP machine

21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Analysis of a Het- mutation in Anabaena sp. strain PCC 7120 implicates a secondary metabolite in the regulation of heterocyst spacing

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.M805823200

1 reference

release_y6v4mn2fdvdvvidyh45agvqt4a

3 November 2017

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/y6v4mn2fdvdvvidyh45agvqt4a

mapped directly with Wikidata item

24 November 2022

based on heuristic

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