Minimal protein-folding systems in hyperthermophilic archaea (Q35697547)

9 August 2017

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title

Minimal protein-folding systems in hyperthermophilic archaea (English)

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9 August 2017

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Frank T Robb

3

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author name string

Pongpan Laksanalamai

series ordinal

1

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9 August 2017

Timothy A Whitehead

series ordinal

2

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9 August 2017

language of work or name

English

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publication date

1 April 2004

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Nature Reviews Microbiology

9 August 2017

published in

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9 August 2017

volume

2

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9 August 2017

issue

4

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9 August 2017

page(s)

315-324

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The composition, structure and stability of a group II chaperonin are temperature regulated in a hyperthermophilic archaeon

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Alpha-crystallin can function as a molecular chaperone

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Multi-subunit assembly of the Pyrococcus furiosus small heat shock protein is essential for cellular protection at high temperature

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31 March 2020

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Repair of extensive ionizing-radiation DNA damage at 95 degrees C in the hyperthermophilic archaeon Pyrococcus furiosus

31 March 2020

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The Last Universal Common Ancestor (LUCA), Simple or Complex?

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Sequence analysis of the AAA protein family

31 March 2020

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Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin

31 March 2020

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Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins

31 March 2020

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Discontinuous occurrence of the hsp70 (dnaK) gene among Archaea and sequence features of HSP70 suggest a novel outlook on phylogenies inferred from this protein.

31 March 2020

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inferred from DOI database lookup

7 January 2021

based on heuristic

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO866

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NRMICRO866

1 reference

9 August 2017

1 reference