(Q84612681)

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Characterization of Xanthomonas campestris pv. campestris heat shock protein A (HspA), which possesses an intrinsic ability to reactivate inactivated proteins

scientific article published on July 29, 2010

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20668846%20AND%20SRC:MED&resulttype=core&format=json

8 February 2020

Characterization of Xanthomonas campestris pv. campestris heat shock protein A (HspA), which possesses an intrinsic ability to reactivate inactivated proteins (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20668846%20AND%20SRC:MED&resulttype=core&format=json

8 February 2020

Xanthomonas campestris

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Xanthomonas campestris

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Ching-Hsuan Lin

1

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8 February 2020

Chia-Ni Lee

2

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8 February 2020

Juey-Wen Lin

3

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8 February 2020

Wan-Ju Tsai

4

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8 February 2020

Szu-Wen Wang

5

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8 February 2020

Shu-Fen Weng

6

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8 February 2020

Yi-Hsiung Tseng

7

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8 February 2020

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29 July 2010

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8 February 2020

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http://link.springer.com/content/pdf/10.1007/s00253-010-2776-z.pdf

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10.1007/S00253-010-2776-Z

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12 June 2024

http://link.springer.com/article/10.1007/s00253-010-2776-z/fulltext.html

1 reference

10.1007/S00253-010-2776-Z

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12 June 2024

http://link.springer.com/content/pdf/10.1007/s00253-010-2776-z

1 reference

10.1007/S00253-010-2776-Z

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Applied Microbiology and Biotechnology

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8 February 2020

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8 February 2020

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8 February 2020

699-709

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8 February 2020

https://scigraph.springernature.com/pub.10.1007/s00253-010-2776-z

0 references

The identity of proteins associated with a small heat shock protein during heat stress in vivo indicates that these chaperones protect a wide range of cellular functions

1

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Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

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Changes in oligomerization are essential for the chaperone activity of a small heat shock protein in vivo and in vitro

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Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisite for chaperone-like activity

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The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure

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Small heat-shock protein structures reveal a continuum from symmetric to variable assemblies

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Activation mechanism of HSP16.5 from Methanococcus jannaschii

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Transient expression and heat-stress-induced co-aggregation of endogenous and heterologous small heat-stress proteins in tobacco protoplasts.

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831

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HD Schweizer

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1993

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