Interactions of Hsp90 with histones and related peptides (Q73272057)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10597896 AND SRC:MED&resulttype=core&format=json

2 November 2019

title

Interactions of Hsp90 with histones and related peptides (English)

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2 November 2019

author name string

T Schnaider

1

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2 November 2019

J Oikarinen

2

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2 November 2019

H Ishiwatari-Hayasaka

3

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2 November 2019

I Yahara

4

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2 November 2019

P Csermely

5

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2 November 2019

language of work or name

English

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publication date

1 January 1999

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2 November 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10597896 AND SRC:MED&resulttype=core&format=json

2 November 2019

volume

65

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2 November 2019

issue

22

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2 November 2019

page(s)

2417-2426

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Molecular chaperones in cellular protein folding

2 November 2019

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The 90 kDa heat shock protein (hsp90) induces the condensation of the chromatin structure.

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Binding affinity of proteins to hsp90 correlates with both hydrophobicity and positive charges. A surface plasmon resonance study

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Interaction between casein kinase II and the 90-kDa stress protein, HSP90

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The ATP/ADP binding domains of actin are conserved in nucleosome complexed with histone H1 and high mobility group-17 protein

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Preferential condensation of SAR-DNA by histone H1 and its SPKK containing octapeptide repeat motif

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Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins

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Reversal of heparin inhibition of nuclear protein kinase NII by polyamines and histones

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Benzoquinoid ansamycins (herbimycin A and geldanamycin) interfere with the maturation of growth factor receptor tyrosine kinases

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7 January 2021

Identifiers

DOI

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2 November 2019

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