(Q42805708)

English

Inhibition of colony formation of NIH 3T3 cells by the expression of the small molecular weight heat shock protein HSP27: involvement of its phosphorylation and aggregation at the C-terminal region

scientific article published on January 1997

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

Inhibition of colony formation of NIH 3T3 cells by the expression of the small molecular weight heat shock protein HSP27: involvement of its phosphorylation and aggregation at the C-terminal region (English)

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

phosphorylation

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based on heuristic

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author name string

Arata S

1

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

Hamaguchi S

2

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

Nose K

3

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

language of work or name

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based on heuristic

inferred from title

publication date

1 January 1997

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

Journal of Cellular Physiology

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Europe PubMed Central

PubMed publication ID

7 November 2017

170

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Europe PubMed Central

PubMed publication ID

7 November 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

19-26

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

Effects of the overexpression of the small heat shock protein, HSP27, on the sensitivity of human fibroblast cells exposed to oxidative stress

1 reference

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Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein

1 reference

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Biological and clinical implications of heat shock protein 27,000 (Hsp27): a review

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Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27.

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Protein folding in the cell

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Characterization of 45-kDa/54-kDa HSP27 kinase, a stress-sensitive kinase which may activate the phosphorylation-dependent protective function of mammalian 27-kDa heat-shock protein HSP27.

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Phosphorylation of HSP27 during development and decay of thermotolerance in Chinese hamster cells

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Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27

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Cytoskeleton--plasma membrane interactions

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Analysis of the resistance to heat and hydrogen peroxide stresses in COS cells transiently expressing wild type or deletion mutants of the Drosophila 27-kDa heat-shock protein

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The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein

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Phosphorylation of the stress protein hsp27 is an early event in murine myelomonocytic leukemic cell differentiation induced by leukemia inhibitory factor/D-factor

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Variation in the expression and/or phosphorylation of the human low molecular weight stress protein during in vitro cell differentiation

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A 25-kD inhibitor of actin polymerization is a low molecular mass heat shock protein

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Tissue-specific expression of the heat shock protein HSP27 during Drosophila melanogaster development

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Phosphorylation of the small heat-shock protein is regulated by interleukin 1, tumour necrosis factor, growth factors, bradykinin and ATP.

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Expression of heat shock genes during differentiation of mammalian osteoblasts and promyelocytic leukemia cells

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Identifiers

10.1002/(SICI)1097-4652(199701)170:1<19::AID-JCP3>3.0.CO;2-O

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

7 November 2017

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