Bacterial GroEL-like heat shock protein 60 protects epithelial cells from stress-induced death through activation of ERK and inhibition of caspase 3. (Q40599695)

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scientific article published on January 2004

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English	Bacterial GroEL-like heat shock protein 60 protects epithelial cells from stress-induced death through activation of ERK and inhibition of caspase 3.	scientific article published on January 2004

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scholarly article

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Europe PubMed Central

21 September 2017

Bacterial GroEL-like heat shock protein 60 protects epithelial cells from stress-induced death through activation of ERK and inhibition of caspase 3. (English)

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Europe PubMed Central

21 September 2017

author name string

Liangxuan Zhang

1

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Europe PubMed Central

21 September 2017

Steven Pelech

2

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Europe PubMed Central

21 September 2017

Veli-Jukka Uitto

3

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Europe PubMed Central

21 September 2017

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publication date

1 January 2004

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Europe PubMed Central

21 September 2017

Experimental Cell Research

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Europe PubMed Central

21 September 2017

292

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Europe PubMed Central

21 September 2017

1

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Europe PubMed Central

21 September 2017

231-240

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Europe PubMed Central

21 September 2017

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Different heat shock protein 60 species share pro-inflammatory activity but not binding sites on macrophages

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Interleukin 15 induces the signals of epidermal proliferation through ERK and PI 3-kinase in a human epidermal keratinocyte cell line, HaCaT.

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MAP kinase pathways activated by stress: the p38 MAPK pathway

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HSP72 can protect cells from heat-induced apoptosis by accelerating the inactivation of stress kinase JNK.

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Hsp72 functions as a natural inhibitory protein of c-Jun N-terminal kinase

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Protein-damaging stresses activate c-Jun N-terminal kinase via inhibition of its dephosphorylation: a novel pathway controlled by HSP72.

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c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity

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Cross-reactivity of specific antibodies directed to heat shock proteins from periodontopathogenic bacteria and of human origin [corrected]

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UV-A-induced expression of GroEL in the UV-A-resistant marine cyanobacterium Oscillatoria sp. NKBG 091600.

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Bacterial heat shock protein-60 increases epithelial cell proliferation through the ERK1/2 MAP kinases

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Cisplatin and UV radiation induce activation of the stress-activated protein kinase p38gamma in human melanoma cells

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Ultraviolet B irradiation induces apoptosis of keratinocytes by direct activation of Fas antigen

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Role of caspases in dexamethasone-induced apoptosis and activation of c-Jun NH2-terminal kinase and p38 mitogen-activated protein kinase in human eosinophils

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Activation of stress-activated protein kinase/c-Jun NH2-terminal kinase and p38 kinase in calphostin C-induced apoptosis requires caspase-3-like proteases but is dispensable for cell death.

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An inhibitor of p38 and JNK MAP kinases prevents activation of caspase and apoptosis of cultured cerebellar granule neurons.

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p38 mitogen-activated protein kinase regulates a novel, caspase-independent pathway for the mitochondrial cytochrome c release in ultraviolet B radiation-induced apoptosis

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Mitochondria as regulators of apoptosis: doubt no more.

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Surface-associated hsp60 chaperonin of Legionella pneumophila mediates invasion in a HeLa cell model

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10.1016/J.YEXCR.2003.08.012

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Europe PubMed Central

21 September 2017

release_5mwdot223fg2zfmfac7te6smuy

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24 November 2022

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mapped directly with Wikidata item

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Europe PubMed Central

21 September 2017

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