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July 1, 1999Journal of Biological ChemistryOpen Access

Regulation of Hsp27 Oligomerization, Chaperone Function, and Protective Activity against Oxidative Stress/Tumor Necrosis Factor α by Phosphorylation

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Authors

TRThorsten RogallaMax Delbrück CenterMEMonika EhrnspergerUniversity of RegensburgXPXavier PrévilleUniversité Claude Bernard Lyon 1

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Rogalla et al. (1999) studied this question.

synapsesocial.com/papers/69da23af8988aeabbe686993https://doi.org/10.1074/jbc.274.27.18947
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Distinct effects of heat shock and ATP depletion on distribution and isoform patterns of human Hsp27 in endothelial cells1996 · 57 citations
  2. 2Constitutive expression of human hsp27, Drosophila hsp27, or human alpha B-crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts.1995 · 338 citations
  3. 3The apparent molecular size of native α‐crystallin B in non‐lenticular tissues1990 · 29 citations
  4. 4Structure and in Vitro Molecular Chaperone Activity of Cytosolic Small Heat Shock Proteins from Pea1995 · 321 citations
  5. 5Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp271994 · 249 citations