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Biology of Extracellular HSP60
2019The exposure of cells or organisms to high temperature leads to the release of alert molecules such as Heat Shock Protein: the HSP. This protein family has been initially described in Drosophila. The cellular response to a heat shock involving HSP is conserved across species, from bacteria to humans and including plants.
Brice Nativel +5 more
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Molecular Chaperone Disorders: Defective Hsp60 in Neurodegeneration
Current Topics in Medicinal Chemistry, 2013Chaperonins, a subgroup of molecular chaperones, form ring-shaped structures and assist folding of proteins by enclosing them in their inner cavity. The mitochondrial Hsp60/Hsp10 chaperonin system is essential for cell viability and only a very small number of mutations causing human disease have so far been found that appear to selectively affect ...
Bross, Peter; id_orcid 0000-0001-9526-8525 +2 more
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Sequence homologies between hsp60 and autoantigens
Immunology Today, 1993The human heat shock protein (hsp) 60 shares sequence homology with a wide range of autoantigens including those of insulin dependent diabetes mellitus, Hashimoto's thyroiditis, glomerulonephritis, scleroderma, pemphigoid, rheumatoid arthritis, multiple sclerosis, chronic active hepatitis, primary biliary cirrhosis and Addison's disease.
D B, Jones, A F, Coulson, G W, Duff
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SERUM CONCENTRATIONS OF HSP60 AND ANTI-HSP60 IN PATIENTS WITH CEREBRAL ATHEROSCLEROSIS
2011INTRODUCTION In the pathogenesis of atherosclerosis both inflammatory and immune components seems to be involved (1). Serum concentrations of heat shock proteins Hsp60 and respective antibodies should contribute to the explanation of possible relationship between inflammation and immune response that could be assumed in development of cerebral ...
Galović Rengel, Ružica +3 more
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2019
?????????????????????? ?????????????????? ?????????????????????????????? ???????????? ?????????????????????????? ???????????????? Hsp60 ?? ?????????? ???????????? ?????? ?????????????????????????? ???????????????????????????? (????????). ???????????????? ???????????????????? ???????????? ?????????????????????????????? ???????????? Hsp60 ?????? ?? ??????
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?????????????????????? ?????????????????? ?????????????????????????????? ???????????? ?????????????????????????? ???????????????? Hsp60 ?? ?????????? ???????????? ?????? ?????????????????????????? ???????????????????????????? (????????). ???????????????? ???????????????????? ???????????? ?????????????????????????????? ???????????? Hsp60 ?????? ?? ??????
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2010
???????????????????? ?????????????????? ???????? HSP60 ???? ?????????? ???????? ?? ???????????????? ?????????????? ??????????????????, ???????????? ???? ?????????????????????? ???????????????????????????? (????????), ???? ???????????????? ???????????? ???????????????????????? ???? ?????????????? ?????????? ???? ?????????????????????????????????? ???????
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???????????????????? ?????????????????? ???????? HSP60 ???? ?????????? ???????? ?? ???????????????? ?????????????? ??????????????????, ???????????? ???? ?????????????????????? ???????????????????????????? (????????), ???? ???????????????? ???????????? ???????????????????????? ???? ?????????????? ?????????? ???? ?????????????????????????????????? ???????
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The multiple roles and therapeutic potential of HSP60 in cancer
Biochemical Pharmacology, 2022Songqing Fan, Qiuyuan Wen
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2019
???????????????????????? ?????????????? Hsp60 ?? ???????????? p70S6 (p70S6K) ?????????????????? ???????????? ???????????????????????????? ???????? ?? ?????????????????? ???????????????????? ?????????????????????????????????? ?? ???????????????? ????????????????????????????. ????????. ?????????????????????? ?????????????????????? ????????????????????????
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???????????????????????? ?????????????? Hsp60 ?? ???????????? p70S6 (p70S6K) ?????????????????? ???????????? ???????????????????????????? ???????? ?? ?????????????????? ???????????????????? ?????????????????????????????????? ?? ???????????????? ????????????????????????????. ????????. ?????????????????????? ?????????????????????? ????????????????????????
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2010
The main functional compartments of molecular chaperone Hsp60 are mitochondria and cytoplasm. Up to 30 % of Hsp60 are located in cytoplasm of cardiomyocytes. The interaction between molecular chaperone Hsp60 and proapoptotic Bax protein in the cytoplasmic fraction from normal human heart tissue has been revealed by co-immunoprecipitation in contrast to
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The main functional compartments of molecular chaperone Hsp60 are mitochondria and cytoplasm. Up to 30 % of Hsp60 are located in cytoplasm of cardiomyocytes. The interaction between molecular chaperone Hsp60 and proapoptotic Bax protein in the cytoplasmic fraction from normal human heart tissue has been revealed by co-immunoprecipitation in contrast to
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Codon usage patterns and evolution of HSP60 in birds
International Journal of Biological Macromolecules, 2021Hengwu Ding, Xianzhao Kan
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