Results 271 to 280 of about 111,857 (291)
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Molecular dissection of amyloid disaggregation by human HSP70
Nature, 2020A. Wentink +8 more
semanticscholar +1 more source
1997
Abstract Grp 75 (Mizzen et al., 1989); P71 (Leustek et al., 1989); Pbp74 (Domanico et al., 1993); C3H strain specific antigen (CSA) (Michikawa et al., 1993); mortalin (Wadhwa et al., 1993) ;mthsp75 (Bhattacharyya etal., 1995).
Hoogenraad, Nicholas J. +3 more
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Abstract Grp 75 (Mizzen et al., 1989); P71 (Leustek et al., 1989); Pbp74 (Domanico et al., 1993); C3H strain specific antigen (CSA) (Michikawa et al., 1993); mortalin (Wadhwa et al., 1993) ;mthsp75 (Bhattacharyya etal., 1995).
Hoogenraad, Nicholas J. +3 more
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HSP40 proteins use class-specific regulation to drive HSP70 functional diversity
Nature, 2020Ofrah Faust +7 more
semanticscholar +1 more source
1994
Abstract The four SSA genes are regulated differently in response to stress and growth state. SSA1 is constitutively expressed as well as being stress-inducible, while SSA2 is constitutive and not ostensibly affected by stress. SSA3 and SSA4 are “classic” heat shock genes whose expression is stress dependent.
R J Nelson, E Craig
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Abstract The four SSA genes are regulated differently in response to stress and growth state. SSA1 is constitutively expressed as well as being stress-inducible, while SSA2 is constitutive and not ostensibly affected by stress. SSA3 and SSA4 are “classic” heat shock genes whose expression is stress dependent.
R J Nelson, E Craig
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Hsp70 proteins in protein translocation
2001Publisher Summary Hsp70 proteins are essential components of the protein translocation systems of the endoplasmic reticulum (ER) and mitochondria. The role of Hsp70s in protein translocation is not confined to the ER and mitochondria. For most proteins of the ER, translocation is coupled with protein synthesis.
Ryan, Michael T., Pfanner, Nikolaus
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2021
Results of the Western-Blot-analysis of heat shock protein 70 kDa (Hsp70) in leaves of 8 species of plants from 7 angiosperm families, different in their ecology, are presented. The tested plants were affected by water deficit, flooding and heat stress under natural or experimental conditions.
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Results of the Western-Blot-analysis of heat shock protein 70 kDa (Hsp70) in leaves of 8 species of plants from 7 angiosperm families, different in their ecology, are presented. The tested plants were affected by water deficit, flooding and heat stress under natural or experimental conditions.
openaire +1 more source
1997
Abstract Fish Hsp70s were originally identified as proteins induced in cultured fish cells by exposure to heat, heavy metal ions or sodium arsenite. Initial biochemical characterizations were done using denaturing polyacrylamide gel electrophoresis (Heikkila et al., 1982; Kothary, Candido, 1982).
L E Hightower, J A Ryan, C E Norris
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Abstract Fish Hsp70s were originally identified as proteins induced in cultured fish cells by exposure to heat, heavy metal ions or sodium arsenite. Initial biochemical characterizations were done using denaturing polyacrylamide gel electrophoresis (Heikkila et al., 1982; Kothary, Candido, 1982).
L E Hightower, J A Ryan, C E Norris
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Science's STKE, 2002
The ability of invariant molecular structures derived from foreign agents to activate the innate immune system through the Toll-like receptor (TLR) pathway is well established. A theory that is emerging is that the innate immune system may also be activated by endogenous ligands released from cells during necrotic cell death, thus ...
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The ability of invariant molecular structures derived from foreign agents to activate the innate immune system through the Toll-like receptor (TLR) pathway is well established. A theory that is emerging is that the innate immune system may also be activated by endogenous ligands released from cells during necrotic cell death, thus ...
openaire +2 more sources
2018
The highly abundant and evolutionary conserved Hsp70 chaperones are central components of the cellular protein quality control system, surveilling the folding status of cellular proteins from birth at the ribosome to death through degradation. To no other chaperone families, more different functions have been assigned, and it is not surprising that ...
Roman Kityk, Matthias P. Mayer
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The highly abundant and evolutionary conserved Hsp70 chaperones are central components of the cellular protein quality control system, surveilling the folding status of cellular proteins from birth at the ribosome to death through degradation. To no other chaperone families, more different functions have been assigned, and it is not surprising that ...
Roman Kityk, Matthias P. Mayer
openaire +1 more source
2019
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