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Organelle-specific Hsp90 inhibitors
Archives of Pharmacal Research, 2015Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that is involved in the folding, activation, and stabilization of numerous oncogenic proteins. It has become an attractive therapeutic target, especially for eradicating malignant cancers and overcoming chemotherapy resistance.
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Hsp90 and Developmental Networks
2007The most abundant cytoplasmic chaperone of eukaryotic cells, Hsp90 is a hub in developmental regulatory networks and the first example described of the phenomenon of molecular buffering. As a chaperone for many different signaling proteins, Hsp90 maintains the clarity and strength of communication within and between cells, concealing developmental and ...
Suzannah, Rutherford +2 more
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1997
Abstract Nucleotide sequence analysis of plant hsp90 genes (GenBank accession numbers M36960, M96549, M99431) predicts a molecular mass between 80, 82 kDa,, pls of 5.73, 5.76 in two cases, for the encoded proteins (Conner et al., 1990; Felsheim, Das, 1992; Koning et al., 1992; Takahashi et al., 1992; Marrs et al., 1993; Yabe et al., 1994)
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Abstract Nucleotide sequence analysis of plant hsp90 genes (GenBank accession numbers M36960, M96549, M99431) predicts a molecular mass between 80, 82 kDa,, pls of 5.73, 5.76 in two cases, for the encoded proteins (Conner et al., 1990; Felsheim, Das, 1992; Koning et al., 1992; Takahashi et al., 1992; Marrs et al., 1993; Yabe et al., 1994)
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2017
Bacterial Hsp90 is an ATP-dependent molecular chaperone involved in protein remodeling and activation. The E. coli Hsp90, Hsp90Ec, collaborates in protein remodeling with another ATP-dependent chaperone, DnaK, the E. coli Hsp70. Both Hsp90Ec and DnaK hydrolyze ATP and client (substrate) proteins stimulate the hydrolysis. Additionally, ATP hydrolysis by
Joel R, Hoskins +2 more
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Bacterial Hsp90 is an ATP-dependent molecular chaperone involved in protein remodeling and activation. The E. coli Hsp90, Hsp90Ec, collaborates in protein remodeling with another ATP-dependent chaperone, DnaK, the E. coli Hsp70. Both Hsp90Ec and DnaK hydrolyze ATP and client (substrate) proteins stimulate the hydrolysis. Additionally, ATP hydrolysis by
Joel R, Hoskins +2 more
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2012
Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential role in many cellular processes including cell cycle control, cell survival, hormone and other signalling pathways. It is important for the cell's response to stress and is a key player in maintaining cellular homeostasis. In the last ten years, it has become a major
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Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential role in many cellular processes including cell cycle control, cell survival, hormone and other signalling pathways. It is important for the cell's response to stress and is a key player in maintaining cellular homeostasis. In the last ten years, it has become a major
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Hsp90 as a capacitor for morphological evolution
Nature, 1998S. Rutherford, S. Lindquist
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HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Nature reviews. Molecular cell biology, 2010Mikko Taipale +2 more
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2010
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??i??????i????i ????i???? ??i????i?? ?????????????????? ???????? Hsp70 ???? Hsp90 ?? ??????????i?? ????????????????i?? ???????????? ???? ???????????????????????? ??i?? ??i??????????????i??????i?? (3, 7, 10 i 14g) ?????????????? ?? ?????????????????????????? ??????????????-????????-????????i????. ???????????????? ??????????i ????i???? ?? ??i????i ??????
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