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pro vyhledávání: '"Blatch, G L"'
publisher version
The Hsp70/Hsp90 organising protein (HOP) is a co-chaperone essential for client protein transfer from Hsp70 to Hsp90 within the Hsp90 chaperone machine. Although HOP is upregulated in various cancers, there is limited informati
The Hsp70/Hsp90 organising protein (HOP) is a co-chaperone essential for client protein transfer from Hsp70 to Hsp90 within the Hsp90 chaperone machine. Although HOP is upregulated in various cancers, there is limited informati
Externí odkaz:
http://hdl.handle.net/10962/66278
publisher version
Plasmodium falciparum, the human pathogen responsible for the most dangerous malaria infection, survives and develops in mature erythrocytes through the export of proteins needed for remodelling of the host cell. Molecular chap
Plasmodium falciparum, the human pathogen responsible for the most dangerous malaria infection, survives and develops in mature erythrocytes through the export of proteins needed for remodelling of the host cell. Molecular chap
Externí odkaz:
http://hdl.handle.net/10962/66098
publisher version
The heat shock protein 40 (Hsp40/DNAJ) family of co-chaperones modulates the activity of the major molecular chaperone heat shock protein 70 (Hsp70) protein group. Hsp40 stimulates the basal ATPase activity of Hsp70 and hence r
The heat shock protein 40 (Hsp40/DNAJ) family of co-chaperones modulates the activity of the major molecular chaperone heat shock protein 70 (Hsp70) protein group. Hsp40 stimulates the basal ATPase activity of Hsp70 and hence r
Externí odkaz:
http://hdl.handle.net/10962/66335
Autor:
Nyakundi, David O, Vuko, Loyiso A M, Bentley, Stephen J, Hoppe, Heinrich C, Blatch, G L, Boshoff, Aileen
publisher version
The majority of mitochondrial proteins are encoded in the nucleus and need to be imported from the cytosol into the mitochondria, and molecular chaperones play a key role in the efficient translocation and proper folding of the
The majority of mitochondrial proteins are encoded in the nucleus and need to be imported from the cytosol into the mitochondria, and molecular chaperones play a key role in the efficient translocation and proper folding of the
Externí odkaz:
http://hdl.handle.net/10962/66109
Plasmodium falciparum 70 kDa heat shock proteins (PfHsp70s) are expressed at all stages of the pathogenic erythrocytic phase of the malaria parasite lifecycle. There are six PfHsp70s,all of which have orthologues in other plasmodial species, except f
Externí odkaz:
http://hdl.handle.net/10962/d1007081
It is becoming increasingly apparent that heat shock proteins play an important role in the survival of Plasmodium falciparum against temperature changes associated with its passage from the cold-blooded mosquito vector to the warm-blooded human host
Externí odkaz:
http://hdl.handle.net/10962/d1006269
Autor:
Nicoll, W S, Botha, M, McNamara, C, Schlange, M, Pesce, E R, Boshoff, A, Ludewig, M H, Zimmerman, R, Cheetham, M E, Chapple, J P, Blatch, G L
Both prokaryotic and eukaryotic cells contain multiple heat shock protein 40 (Hsp40) and heat shock protein 70 (Hsp70) proteins, which cooperate as molecular chaperones to ensure fidelity at all stages of protein biogenesis. The Hsp40 signature domai
Externí odkaz:
http://hdl.handle.net/10962/d1006261
http://www.sciencedirect.com/science/article/pii/S1357272506003268
http://www.sciencedirect.com/science/article/pii/S1357272506003268
The discovery of the African coelacanth in 1938 and subsequently the Indonesian coelacanth in 1998 has resulted in a keen interest in molecular studies on the coelacanth. A major focus has been on the phylogenetic position of the coelacanth. Lobe-fin
Externí odkaz:
http://hdl.handle.net/10962/d1005795
The process of assisted protein folding, characteristic of members of the heat shock protein 70 (Hsp70) and heat shock protein 40 (Hsp40) molecular chaperone families, is important for maintaining the structural integrity of cellular protein machiner
Externí odkaz:
http://hdl.handle.net/10962/d1005794
Autor:
Boshoff, A, Nicoll, W S, Hennessy, F, Ludewig, M H, Daniel, S, Modisakeng, K W, Shonhai, A, McNamara, C, Bradley, G, Blatch, G L
Molecular chaperones consist of several highly conserved families of proteins, many of which consist of heat shock proteins. The primary function of molecular chaperones is to facilitate the folding or refolding of proteins, and therefore they play a
Externí odkaz:
http://hdl.handle.net/10962/d1004479