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pro vyhledávání: '"Ludewig, M H"'
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 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
Akademický článek
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