Insights into the function of Hsp70 chaperones.
Zylicz
M
M
Department of Molecular Biology, International Institute of Molecular and Cell Biology, UNESCO, Trojdena, Warsaw, Poland. zylicz@iimcb.gov.pl
Wawrzynow
A
A
D000251:Adenosine Triphosphatases / Q000502:physiology; D000818:Animals; D029968:Escherichia coli Proteins; D050886:HSP20 Heat-Shock Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology*; D006360:Heat-Shock Proteins / Q000502:physiology; D006801:Humans; D010750:Phosphoproteins / Q000502:physiology; D011485:Protein Binding; D017510:Protein Folding
D029968:Escherichia coli Proteins; D050886:HSP20 Heat-Shock Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; C494382:HSPB6 protein, human; D006360:Heat-Shock Proteins; D010750:Phosphoproteins; D000251:Adenosine Triphosphatases; C063842:dnaK protein, E coli