title: Hsp70 structure, function, regulation and influence on yeast prions.
abstract: Heat shock proteins protect cells from various conditions of stress. Hsp70, the most ubiquitous and highly conserved Hsp, helps proteins adopt native conformation or regain function after misfolding. Various co-chaperones specify Hsp70 function and broaden its substrate range. We discuss Hsp70 structure and function, regulation by co-factors and influence on propagation of yeast prions.
authors.affiliation: Laboratory of Biochemistry and Genetics, National Institute of Diabetes, Digestive and Kidney Diseases, National institutes of Health, Bethesda, MD 20892-0851, USA.
authors.forename: Deepak
authors.initials: D
authors.lastname: Sharma
authors.forename: Daniel C
authors.initials: DC
authors.lastname: Masison
mesh_terms: D005656:Fungal Proteins / Q000737:chemistry / Q000502:physiology; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry / Q000502:physiology*; D018832:Molecular Chaperones / Q000737:chemistry / Q000502:physiology; D011328:Prions / Q000502:physiology*; D011487:Protein Conformation; D017510:Protein Folding; D015003:Yeasts / Q000502:physiology*
chemical_list: D005656:Fungal Proteins; D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D011328:Prions