References
Amir-Shapira D, Leustek T, Dalie B, Weissbach H, Brot N (1990) Hsp70 proteins, similar toEscherichia coli dnaK, in chloroplasts and mitochondria ofEuglena gracilis. Proc Natl Acad Sci USA 87: 749
Beckmann RP, Mizzen LA, Welch WJ (1990) Interaction of hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science 248: 850
Bennett WSJ, Steitz TZ (1980) Structure of a complex between yeast hexokinase A and glucose. II. Detailed comparisons of conformation and active site configuration with the native hexokinase B monomer and dimer. J Mol Biol 140: 211
Burton ZF, Eisenberg D (1980) A procedure for rapid isolation of both groE protein and glutamine synthetase fromE.coli. Arch Biochem Biophys 205: 478
Chappell TG, Konforti BB, Schmid SL, Rothmann JE (1987) The ATPase core of a clathrin uncoating protein. J Biol Chem 262: 746
Cheng MY, Hartl FU, Martin J, Pollock RA, Kalousek F, Neupert W, Hallberg EM, Hallberg RL, Horwich AL (1989) Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337: 620
DeLuca-Flaherty C, McKay DB, Parham P, Hill BL (1990) Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. Cell 62: 875
Dworniczak B, Mirault M-E (1987) Structure and expression of a human gene coding for a 71kd heat shock ‘cognate’ protein. Nucleic Acids Res 15: 5181
Ellis RJ (1987) Proteins as molecular chaperones. Nature 328: 378
Ellis RJ, van der Vies SM, Hemmingsen SM (1989) The molecular chaperone concept. Biochem Soc Symp 55: 145
Flaherty KM, DeLuca-Flaherty C, McKay DB (1990) Three-dimensional structure of the ATPase fragment of a 70-kilodalton heat shock cognate protein. Nature 346: 623
Flaherty KM, McKay DB, Kabsch W, Holmes KC (1991) Similarity of the three-dimensional structures of actin and the ATPase fragment of a 70-kDa heat shock cognate protein. Proc Natl Acad Sci USA 88: 5041
Fletterick RJ, Bates DJ, Steitz TA (1975) The structure of a yeast hexokinase monomer and its complexes with substrates at 2.7 Å resolution. Proc Natl Acad Sci USA 72: 38
Gaitanaris GA, Papavassiliou AG, Rubock P, Silverstein SJ, Gottesman ME (1990) Renaturation of denatured lambda repressor requires heat shock proteins. Cell 61: 1013
Haas IG, Wabl M (1983) Immunoglobulin heavy chain binding protein. Nature 306: 387
Hearne CM, Ellar DJ (1989) Nucleotide sequence of aBacillus subtilis gene homologous to the dnaK gene ofEscherichia coli. Nucleic Acids Res 17: 8373
Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ (1988) Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333: 330
Hendrix RW (1979) Purification and properties of groE, a host protein involved in bacteriophage assembly. J Mol Biol 129: 375
Hohn T, Hohn B, Engel A, Wurtz M (1979) Isolation and characterization of the host protein groE involved in bacteriophage lambda assembly. J Mol Biol 129: 359
Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC (1990) Atomic structure of the actin: DNase I complex. Nature 347: 37
Leustek T, Dalie B, Amir-Shapira D, Brot N, Weissbach H (1989) A member of the Hsp70 family is localized in mitochondria and resemblesEscherichia coli DnaK. Proc Natl Acad Sci USA 86: 7805
Lewis MJ, Pelham HRB (1990) The sequence of theKluyveromyces lactis BiP gene. Nucleic Acids Res 18: 6438
Liberek K, Georgopoulos C, Zylicz M (1988) Role of theEscherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication. Proc Natl Acad Sci USA 85: 6632
Marshall JS, DeRocher AE, Keegstra K, Vierling E (1990) Identification of heat shock protein hsp70 homologues in chloroplasts. Proc Natl Acad Sci USA 87: 374
Munro S, Pelham HR (1986) An hsp70-like protein in the ER: identity with the 78-kDa glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46: 291
Normington K, Kohno K, Kozutsumi Y, Gething MJ, Sambrook J (1989) S.cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57: 1223
Ostermann J, Voos W, Kang PJ, Craig EA, Neupert W, Pfanner N (1990) Precursor proteins in transit through mitochondrial contact sites interact with hsp70 in the matrix. FEBS Lett 277: 281
Pelham HR (1984) Hsp70 accelerates the recovery of nucleolar morphology after heat shock. EMBO J 3: 3095
Pelham HRB (1986) Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46: 959
Pfanner N, Ostermann J, Rassow J, Haiti F-U, Neupert W (1990) Stress proteins and mitochondrial protein import. Antonie Van Leeuwenhoek 58: 191
Rochester DE, Winer JA, Shah DM (1986) The structure and expression of maize genes encoding the major heat shock protein, hsp70. EMBO J, 5: 451
Rose MD, Misra LM, Vogel JP (1989) KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57: 1211
Scherer PE, Krieg UC, Hwang ST, Vestweber D, Schatz G (1990) A precursor protein partly translocated into yeast mitochondria is bound to a 70-kDa mitochondrial stress protein.
Schlossmann DM, Schmid SL, Braell WA, Rothmann JE (1984) An enzyme that removes clathrin coats: purification of an uncoating ATPase. J Cell Biol 99: 723
Shiu RPC, Pastan IH (1979) Properties and purification of a glucose-regulated protein from chick embryo fibroblasts. Biochim Biophys Acta 576: 141
Skowyra D, Georgopoulos C, Zylicz M (1990) TheE. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner. Cell 62: 939
Sorger PK, Pelham HR (1987) Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells. EMBO J 6: 993
Sussmann MD, Setlow P (1987) Nucleotide sequence of aBacillus megaterium gene homologous to the dnaK gene ofEscherichia coli. Nucleic Acids Res 15: 3923
Ting J, Lee AS (1988) Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA 7: 275
Werner-Washburne M, Stone DE, Craig EA (1987) Complex interactions among members of an essential subfamily of hsp70 genes inSaccharomyces cerevisiae. Mol Cell Biol 7: 2568
Winter J Wright R, Duck N, Gasser C, Fraley R, Shah D (1988) The inhibition of petunia hsp 70 mRNA processing during CdC1(2) stress. Mol Gen Genet 211: 315
Young RA, Elliott TJ (1989) Stress proteins, infection, and immune surveillance. Cell 59: 5
Zwickl P, Pfeifer G, Lottspeich F, Kopp F, Dahlmann B, Baumeister W (1990) Electron microscopy and image analysis reveal common principles of organization in two large protein complexes: groEL-type proteins and proteasomes. J Struct Biol 103: 197
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McKay, D.B. Structure of the 70-kiloDalton heat-shock-related proteins. Springer Semin Immunopathol 13, 1–9 (1991). https://doi.org/10.1007/BF01225274
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DOI: https://doi.org/10.1007/BF01225274