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1
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0031895351
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The hsp90-based chaperone system: Involvement in signal transduction from a variety of hormone and growth factor receptors
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Pratt W.B. The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors. Proc Soc Exp Biol Med. 217:1998;420-434.
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Proc Soc Exp Biol Med
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Pratt, W.B.1
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2
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0031444238
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Identification and structural characterisation of the ATP/ADP binding site in the Hsp90 molecular chaperone
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Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. Identification and structural characterisation of the ATP/ADP binding site in the Hsp90 molecular chaperone. Cell. 90:1997;65-75.
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Cell
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Prodromou, C.1
Roe, S.M.2
O'Brien, R.3
Ladbury, J.E.4
Piper, P.W.5
Pearl, L.H.6
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3
-
-
0030863995
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The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation
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Grenert J.P., Sullivan W.P., Fadden P., Haystead T.A.J., Clark J., Mimnaugh E., Krutzsch H., Ochel H-J., Schulte T.W., Sausville E.et al. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J Biol Chem. 272:1997;23843-23850.
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J Biol Chem
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Grenert, J.P.1
Sullivan, W.P.2
Fadden, P.3
Haystead, T.A.J.4
Clark, J.5
Mimnaugh, E.6
Krutzsch, H.7
Ochel, H.-J.8
Schulte, T.W.9
Sausville, E.10
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4
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0032541344
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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo
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This paper provides the first demonstration that Hsp90 both binds and hydrolyses ATP, and that mutations in the ATP-binding site that abolish these properties in vitro abolish yeast Hsp90's essential functions in vivo
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Panaretou B., Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo. EMBO J. 17:1998;4829-4836. This paper provides the first demonstration that Hsp90 both binds and hydrolyses ATP, and that mutations in the ATP-binding site that abolish these properties in vitro abolish yeast Hsp90's essential functions in vivo.
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(1998)
EMBO J
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, pp. 4829-4836
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Panaretou, B.1
Prodromou, C.2
Roe, S.M.3
O'Brien, R.4
Ladbury, J.E.5
Piper, P.W.6
Pearl, L.H.7
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5
-
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0032538995
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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis
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A second demonstration of the in vivo dependence of Hsp90 function on ATPase activity
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Obermann W.M.J., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U. In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis. J Cell Biol. 143:1998;901-910. A second demonstration of the in vivo dependence of Hsp90 function on ATPase activity.
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(1998)
J Cell Biol
, vol.143
, pp. 901-910
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Obermann, W.M.J.1
Sondermann, H.2
Russo, A.A.3
Pavletich, N.P.4
Hartl, F.U.5
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6
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0033581021
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The importance of ATP binding and hydrolysis by Hsp90 in formation and function of protein heterocomplexes
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The first demonstration in vitro that the activation of an authentic Hsp90-dependent client protein, progesterone receptor, to a functional state in vitro is dependent on the functional ATPase activity of Hsp90
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Grenert J.P., Johnson B.D., Toft D.O. The importance of ATP binding and hydrolysis by Hsp90 in formation and function of protein heterocomplexes. J Biol Chem. 274:1999;17525-17533. The first demonstration in vitro that the activation of an authentic Hsp90-dependent client protein, progesterone receptor, to a functional state in vitro is dependent on the functional ATPase activity of Hsp90.
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J Biol Chem
, vol.274
, pp. 17525-17533
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Grenert, J.P.1
Johnson, B.D.2
Toft, D.O.3
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7
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0030901877
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A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
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Prodromou C., Roe S.M., Piper P.W., Pearl L.H. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nat Struct Biol. 4:1997;477-482.
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(1997)
Nat Struct Biol
, vol.4
, pp. 477-482
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Prodromou, C.1
Roe, S.M.2
Piper, P.W.3
Pearl, L.H.4
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8
-
-
0032959590
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The structural basis for inhibition of the Hsp90 molecular chaperone, by the anti-tumour antibiotics radicicol and geldanamycin
-
This paper describes crystal structures of the N-terminal domain of yeast Hsp90 in complexes with geldanamycin and radicicol, compares them with complexes with bound ATP/ADP and defines key pharmacophores for future drug development
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Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. The structural basis for inhibition of the Hsp90 molecular chaperone, by the anti-tumour antibiotics radicicol and geldanamycin. J Med Chem. 42:1999;260-266. This paper describes crystal structures of the N-terminal domain of yeast Hsp90 in complexes with geldanamycin and radicicol, compares them with complexes with bound ATP/ADP and defines key pharmacophores for future drug development.
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(1999)
J Med Chem
, vol.42
, pp. 260-266
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-
Roe, S.M.1
Prodromou, C.2
O'Brien, R.3
Ladbury, J.E.4
Piper, P.W.5
Pearl, L.H.6
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9
-
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0031005361
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Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
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Stebbins C.E., Russo A.A., Schneider C., Rosen N., Hartl F.U., Pavletich N.P. Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell. 89:1997;239-250.
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Cell
, vol.89
, pp. 239-250
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Stebbins, C.E.1
Russo, A.A.2
Schneider, C.3
Rosen, N.4
Hartl, F.U.5
Pavletich, N.P.6
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10
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0032514843
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Crystal structure and ATPase activity of MutL: Implications for DNA repair and mutagenesis
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Ban C., Yang W. Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis. Cell. 95:1998;541-552.
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(1998)
Cell
, vol.95
, pp. 541-552
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Ban, C.1
Yang, W.2
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11
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0033515522
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Transformation of MutL by ATP binding and hydrolysis: A switch in DNA mismatch repair
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This paper describes the crystal structure of MutL bound to an ATP analogue. It provides a valuable assessment of the common structural and functional characteristics of the GyrB-Hsp90-MutL family of N-terminal ATPase domains
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Ban C., Junop M., Yang W. Transformation of MutL by ATP binding and hydrolysis: a switch in DNA mismatch repair. Cell. 97:1999;85-97. This paper describes the crystal structure of MutL bound to an ATP analogue. It provides a valuable assessment of the common structural and functional characteristics of the GyrB-Hsp90-MutL family of N-terminal ATPase domains.
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(1999)
Cell
, vol.97
, pp. 85-97
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Ban, C.1
Junop, M.2
Yang, W.3
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12
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0033534368
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Structure of CheA, a signal-transducing histidine kinase
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Bilwes A.M., Alex L.A., Crane B.R., Simon M.I. Structure of CheA, a signal-transducing histidine kinase. Cell. 96:1999;131-141.
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(1999)
Cell
, vol.96
, pp. 131-141
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Bilwes, A.M.1
Alex, L.A.2
Crane, B.R.3
Simon, M.I.4
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13
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0033593528
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Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies
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An electron microscopy study of Hsp90 that shows direct evidence for the association of N-terminal domains within an Hsp90 dimer following heat shock and, possibly, ATP binding
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Maruya M., Sameshima M., Nemoto T., Yahara I. Monomer arrangement in HSP90 dimer as determined by decoration with N and C-terminal region specific antibodies. J Mol Biol. 285:1999;903-907. An electron microscopy study of Hsp90 that shows direct evidence for the association of N-terminal domains within an Hsp90 dimer following heat shock and, possibly, ATP binding.
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(1999)
J Mol Biol
, vol.285
, pp. 903-907
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Maruya, M.1
Sameshima, M.2
Nemoto, T.3
Yahara, I.4
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15
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0030989277
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Folding of the glucocorticoid receptor by the reconstituted hsp90-based chaperone machinery
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Dittmar K., Pratt W.B. Folding of the glucocorticoid receptor by the reconstituted hsp90-based chaperone machinery. J Biol Chem. 272:1997;13047-13054.
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(1997)
J Biol Chem
, vol.272
, pp. 13047-13054
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Dittmar, K.1
Pratt, W.B.2
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16
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0032484127
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The assembly of progesterone receptor-hsp90 complexes using purified proteins
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Kosano H., Stensgard B., Charlesworth M.C., McMahon N., Toft D. The assembly of progesterone receptor-hsp90 complexes using purified proteins. J Biol Chem. 273:1998;32973-32979.
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(1998)
J Biol Chem
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, pp. 32973-32979
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Kosano, H.1
Stensgard, B.2
Charlesworth, M.C.3
McMahon, N.4
Toft, D.5
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17
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0032473425
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The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
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The authors describe the first crystal structure of a TPR domain, revealing a channel for peptide binding
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Das A.K., Cohen P.T.W., Barford D. The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions. EMBO J. 17:1998;1192-1199. The authors describe the first crystal structure of a TPR domain, revealing a channel for peptide binding.
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(1998)
EMBO J
, vol.17
, pp. 1192-1199
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Das, A.K.1
Cohen, P.T.W.2
Barford, D.3
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18
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0033575232
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Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90
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This mutagenesis study shows the importance of basic residues within the TPR domain groove and acidic residues in the C terminus of Hsp90 in mediating Hsp90-TPR-containing co-chaperone interactions
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Russell L.C., Whitt S.R., Chen M-S., Chinkers M. Identification of conserved residues required for the binding of a tetratricopeptide repeat domain to heat shock protein 90. J Biol Chem. 274:1999;20060-20063. This mutagenesis study shows the importance of basic residues within the TPR domain groove and acidic residues in the C terminus of Hsp90 in mediating Hsp90-TPR-containing co-chaperone interactions.
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(1999)
J Biol Chem
, vol.274
, pp. 20060-20063
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Russell, L.C.1
Whitt, S.R.2
Chen, M.-S.3
Chinkers, M.4
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19
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0033613950
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The common tetratricopeptide repeat acceptor site for steroid receptor associated immunophilins and hop is located in the dimerization domain of Hsp90
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Carrello A., Ingley E., Minchin R.F., Tsai S., Ratajczak T. The common tetratricopeptide repeat acceptor site for steroid receptor associated immunophilins and hop is located in the dimerization domain of Hsp90. J Biol Chem. 274:1999;2682-2689.
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(1999)
J Biol Chem
, vol.274
, pp. 2682-2689
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Carrello, A.1
Ingley, E.2
Minchin, R.F.3
Tsai, S.4
Ratajczak, T.5
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20
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0031846768
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Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants
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Mutational analysis of Hsp90 showed its C-terminal region to be essential for TPR-domain-containing co-chaperone binding
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Chen S.Y., Sullivan W.P., Toft D.O., Smith D.F. Differential interactions of p23 and the TPR-containing proteins Hop, Cyp40, FKBP52 and FKBP51 with Hsp90 mutants. Cell Stress Chaperones. 3:1998;118-129. Mutational analysis of Hsp90 showed its C-terminal region to be essential for TPR-domain-containing co-chaperone binding.
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(1998)
Cell Stress Chaperones
, vol.3
, pp. 118-129
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Chen, S.Y.1
Sullivan, W.P.2
Toft, D.O.3
Smith, D.F.4
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22
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0033081968
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Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones
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The TPR-containing co-chaperone p60/Hop/Sti1 was shown to inhibit the ATPase activity of Hsp90 and produce significant conformational change on binding. This study also provides the first direct measurement of the stoichiometry of TPR-containing co-chaperone binding to Hsp90, revealing two TPR-binding sites per Hsp90 dimer, rather than one (as previously thought)
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Prodromou C., Siligardi G., O'Brien R., Woolfson D.N., Regan L., Panaretou B., Ladbury J.E., Piper P.W., Pearl L.H. Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J. 18:1999;754-762. The TPR-containing co-chaperone p60/Hop/Sti1 was shown to inhibit the ATPase activity of Hsp90 and produce significant conformational change on binding. This study also provides the first direct measurement of the stoichiometry of TPR-containing co-chaperone binding to Hsp90, revealing two TPR-binding sites per Hsp90 dimer, rather than one (as previously thought).
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(1999)
EMBO J
, vol.18
, pp. 754-762
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-
Prodromou, C.1
Siligardi, G.2
O'Brien, R.3
Woolfson, D.N.4
Regan, L.5
Panaretou, B.6
Ladbury, J.E.7
Piper, P.W.8
Pearl, L.H.9
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23
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0031755018
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Cns1 is an essential protein associated with the Hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Δ cells
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•], reports the discovery of the first essential TPR-containing co-chaperone and the existence of a Cns1-Hsp90-Cpr7 complex. This latter discovery suggests the presence of two TPR-binding sites per Hsp90 dimer
-
•], reports the discovery of the first essential TPR-containing co-chaperone and the existence of a Cns1-Hsp90-Cpr7 complex. This latter discovery suggests the presence of two TPR-binding sites per Hsp90 dimer.
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(1998)
Mol Cell Biol
, vol.18
, pp. 7353-7359
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Marsh, J.A.1
Kalton, H.M.2
Gaber, R.F.3
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25
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0033055908
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P50cdc37 acting in concert with Hsp90 is required for Raf-1 function
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Grammatikakis N., Lin J-H., Grammatikakis A., Tsichlis P.N., Cochran B.H. p50cdc37 acting in concert with Hsp90 is required for Raf-1 function. Mol Cell Biol. 19:1999;1661-1672.
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(1999)
Mol Cell Biol
, vol.19
, pp. 1661-1672
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Grammatikakis, N.1
Lin, J.-H.2
Grammatikakis, A.3
Tsichlis, P.N.4
Cochran, B.H.5
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26
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0032493624
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P50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site
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Silverstein A.M., Grammatikakis N., Cochran B.H., Chinkers M., Pratt W.B. P50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site. J Biol Chem. 273:1998;20090-20095.
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(1998)
J Biol Chem
, vol.273
, pp. 20090-20095
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Silverstein, A.M.1
Grammatikakis, N.2
Cochran, B.H.3
Chinkers, M.4
Pratt, W.B.5
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27
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0032567434
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Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery
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Chen S., Smith D.F. Hop as an adaptor in the heat shock protein 70 (Hsp70) and Hsp90 chaperone machinery. J Biol Chem. 273:1998;35194-35200.
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(1998)
J Biol Chem
, vol.273
, pp. 35194-35200
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Chen, S.1
Smith, D.F.2
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29
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0031832233
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SBA1 encodes a yeast Hsp90 cochaperone that is homologous to vertebrate p23 proteins
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Fang Y., Fliss A.E., Rao J., Caplan A.J. SBA1 encodes a yeast Hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol Cell Biol. 18:1998;3727-3734.
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Mol Cell Biol
, vol.18
, pp. 3727-3734
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Fang, Y.1
Fliss, A.E.2
Rao, J.3
Caplan, A.J.4
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30
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0033574059
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Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation
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•]) was identified in a different genetic screen with Hsp90 ts mutants, which also identified Hch1 - a new non-TPR-containing co-chaperone
-
•]) was identified in a different genetic screen with Hsp90 ts mutants, which also identified Hch1 - a new non-TPR-containing co-chaperone.
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(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 1409-1414
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Nathan, D.F.1
Vos, M.H.2
Lindquist, S.3
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31
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0032079539
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The peptidyl-prolyl isomerase domain of the Cyp-40 cyclophilin homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae
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Duina A.A., Marsh J.A., Kurtz R.B., Chang H-C.J., Lindquist S., Gaber R.F. The peptidyl-prolyl isomerase domain of the Cyp-40 cyclophilin homolog Cpr7 is not required to support growth or glucocorticoid receptor activity in Saccharomyces cerevisiae. J Biol Chem. 273:1998;10819-10822.
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J Biol Chem
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Duina, A.A.1
Marsh, J.A.2
Kurtz, R.B.3
Chang, H.-C.J.4
Lindquist, S.5
Gaber, R.F.6
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32
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0031871101
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Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly
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Pratt W.B., Dittmar K.D. Studies with purified chaperones advance the understanding of the mechanism of glucocorticoid receptor hsp90 heterocomplex assembly. Trends Endocrinol Metabol. 9:1998;244-252.
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(1998)
Trends Endocrinol Metabol
, vol.9
, pp. 244-252
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Pratt, W.B.1
Dittmar, K.D.2
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33
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0032493733
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A conserved proline in the hsp90 binding region of the glucocorticoid receptor is required for hsp90 heterocomplex stabilization and receptor signalling
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Caamano C.A., Morano M.I., Dalman F.C., Pratt W.B., Akil H. A conserved proline in the hsp90 binding region of the glucocorticoid receptor is required for hsp90 heterocomplex stabilization and receptor signalling. J Biol Chem. 273:1998;20473-20480.
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J Biol Chem
, vol.273
, pp. 20473-20480
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Caamano, C.A.1
Morano, M.I.2
Dalman, F.C.3
Pratt, W.B.4
Akil, H.5
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34
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0032577591
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Binding of hsp90 to the glucocorticoid receptor requires a specific 7-amino acid sequence at the amino terminus of the hormone-binding domain
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Xu M., Dittmar K.D., Giannoukos G., Pratt W.B., Simons S.S. Binding of hsp90 to the glucocorticoid receptor requires a specific 7-amino acid sequence at the amino terminus of the hormone-binding domain. J Biol Chem. 273:1998;13918-13924.
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J Biol Chem
, vol.273
, pp. 13918-13924
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Xu, M.1
Dittmar, K.D.2
Giannoukos, G.3
Pratt, W.B.4
Simons, S.S.5
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35
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0033524442
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Maturation of the tyrosine kinase c Src as a kinase and as a substrate depends on the molecular chaperone Hsp90
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An in vivo study that demonstrates conclusively that, as for oncogenic v-Src, the activation of normal cellular Src kinase (and probably other Src-family kinases) is Hsp90-dependent
-
Xu Y., Singer M.A., Lindquist S. Maturation of the tyrosine kinase c Src as a kinase and as a substrate depends on the molecular chaperone Hsp90. Proc Natl Acad Sci USA. 96:1999;109-114. An in vivo study that demonstrates conclusively that, as for oncogenic v-Src, the activation of normal cellular Src kinase (and probably other Src-family kinases) is Hsp90-dependent.
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(1999)
Proc Natl Acad Sci USA
, vol.96
, pp. 109-114
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Xu, Y.1
Singer, M.A.2
Lindquist, S.3
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36
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0032478703
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Modular folding and evidence for phosphorylation-induced stabilization of an Hsp90-dependent kinase
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Hartson S.D., Ottinger E.A., Huang W., Barany G., Burn P., Matts R.L. Modular folding and evidence for phosphorylation-induced stabilization of an Hsp90-dependent kinase. J Biol Chem. 273:1998;8475-8482.
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(1998)
J Biol Chem
, vol.273
, pp. 8475-8482
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Hartson, S.D.1
Ottinger, E.A.2
Huang, W.3
Barany, G.4
Burn, P.5
Matts, R.L.6
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37
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0032401771
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Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteosome
-
Loo M.A., Jensen T.J., Cui L., Hou Y-X., Chang X-B., Riordan J.R. Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteosome. EMBO J. 17:1998;6879-6887.
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(1998)
EMBO J
, vol.17
, pp. 6879-6887
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Loo, M.A.1
Jensen, T.J.2
Cui, L.3
Hou, Y.-X.4
Chang, X.-B.5
Riordan, J.R.6
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38
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0009621605
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Dynamic activation of endothelial nitric oxide synthase by Hsp90
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Garcia-Cardena G., Fan R., Shah V., Sorrentino R., Cirino G., Papapetropoulos A., Sessa W.C. Dynamic activation of endothelial nitric oxide synthase by Hsp90. Nature. 392:1998;821-824.
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(1998)
Nature
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Garcia-Cardena, G.1
Fan, R.2
Shah, V.3
Sorrentino, R.4
Cirino, G.5
Papapetropoulos, A.6
Sessa, W.C.7
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39
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0033118355
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Functional requirement of p23 and Hsp90 in telomerase complexes
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Holt S.E., Aisner D.L., Baur J., Tesmer V.M., Dy M., Ouellette M., Trager J.B., Morin G.B., Toft D.O., Shay J.W.et al. Functional requirement of p23 and Hsp90 in telomerase complexes. Genes Dev. 13:1999;817-826.
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Holt, S.E.1
Aisner, D.L.2
Baur, J.3
Tesmer, V.M.4
Dy, M.5
Ouellette, M.6
Trager, J.B.7
Morin, G.B.8
Toft, D.O.9
Shay, J.W.10
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40
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0032100480
-
Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression
-
Hoshino T., Wang J., Devetten M.P., Iwata N., Kajigaya S., Wise R.J., Liu J.M., Youssoufian H. Molecular chaperone GRP94 binds to the Fanconi anemia group C protein and regulates its intracellular expression. Blood. 91:1998;4379-4386.
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Blood
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Hoshino, T.1
Wang, J.2
Devetten, M.P.3
Iwata, N.4
Kajigaya, S.5
Wise, R.J.6
Liu, J.M.7
Youssoufian, H.8
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41
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0032555685
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Repression of heat shock transcription factor HSF1 activation by Hsp90 (Hsp90 complex) that forms a stress-sensitive complex with HSF1
-
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