-
1
-
-
0023668329
-
Proteins as molecular chaperones
-
ELLIS, J. 1987. Proteins as molecular chaperones. Nature 328: 378-379.
-
(1987)
Nature
, vol.328
, pp. 378-379
-
-
Ellis, J.1
-
2
-
-
0027184721
-
Molecular chaperone functions of heat-shock proteins
-
HENDRICK, J. P. & F. U. A. HARTL. 1993. Molecular chaperone functions of heat-shock proteins. Ann. Rev. Biochem. 62: 349-384.
-
(1993)
Ann. Rev. Biochem.
, vol.62
, pp. 349-384
-
-
Hendrick, J.P.1
Hartl, F.U.A.2
-
3
-
-
0029992278
-
-
HARTL, F. U. 1996. Nature 381: 571-580.
-
(1996)
Nature
, vol.381
, pp. 571-580
-
-
Hartl, F.U.1
-
4
-
-
0026669310
-
The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity
-
MIYATA, Y. & I. YAHARA. 1992. The 90-kDa heat shock protein, HSP90, binds and protects casein kinase II from self-aggregation and enhances its kinase activity. J. Biol. Chem. 267: 7042-7047.
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 7042-7047
-
-
Miyata, Y.1
Yahara, I.2
-
5
-
-
0030060955
-
Heat-induced chaperone activity of HSP90
-
YONEHARA, M., Y. MINAMI, Y. KAWATA, J. NAGAI & I. YAHARA. 1996. Heat-induced chaperone activity of HSP90. J. Biol. Chem. 271: 2641-2645.
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 2641-2645
-
-
Yonehara, M.1
Minami, Y.2
Kawata, Y.3
Nagai, J.4
Yahara, I.5
-
6
-
-
0342651927
-
Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins
-
KOYASU, S., E. NISHIDA, Y. KADOWAKI, F. MATSUZAKI, K. IIDA, F. HARADA, M. KASUGA, H. SAKAI & I. YAHARA. 1986. Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins. Proc. Natl. Acad. Sci. USA 83: 8054-8058.
-
(1986)
Proc. Natl. Acad. Sci. USA
, vol.83
, pp. 8054-8058
-
-
Koyasu, S.1
Nishida, E.2
Kadowaki, Y.3
Matsuzaki, F.4
Iida, K.5
Harada, F.6
Kasuga, M.7
Sakai, H.8
Yahara, I.9
-
7
-
-
0024542186
-
Murine 86- And 84-kDa heat shock proteins, cDNA sequences, choromosomal assignments, and evolutionary origins
-
MOORE, S. K., C. KOZAK, E. A. ROBINSON, S. J. ULLRICH & E. APPELLA. 1989. Murine 86- and 84-kDa heat shock proteins, cDNA sequences, choromosomal assignments, and evolutionary origins. J. Biol. Chem. 264: 5343-5351.
-
(1989)
J. Biol. Chem.
, vol.264
, pp. 5343-5351
-
-
Moore, S.K.1
Kozak, C.2
Robinson, E.A.3
Ullrich, S.J.4
Appella, E.5
-
8
-
-
0025874261
-
Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90
-
MINAMI, Y., H. KAWASAKI, Y. MIYATA, K. SUZUKI & I. YAHARA. 1991. Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90. J. Biol. Chem. 266: 10099-10103.
-
(1991)
J. Biol. Chem.
, vol.266
, pp. 10099-10103
-
-
Minami, Y.1
Kawasaki, H.2
Miyata, Y.3
Suzuki, K.4
Yahara, I.5
-
9
-
-
0028012587
-
The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo
-
MINAMI, Y., Y. KIMURA, H. KAWASAKI, K. SUZUKI & I. YAHARA. 1994. The carboxy-terminal region of mammalian HSP90 is required for its dimerization and function in vivo. Mol. Cell. Biol. 14: 1459-1464.
-
(1994)
Mol. Cell. Biol.
, vol.14
, pp. 1459-1464
-
-
Minami, Y.1
Kimura, Y.2
Kawasaki, H.3
Suzuki, K.4
Yahara, I.5
-
10
-
-
0030901877
-
A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone
-
PRODROMOU, C., S. M. ROE, P. W. PIPER & L. H. PEARL. 1997. A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone. Nature Struct. Biol. 4: 477-482.
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 477-482
-
-
Prodromou, C.1
Pearl, L.H.2
-
11
-
-
0031005361
-
Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
-
STEBBINS, C. E., A. A. RUSSO, C. SCHNEIDER, N. ROSEN, F. U. HARTL & N. P. PAVIETICH. 1997. Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent. Cell 89: 239-250.
-
(1997)
Cell
, vol.89
, pp. 239-250
-
-
Stebbins, C.E.1
Russo, A.A.2
Schneider, C.3
Rosen, N.4
Hartl, F.U.5
Pavietich, N.P.6
-
12
-
-
0028848373
-
Mechanism of dimer formation of the 90-kDa heat-shock protein
-
NEMOTO, T., Y. OHARA-NEMOTO, M. OTA, T. TAKAGI & K. YOKOYAMA. 1995. Mechanism of dimer formation of the 90-kDa heat-shock protein. Eur. J. Biochem. 233: 1-8.
-
(1995)
Eur. J. Biochem.
, vol.233
, pp. 1-8
-
-
Nemoto, T.1
Ohara-Nemoto, Y.2
Ota, M.3
Takagi, T.4
Yokoyama, K.5
-
13
-
-
0029922568
-
Mutational analysis of Hsp90α dimerization and subcellular localization: Dimer disruption does not impede "in vivo" interaction with estrogen receptor
-
MENG, XIA, J. DEVIN, W. P. SULLIVAN, D. TOFT & E.-E. BAULIEU. 1996. Mutational analysis of Hsp90α dimerization and subcellular localization: dimer disruption does not impede "in vivo" interaction with estrogen receptor. J. Cell Sci. 109: 1677-1667.
-
(1996)
J. Cell Sci.
, vol.109
, pp. 1677-11667
-
-
Devin, J.1
Sullivan, W.P.2
Toft, D.3
Baulieu, E.-E.4
-
14
-
-
0026778032
-
Hsp90 chaperones protein folding in vitro
-
WIECH, H., J. BUCHNER, R. ZIMMERMANN & U. JAKOB. 1992. Hsp90 chaperones protein folding in vitro. Nature 358: 169-170.
-
(1992)
Nature
, vol.358
, pp. 169-170
-
-
Wiech, H.1
Buchner R Zimmermann, J.2
Jakob, U.3
-
15
-
-
0026416043
-
Chaperonin-mediated protein folding at the surface of groEL through a "moleten globule"-like intermediate
-
MARTIN, J., T. LANGER, R. BOTEVA, A. SCHRAMEL, A. L. HORWICH & F.-U. HARTL. 1991. Chaperonin-mediated protein folding at the surface of groEL through a "moleten globule"-like intermediate. Nature 352: 36-42.
-
(1991)
Nature
, vol.352
, pp. 36-42
-
-
Martin, J.1
Langer, T.2
Boteva, R.3
Schramel, A.4
Horwich, A.L.5
Hartl, F.-U.6
-
16
-
-
0029887140
-
The human cytosolic molecular chaperones Hsp90, Hsp70 (Hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
-
FREEMAN, B. C. & R. I. MORIMOTO. 1996. The human cytosolic molecular chaperones Hsp90, Hsp70 (Hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 15: 2969-2979.
-
(1996)
EMBO J.
, vol.15
, pp. 2969-2979
-
-
Freeman, B.C.1
Morimoto, R.I.2
-
17
-
-
0028360710
-
-
SCHUMACHER, R. J., R. HURST, W. P. SULLIVAN, N. J. MCMAHON & D. O. TOFT. 1994. ATP-dependent chaperoning activity of reticulocyte lysate. J. Biol. Chem. 269: 9493-9499.
-
(1994)
J. ATP-Biol Chem.
, vol.269
, pp. 9499
-
-
Schumacher, R.J.1
Hurst, R.2
Sullivan, W.P.3
Mcmahon, N.J.4
Toft, D.O.5
-
18
-
-
0027214861
-
The calmodulin-binding domain of the mouse 90-kDa heat shock protein
-
MINAMI, Y., H. KAWASAKI, K. SUZUKI & I. YAHARA. 1993. The calmodulin-binding domain of the mouse 90-kDa heat shock protein. J. Biol. Chem. 268: 9604-9610.
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 9604-9610
-
-
Minami, Y.1
Kawasaki K Suzuki, H.2
Yahara, I.3
-
19
-
-
0028618296
-
Protein folding and the regulation of signaling pathways
-
RUTHERFORD, S. L. & C. S. ZUKER. 1994. Protein folding and the regulation of signaling pathways. Cell 79: 1129-1132.
-
(1994)
Cell
, vol.79
, pp. 1129-1132
-
-
Rutherford, S.L.1
Zuker, C.S.2
-
20
-
-
0002830140
-
Modulation of steroid receptor signal transduction by heat shock proteins
-
R. I. Morimoto, A. Tissieres & C. Georgopoulos, Eds.: Cold Spring Harbor Laboratory Press. Cold Spring Harbor, New York.
-
BOHEN, S. P. & K. R. YAMAMOTO. 1994. Modulation of steroid receptor signal transduction by heat shock proteins. In The Biology of Heat Shock Proteins and Molecular Chaperones. R. I. Morimoto, A. Tissieres & C. Georgopoulos, Eds.: 313-334. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, New York.
-
(1994)
The Biology of Heat Shock Proteins and Molecular Chaperones
, pp. 313-334
-
-
Bohen, S.P.1
Yamamoto, K.R.2
-
21
-
-
0029872081
-
The involvement of p23, hsp90, and immunophillins in the assembly of progesterone receptor complexes
-
JOHNSTON, J., R. CARBISIER, S. STENGGARD & D. TOFT. 1996. The involvement of p23, hsp90, and immunophillins in the assembly of progesterone receptor complexes. J. Steroid Biochem. Mol. Biol. 56: 31-37.
-
(1996)
J. Steroid Biochem. Mol. Biol.
, vol.56
, pp. 31-37
-
-
Johnston, J.1
Toft, D.2
-
22
-
-
0024567048
-
Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor
-
BRESNICK, E. H., F. C. DALMAN, E. R. SANCHES & W. B. PRATT. 1989. Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J. Biol. Chem. 264: 4992-4997.
-
(1989)
J. Biol. Chem.
, vol.264
, pp. 4992-4997
-
-
Bresnick, E.H.1
Pratt, W.B.2
-
23
-
-
0025161860
-
The transformed glucocorticoid receptor has a lower steroid-binding affinity than the nontransformed receptor
-
NEMOTO, T., Y. OHARA-NEMOTO, M. DENIS & J.-A. GUSTAFSSON. 1990. The transformed glucocorticoid receptor has a lower steroid-binding affinity than the nontransformed receptor. Biochemistry 29: 1880-1886.
-
(1990)
Biochemistry
, vol.29
, pp. 1880-1886
-
-
Nemoto, T.1
Gustafsson, J.-A.2
-
24
-
-
0025175208
-
Reduced levels of hsp90 compromise steroid receptor action in vivo
-
PICARD, D., B. KHURSHEED, M. J. GARABEDIAN, M. G. FORTIN, S. LINDQUIST & K. R. YAMAMOTO. 1990. Reduced levels of hsp90 compromise steroid receptor action in vivo. Nature 348: 166-168.
-
(1990)
Nature
, vol.348
, pp. 166-168
-
-
Picard, D.1
Khursheed, B.2
Garabedian, M.J.3
Fortin, M.G.4
Lindquist, S.5
Yamamoto, K.R.6
-
25
-
-
0029063877
-
Interaction between casein kinase II and the 90-kDa stress protein, HSP90
-
MIYATA, Y. & I. YAHARA. 1995. Interaction between casein kinase II and the 90-kDa stress protein, HSP90. Biochemistry 34: 8123-8129.
-
(1995)
Biochemistry
, vol.34
, pp. 8123-8129
-
-
Miyata, Y.1
Yahara, I.2
-
26
-
-
0024548919
-
Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II
-
LEES-MILLER, S. P. & C. W. ANDERSON. 1989. Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II. J. Biol. Chem. 264: 2431-2437.
-
(1989)
J. Biol. Chem.
, vol.264
, pp. 2431-2437
-
-
Lees-Miller, S.P.1
Anderson, C.W.2
|