-
1
-
-
33746330168
-
Hsp70 molecular chaperones: emerging roles in human disease and identification of small molecule modulators
-
Brodsky J.L., and Chiosis G. Hsp70 molecular chaperones: emerging roles in human disease and identification of small molecule modulators. Curr. Top. Med. Chem. 6 (2006) 1215-1225
-
(2006)
Curr. Top. Med. Chem.
, vol.6
, pp. 1215-1225
-
-
Brodsky, J.L.1
Chiosis, G.2
-
2
-
-
17044387386
-
Hsp70 chaperones: cellular functions and molecular mechanism
-
Mayer M.P., and Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol. Life Sci. 62 (2005) 670-684
-
(2005)
Cell Mol. Life Sci.
, vol.62
, pp. 670-684
-
-
Mayer, M.P.1
Bukau, B.2
-
3
-
-
33745749328
-
-
Raviol, H., Sadlish, H., Rodriguez, F., Mayer, M.P. and Bukau, B. (2006) Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 25, 2510-2518.
-
Raviol, H., Sadlish, H., Rodriguez, F., Mayer, M.P. and Bukau, B. (2006) Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 25, 2510-2518.
-
-
-
-
4
-
-
29344449706
-
Human and yeast Hsp110 chaperones exhibit functional differences
-
Raviol H., Bukau B., and Mayer M.P. Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett. 580 (2006) 168-174
-
(2006)
FEBS Lett.
, vol.580
, pp. 168-174
-
-
Raviol, H.1
Bukau, B.2
Mayer, M.P.3
-
5
-
-
0036678054
-
Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity
-
Goeckeler J.L., Stephens A., Lee P., Caplan A.J., and Brodsky J.L. Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activity. Mol. Biol. Cell 13 (2002) 2760-2770
-
(2002)
Mol. Biol. Cell
, vol.13
, pp. 2760-2770
-
-
Goeckeler, J.L.1
Stephens, A.2
Lee, P.3
Caplan, A.J.4
Brodsky, J.L.5
-
6
-
-
0001133526
-
Hsp110 protects heat-denatured proteins and confers cellular thermoresistance
-
Oh H.J., Chen X., and Subjeck J.R. Hsp110 protects heat-denatured proteins and confers cellular thermoresistance. J. Biol. Chem. 272 (1997) 31636-31640
-
(1997)
J. Biol. Chem.
, vol.272
, pp. 31636-31640
-
-
Oh, H.J.1
Chen, X.2
Subjeck, J.R.3
-
7
-
-
33745762927
-
-
Dragovic, Z., Broadley, S., Shomura, Y., Bracher, A. and Hartl, F.U. (2006) Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J. 25, 2519-2528.
-
Dragovic, Z., Broadley, S., Shomura, Y., Bracher, A. and Hartl, F.U. (2006) Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J. 25, 2519-2528.
-
-
-
-
8
-
-
33845587149
-
Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1
-
Shaner L., Sousa R., and Morano K.A. Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1. Biochemistry 45 (2006) 15075-15084
-
(2006)
Biochemistry
, vol.45
, pp. 15075-15084
-
-
Shaner, L.1
Sousa, R.2
Morano, K.A.3
-
9
-
-
13244278043
-
Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange
-
Shomura Y., et al. Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Mol. Cell 17 (2005) 367-379
-
(2005)
Mol. Cell
, vol.17
, pp. 367-379
-
-
Shomura, Y.1
-
10
-
-
0027445375
-
Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family
-
Mukai H., Kuno T., Tanaka H., Hirata D., Miyakawa T., and Tanaka C. Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family. Gene 132 (1993) 57-66
-
(1993)
Gene
, vol.132
, pp. 57-66
-
-
Mukai, H.1
Kuno, T.2
Tanaka, H.3
Hirata, D.4
Miyakawa, T.5
Tanaka, C.6
-
11
-
-
0027491078
-
MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae
-
Shirayama M., Kawakami K., Matsui Y., Tanaka K., and Toh-e A. MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae. Mol. Gen. Genet. 240 (1993) 323-332
-
(1993)
Mol. Gen. Genet.
, vol.240
, pp. 323-332
-
-
Shirayama, M.1
Kawakami, K.2
Matsui, Y.3
Tanaka, K.4
Toh-e, A.5
-
12
-
-
29244432181
-
Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
-
Yam A.Y.-W., Albanese V., Lin H.-T.J., and Frydman J. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J. Biol. Chem. 280 (2005) 41252-41261
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 41252-41261
-
-
Yam, A.Y.-W.1
Albanese, V.2
Lin, H.-T.J.3
Frydman, J.4
-
13
-
-
29244467709
-
The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb
-
Shaner L., Wegele H., Buchner J., and Morano K.A. The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb. J. Biol. Chem. 280 (2005) 41262-41269
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 41262-41269
-
-
Shaner, L.1
Wegele, H.2
Buchner, J.3
Morano, K.A.4
-
14
-
-
0033625965
-
-
Easton, D.P., Kaneko, Y. and Subjeck, J.R. (2000) The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress & Chaperones 5, 276-290.
-
Easton, D.P., Kaneko, Y. and Subjeck, J.R. (2000) The Hsp110 and Grp170 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress & Chaperones 5, 276-290.
-
-
-
-
15
-
-
34848869936
-
Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1
-
Liu Q., and Hendrickson W.A. Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1. Cell 131 (2007) 106-120
-
(2007)
Cell
, vol.131
, pp. 106-120
-
-
Liu, Q.1
Hendrickson, W.A.2
-
16
-
-
0024325535
-
Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides
-
Kassenbrock C.K., and Kelly R.B. Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides. EMBO J. 8 (1989) 1461-1467
-
(1989)
EMBO J.
, vol.8
, pp. 1461-1467
-
-
Kassenbrock, C.K.1
Kelly, R.B.2
-
17
-
-
2542435778
-
The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related Hsp70 family
-
Shaner L., Trott A., Goeckeler J.L., Brodsky J.L., and Morano K.A. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related Hsp70 family. J. Biol. Chem. 279 (2004) 21992-22001
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 21992-22001
-
-
Shaner, L.1
Trott, A.2
Goeckeler, J.L.3
Brodsky, J.L.4
Morano, K.A.5
-
18
-
-
0033785942
-
Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum
-
McClellan A.J., and Brodsky J.L. Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum. Genetics 156 (2000) 501-512
-
(2000)
Genetics
, vol.156
, pp. 501-512
-
-
McClellan, A.J.1
Brodsky, J.L.2
-
19
-
-
6344275303
-
Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast
-
Youker R.T., Walsh P., Beilharz T., Lithgow T., and Brodsky J.L. Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast. Mol. Biol. Cell 15 (2004) 4787-4797
-
(2004)
Mol. Biol. Cell
, vol.15
, pp. 4787-4797
-
-
Youker, R.T.1
Walsh, P.2
Beilharz, T.3
Lithgow, T.4
Brodsky, J.L.5
-
20
-
-
1842737657
-
cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides
-
Han W., and Christen P. cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides. FEBS Lett. 563 (2004) 146-150
-
(2004)
FEBS Lett.
, vol.563
, pp. 146-150
-
-
Han, W.1
Christen, P.2
-
21
-
-
44849097137
-
-
Kang, Y., Taldone, T., Clement, C.C., Fewell, S.W., Aguirre, J., Brodsky, J.L. and Chiosis, G. (2008) Design of a fluorescence polarization assay platform for the study of human Hsp70. Bioorg. Med. Chem. Lett. [Epub ahead of print] PMID: 18515098.
-
Kang, Y., Taldone, T., Clement, C.C., Fewell, S.W., Aguirre, J., Brodsky, J.L. and Chiosis, G. (2008) Design of a fluorescence polarization assay platform for the study of human Hsp70. Bioorg. Med. Chem. Lett. [Epub ahead of print] PMID: 18515098.
-
-
-
-
22
-
-
0031774206
-
Specific molecular chaperone interactions and an ATP-dependent conformational change are required during post-translational protein translocation into the yeast ER
-
McClellan A.J., Endres J.B., Vogel J.P., Palazzi D., Rose M.D., and Brodsky J.L. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during post-translational protein translocation into the yeast ER. Mol. Biol. Cell 9 (1998) 3533-3545
-
(1998)
Mol. Biol. Cell
, vol.9
, pp. 3533-3545
-
-
McClellan, A.J.1
Endres, J.B.2
Vogel, J.P.3
Palazzi, D.4
Rose, M.D.5
Brodsky, J.L.6
-
23
-
-
0032561360
-
Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1
-
Lu Z., and Cyr D.M. Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1. J. Biol. Chem. 273 (1998) 27824-27830
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 27824-27830
-
-
Lu, Z.1
Cyr, D.M.2
-
24
-
-
0030991023
-
Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-string protein
-
Chamberlain L.H., and Burgoyne R.D. Activation of the ATPase activity of heat-shock proteins Hsc70/Hsp70 by cysteine-string protein. Biochem. J. 322 (1997) 853-858
-
(1997)
Biochem. J.
, vol.322
, pp. 853-858
-
-
Chamberlain, L.H.1
Burgoyne, R.D.2
-
25
-
-
0028584378
-
ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain
-
Ha J.H., and McKay D.B. ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain. Biochemistry 33 (1994) 14625-14635
-
(1994)
Biochemistry
, vol.33
, pp. 14625-14635
-
-
Ha, J.H.1
McKay, D.B.2
-
26
-
-
0030589149
-
The second step of ATP binding to DnaK induces peptide release
-
Theyssen H., Schuster H.P., Packschies L., Bukau B., and Reinstein J. The second step of ATP binding to DnaK induces peptide release. J. Mol. Biol. 263 (1996) 657-670
-
(1996)
J. Mol. Biol.
, vol.263
, pp. 657-670
-
-
Theyssen, H.1
Schuster, H.P.2
Packschies, L.3
Bukau, B.4
Reinstein, J.5
-
27
-
-
0029013908
-
The role of ATP in the functional cycle of the DnaK chaperone system
-
McCarty J.S., Buchberger A., Reinstein J., and Bukau B. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249 (1995) 126-137
-
(1995)
J. Mol. Biol.
, vol.249
, pp. 126-137
-
-
McCarty, J.S.1
Buchberger, A.2
Reinstein, J.3
Bukau, B.4
-
28
-
-
0030976048
-
Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
-
Rudiger S., Germeroth L., Schneider-Mergener J., and Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16 (1997) 1501-1507
-
(1997)
EMBO J.
, vol.16
, pp. 1501-1507
-
-
Rudiger, S.1
Germeroth, L.2
Schneider-Mergener, J.3
Bukau, B.4
-
29
-
-
0035283043
-
Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone
-
Rudiger S., Schneider-Mergener J., and Bukau B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J. 20 (2001) 1042-1050
-
(2001)
EMBO J.
, vol.20
, pp. 1042-1050
-
-
Rudiger, S.1
Schneider-Mergener, J.2
Bukau, B.3
-
30
-
-
0033525198
-
The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
-
Brodsky J.L., Werner E.D., Dubas M.E., Goeckeler J.L., Kruse K.B., and McCracken A.A. The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274 (1999) 3453-3460
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 3453-3460
-
-
Brodsky, J.L.1
Werner, E.D.2
Dubas, M.E.3
Goeckeler, J.L.4
Kruse, K.B.5
McCracken, A.A.6
-
31
-
-
0032564386
-
Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ
-
Pierpaoli E.V., Gisler S.M., and Christen P. Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ. Biochemistry 37 (1998) 16741-16748
-
(1998)
Biochemistry
, vol.37
, pp. 16741-16748
-
-
Pierpaoli, E.V.1
Gisler, S.M.2
Christen, P.3
-
32
-
-
0033605086
-
Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling
-
Montgomery D.L., Morimoto R.I., and Gierasch L.M. Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling. J. Mol. Biol. 286 (1999) 915-932
-
(1999)
J. Mol. Biol.
, vol.286
, pp. 915-932
-
-
Montgomery, D.L.1
Morimoto, R.I.2
Gierasch, L.M.3
-
33
-
-
36349015924
-
The Hsp110 molecular chaperone stabilizes apolipoproteinB from endoplasmic reticulum-associated degradation (ERAD)
-
Hrizo S.L., Gusarova V., Habiel D.M., Goeckeler J.L., Fisher E.A., and Brodsky J.L. The Hsp110 molecular chaperone stabilizes apolipoproteinB from endoplasmic reticulum-associated degradation (ERAD). J. Biol. Chem. 282 (2007) 32665-32675
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 32665-32675
-
-
Hrizo, S.L.1
Gusarova, V.2
Habiel, D.M.3
Goeckeler, J.L.4
Fisher, E.A.5
Brodsky, J.L.6
-
34
-
-
33646675316
-
Heat shock proteins as vaccine adjuvants in infections and cancer
-
Segal B.H., Wang X.Y., Dennis C.G., Youn R., Repasky E.A., Manjili M.H., and Subjeck J.R. Heat shock proteins as vaccine adjuvants in infections and cancer. Drug Discov. Today 11 (2006) 534-540
-
(2006)
Drug Discov. Today
, vol.11
, pp. 534-540
-
-
Segal, B.H.1
Wang, X.Y.2
Dennis, C.G.3
Youn, R.4
Repasky, E.A.5
Manjili, M.H.6
Subjeck, J.R.7
|