-
1
-
-
34250561475
-
A new puffing pattern induced by temperature shock and DNP in Drosophila
-
Ritossa F. A new puffing pattern induced by temperature shock and DNP in Drosophila. Experientia, 1962, 18: 571-573.
-
(1962)
Experientia
, vol.18
, pp. 571-573
-
-
Ritossa, F.1
-
2
-
-
0030154255
-
Discovery of the heat shock response
-
Ritossa F. Discovery of the heat shock response. Cell Stress Chaperones, 1996, 1: 97-98.
-
(1996)
Cell Stress Chaperones
, vol.1
, pp. 97-98
-
-
Ritossa, F.1
-
3
-
-
0016373748
-
Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs
-
Tissieres A, Mitchell H K, Tracy U M. Protein synthesis in salivary glands of Drosophila melanogaster: Relation to chromosome puffs. J Mol Biol, 1974, 85: 389-398.
-
(1974)
J Mol Biol
, vol.85
, pp. 389-398
-
-
Tissieres, A.1
Mitchell, H.K.2
Tracy, U.M.3
-
4
-
-
0017950371
-
Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts
-
Lemeux P G, Herendeen S L, Bloch P L, et al. Transient rates of synthesis of individual polypeptides in E. coli following temperature shifts. Cell, 1978, 13: 427-434.
-
(1978)
Cell
, vol.13
, pp. 427-434
-
-
Lemeux, P.G.1
Herendeen, S.L.2
Bloch, P.L.3
-
5
-
-
0019120707
-
Heat shock induced proteins in plant cells
-
Barnett T, Altschuler M, McDaniel C N, et al. Heat shock induced proteins in plant cells. Dev Genet, 1980, 1: 331-340.
-
(1980)
Dev Genet
, vol.1
, pp. 331-340
-
-
Barnett, T.1
Altschuler, M.2
McDaniel, C.N.3
-
6
-
-
0020031366
-
Antibodies to two major chicken heat shock proteins cross-react with similar proteins in widely divergent species
-
Kelley P M, Schlesinger M J. Antibodies to two major chicken heat shock proteins cross-react with similar proteins in widely divergent species. Mol Cell Biol, 1982, 2: 267-274.
-
(1982)
Mol Cell Biol
, vol.2
, pp. 267-274
-
-
Kelley, P.M.1
Schlesinger, M.J.2
-
8
-
-
0022555843
-
The heat shock response
-
Lindguist S. The heat shock response. Annu Rev Biochem, 1986, 55: 1151-1191.
-
(1986)
Annu Rev Biochem
, vol.55
, pp. 1151-1191
-
-
Lindguist, S.1
-
9
-
-
0027522356
-
Cells in stress: Transcriptional activation of heat shock genes
-
Morimoto R I. Cells in stress: transcriptional activation of heat shock genes. Science, 1993, 259: 1409-1410.
-
(1993)
Science
, vol.259
, pp. 1409-1410
-
-
Morimoto, R.I.1
-
10
-
-
15544377794
-
Molecular and evolutionary basis of the cellular stress response
-
Kültz D. Molecular and evolutionary basis of the cellular stress response. Annu Rev Physiol, 2005, 67: 225-257.
-
(2005)
Annu Rev Physiol
, vol.67
, pp. 225-257
-
-
Kültz, D.1
-
11
-
-
0023900525
-
Homologous plant and bacterial proteins chaperone oligomeric protein assembly
-
Hemmingsen S M, Woolford C, van der Vies S M, et al. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature, 1988, 333: 330-334.
-
(1988)
Nature
, vol.333
, pp. 330-334
-
-
Hemmingsen, S.M.1
Woolford, C.2
van der Vies, S.M.3
-
12
-
-
0024578552
-
GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
-
Goloubinoff P, Gatenby A A, Lorimer G H. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature, 1989, 337: 44-47.
-
(1989)
Nature
, vol.337
, pp. 44-47
-
-
Goloubinoff, P.1
Gatenby, A.A.2
Lorimer, G.H.3
-
13
-
-
0024298711
-
A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
-
Deshaies R J, Koch B D, Werner-Washburne M, et al. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature, 1988, 332: 800-805.
-
(1988)
Nature
, vol.332
, pp. 800-805
-
-
Deshaies, R.J.1
Koch, B.D.2
Werner-Washburne, M.3
-
14
-
-
0024298706
-
70K heat shock related proteins stimulate protein translocation into microsomes
-
Chirico W J, Waters M G, Blobel G. 70K heat shock related proteins stimulate protein translocation into microsomes. Nature, 1988, 332: 805-810.
-
(1988)
Nature
, vol.332
, pp. 805-810
-
-
Chirico, W.J.1
Waters, M.G.2
Blobel, G.3
-
15
-
-
0023761756
-
Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein
-
Bochkareva E S, Lissin N M, Girshovich A S. Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. Nature, 1988, 336: 254-257.
-
(1988)
Nature
, vol.336
, pp. 254-257
-
-
Bochkareva, E.S.1
Lissin, N.M.2
Girshovich, A.S.3
-
16
-
-
0025303147
-
Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
-
Beckmann R P, Mizzen L A, Welch W J. Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science, 1990, 248: 850-854.
-
(1990)
Science
, vol.248
, pp. 850-854
-
-
Beckmann, R.P.1
Mizzen, L.A.2
Welch, W.J.3
-
17
-
-
0026540796
-
Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli
-
Sherman M Y, Goldberg A L. Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli. EMBO J, 1992, 11: 71-77.
-
(1992)
EMBO J
, vol.11
, pp. 71-77
-
-
Sherman, M.Y.1
Goldberg, A.L.2
-
18
-
-
0030052910
-
Roles of Molecular Chaperones in Protein Degradation
-
Hayes S A, Dice J F. Roles of Molecular Chaperones in Protein Degradation. J Cell Biol, 1996, 132: 255-258.
-
(1996)
J Cell Biol
, vol.132
, pp. 255-258
-
-
Hayes, S.A.1
Dice, J.F.2
-
19
-
-
0027996115
-
Protein disaggregation mediated by heat-shock protein Hsp104
-
Parsell D A, Kowal A S, Singer M A, et al. Protein disaggregation mediated by heat-shock protein Hsp104. Nature, 1994, 372: 475-478.
-
(1994)
Nature
, vol.372
, pp. 475-478
-
-
Parsell, D.A.1
Kowal, A.S.2
Singer, M.A.3
-
20
-
-
0022969885
-
Speculations on the functions of the major heat shock and glucose-regulated proteins
-
Pelham H R B. Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell, 1986, 46: 959-961.
-
(1986)
Cell
, vol.46
, pp. 959-961
-
-
Pelham, H.R.B.1
-
21
-
-
0023668329
-
Proteins as molecular Chaperones
-
Ellis J. Proteins as molecular Chaperones. Nature, 1987, 328: 378-379.
-
(1987)
Nature
, vol.328
, pp. 378-379
-
-
Ellis, J.1
-
23
-
-
0027184721
-
Molecular chaperone functions of heat-shock proteins
-
Hendrick J P, Hartl F. Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem, 1993, 62: 349-384.
-
(1993)
Annu Rev Biochem
, vol.62
, pp. 349-384
-
-
Hendrick, J.P.1
Hartl, F.2
-
24
-
-
33646127577
-
Molecular chaperones and protein quality control
-
Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell, 2006, 125:443-451.
-
(2006)
Cell
, vol.125
, pp. 443-451
-
-
Bukau, B.1
Weissman, J.2
Horwich, A.3
-
25
-
-
0000832972
-
Evidence for a negative-feedback mechanism in the biosynthesis of isoleucine
-
Umbarger H E. Evidence for a negative-feedback mechanism in the biosynthesis of isoleucine. Science, 1956, 123: 848.
-
(1956)
Science
, vol.123
, pp. 848
-
-
Umbarger, H.E.1
-
26
-
-
0001738509
-
Control of pyrimidine biosynthesis in E. coli by a feedback mechanism
-
Yates R A, Pardee A B. Control of pyrimidine biosynthesis in E. coli by a feedback mechanism. J Biol Chem, 1956, 221: 743-756.
-
(1956)
J Biol Chem
, vol.221
, pp. 743-756
-
-
Yates, R.A.1
Pardee, A.B.2
-
27
-
-
32344434479
-
The changing landscape of protein allostery
-
Swain J F, Gierasch L M. The changing landscape of protein allostery. Curr Opin Struct Biol, 2006, 16: 102-108.
-
(2006)
Curr Opin Struct Biol
, vol.16
, pp. 102-108
-
-
Swain, J.F.1
Gierasch, L.M.2
-
28
-
-
0032489016
-
The Hsp70 and Hsp60 chaperone machines
-
Bukau B, Horwich A L. The Hsp70 and Hsp60 chaperone machines. Cell, 1998, 92: 351-366.
-
(1998)
Cell
, vol.92
, pp. 351-366
-
-
Bukau, B.1
Horwich, A.L.2
-
29
-
-
39149143645
-
Chaperone machines in action
-
Saibil H R. Chaperone machines in action. Curr Opin Struc Biol, 2008, 18: 35-42.
-
(2008)
Curr Opin Struc Biol
, vol.18
, pp. 35-42
-
-
Saibil, H.R.1
-
31
-
-
0030592538
-
The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
-
Roseman A M, Chen S, White H, et al. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell, 1996, 87: 241-251.
-
(1996)
Cell
, vol.87
, pp. 241-251
-
-
Roseman, A.M.1
Chen, S.2
White, H.3
-
33
-
-
0031444238
-
Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
-
Prodromou C, Roe S M, O'Brien R, et al. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell, 1997, 90: 65-75.
-
(1997)
Cell
, vol.90
, pp. 65-75
-
-
Prodromou, C.1
Roe, S.M.2
O'Brien, R.3
-
34
-
-
33750008686
-
Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
-
Shiau A K, Harris S F, Southworth D R, et al. Structural analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell, 2006, 127: 329-340.
-
(2006)
Cell
, vol.127
, pp. 329-340
-
-
Shiau, A.K.1
Harris, S.F.2
Southworth, D.R.3
-
35
-
-
31444442284
-
Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides
-
Bosl B, Grimminger B, Walter S. Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides. J Biol Chem, 2005, 280: 38170-38176.
-
(2005)
J Biol Chem
, vol.280
, pp. 38170-38176
-
-
Bosl, B.1
Grimminger, B.2
Walter, S.3
-
36
-
-
1642267570
-
Mechanisms of ATPases-a multi-disciplinary approach
-
Rappas M, Niwa H, Zhang X. Mechanisms of ATPases-a multi-disciplinary approach. Curr Protein Pept Sci, 2004, 5:89-105.
-
(2004)
Curr Protein Pept Sci
, vol.5
, pp. 89-105
-
-
Rappas, M.1
Niwa, H.2
Zhang, X.3
-
37
-
-
0043028205
-
What is a co-chaperone?
-
Caplan A J. What is a co-chaperone? Cell Stress Chaperones, 2003, 8: 105-107.
-
(2003)
Cell Stress Chaperones
, vol.8
, pp. 105-107
-
-
Caplan, A.J.1
-
38
-
-
0018193766
-
Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication
-
Yochem J, Uchida H, Sunshine M, et al. Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication. Mol Gen Genet, 1978, 164: 9-14.
-
(1978)
Mol Gen Genet
, vol.164
, pp. 9-14
-
-
Yochem, J.1
Uchida, H.2
Sunshine, M.3
-
39
-
-
0017395649
-
Initiation of DNA-replication of bacteriophage-lambda in Escherichia coli-K12
-
Saito H, Uchida H. Initiation of DNA-replication of bacteriophage-lambda in Escherichia coli-K12. J Mol Biol, 1977, 113: 1-25.
-
(1977)
J Mol Biol
, vol.113
, pp. 1-25
-
-
Saito, H.1
Uchida, H.2
-
40
-
-
0023622594
-
The grpE protein of Escherichia coli
-
Zylicz M, Ang D, Georgopolous C. The grpE protein of Escherichia coli. J Biol Chem, 1987, 262: 17437-17442.
-
(1987)
J Biol Chem
, vol.262
, pp. 17437-17442
-
-
Zylicz, M.1
Ang, D.2
Georgopolous, C.3
-
41
-
-
0025730978
-
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
-
Liberek K, Marszalek J, Ang D, et al. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci U S A, 1991, 88: 2874-2878.
-
(1991)
Proc Natl Acad Sci U S A
, vol.88
, pp. 2874-2878
-
-
Liberek, K.1
Marszalek, J.2
Ang, D.3
-
42
-
-
0026596223
-
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
-
Langer T, Lu C, Echols H, et al. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature, 1992, 356: 683-689.
-
(1992)
Nature
, vol.356
, pp. 683-689
-
-
Langer, T.1
Lu, C.2
Echols, H.3
-
43
-
-
0028151509
-
The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE
-
Szabo A, Langer T, Schröder H, et al. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc Natl Acad Sci USA, 1994, 91: 10345-10349.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 10345-10349
-
-
Szabo, A.1
Langer, T.2
Schröder, H.3
-
44
-
-
0028842615
-
Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
-
Höhfeld J, Minami Y, Hartl F U. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell, 1995, 83: 589-598.
-
(1995)
Cell
, vol.83
, pp. 589-598
-
-
Höhfeld, J.1
Minami, Y.2
Hartl, F.U.3
-
45
-
-
0024820705
-
Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
-
Goloubinoff P, Christeller J T, Gatenby A A, et al. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature, 1989, 342: 884-889.
-
(1989)
Nature
, vol.342
, pp. 884-889
-
-
Goloubinoff, P.1
Christeller, J.T.2
Gatenby, A.A.3
-
46
-
-
0028785583
-
Mechanism of GroEL action: Productive release of polypeptide from a sequestered position under GroES
-
Weissman J S, Hohl C M, Kovalenko O, et al. Mechanism of GroEL action: productive release of polypeptide from a sequestered position under GroES. Cell, 1995, 83: 577-587.
-
(1995)
Cell
, vol.83
, pp. 577-587
-
-
Weissman, J.S.1
Hohl, C.M.2
Kovalenko, O.3
-
47
-
-
11844276669
-
Functional specificity of co-chaperone interactions with Hsp90 client proteins
-
Riggs D L, Cox M B, Cheung-Flynn J, et al. Functional specificity of co-chaperone interactions with Hsp90 client proteins. Crit Rev Biochem Mol Biol, 2004, 39: 279-295.
-
(2004)
Crit Rev Biochem Mol Biol
, vol.39
, pp. 279-295
-
-
Riggs, D.L.1
Cox, M.B.2
Cheung-Flynn, J.3
-
48
-
-
0032924953
-
Hsp90 & Co. - A holding for folding
-
Buchner J. Hsp90 & Co. - a holding for folding. Trends Biochem Sci, 1999, 24: 136-141.
-
(1999)
Trends Biochem Sci
, vol.24
, pp. 136-141
-
-
Buchner, J.1
-
49
-
-
0027220168
-
Heat shock of Escherichia coli increases binding of dnaK (the hsp70 homolog) to polypeptides by promoting its phosphorylation
-
Sherman M Y, Goldberg A L. Heat shock of Escherichia coli increases binding of dnaK (the hsp70 homolog) to polypeptides by promoting its phosphorylation. Proc Natl Acad Sci USA, 1993, 90: 8648-8652.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 8648-8652
-
-
Sherman, M.Y.1
Goldberg, A.L.2
-
50
-
-
0026519887
-
Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation
-
Sherman M Y, Goldberg A L. Heat shock in Escherichia coli alters the protein-binding properties of the chaperonin groEL by inducing its phosphorylation, Nature, 1992b, 357: 167-169.
-
(1992)
Nature
, vol.357
, pp. 167-169
-
-
Sherman, M.Y.1
Goldberg, A.L.2
-
51
-
-
0028075838
-
Heat shock-induced phosphorylation of GroEL alters its binding and dissociation from unfolded proteins
-
Sherman M, Goldberg A L. Heat shock-induced phosphorylation of GroEL alters its binding and dissociation from unfolded proteins. J Biol Chem, 1994, 269: 31479-31483.
-
(1994)
J Biol Chem
, vol.269
, pp. 31479-31483
-
-
Sherman, M.1
Goldberg, A.L.2
-
52
-
-
0028346451
-
Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27
-
Kato K, Hasegawa K, Goto S, et al. Dissociation as a result of phosphorylation of an aggregated form of the small stress protein, hsp27. J Biol Chem, 1994, 269: 11274-11278.
-
(1994)
J Biol Chem
, vol.269
, pp. 11274-11278
-
-
Kato, K.1
Hasegawa, K.2
Goto, S.3
-
53
-
-
0033927557
-
Structure and function of small heat shock/alphacrystallin proteins: Established concepts and emerging ideas
-
MacRae T H. Structure and function of small heat shock/alphacrystallin proteins: established concepts and emerging ideas. Cell Mol Life Sci, 2000, 57: 899-913.
-
(2000)
Cell Mol Life Sci
, vol.57
, pp. 899-913
-
-
MacRae, T.H.1
-
54
-
-
20844444338
-
S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities
-
Martínez-Ruiz A, Villanueva L, González de Orduña C, et al. S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities. Proc Natl Acad Sci USA, 2005, 102: 8525-8530.
-
(2005)
Proc Natl Acad Sci USA
, vol.102
, pp. 8525-8530
-
-
Martínez-Ruiz, A.1
Villanueva, L.2
González de Orduña, C.3
-
55
-
-
0033524938
-
Chaperone activity with a redox switch
-
Jakob U, Muse W, Eser M, et al. Chaperone activity with a redox switch. Cell, 1999, 96: 341-352.
-
(1999)
Cell
, vol.96
, pp. 341-352
-
-
Jakob, U.1
Muse, W.2
Eser, M.3
-
56
-
-
11444262208
-
Beyond transcription-new mechanisms for the regulation of molecular chaperones
-
Winter J, Jakob U. Beyond transcription-new mechanisms for the regulation of molecular chaperones. Crit Rev Biochem Mol Biol, 2004, 39: 297-317.
-
(2004)
Crit Rev Biochem Mol Biol
, vol.39
, pp. 297-317
-
-
Winter, J.1
Jakob, U.2
-
57
-
-
0033485868
-
Hsp26: A temperature-regulated chaperone
-
Haslbeck M, Walke S, Stromer T, et al. Hsp26: a temperature-regulated chaperone. EMBO J, 1999, 18: 6744-6751.
-
(1999)
EMBO J
, vol.18
, pp. 6744-6751
-
-
Haslbeck, M.1
Walke, S.2
Stromer, T.3
-
58
-
-
0032898210
-
The Mycobacterium tuberculosis small heat shock protein HSP16.3 exposes hydrophobic surfaces at mild conditions: Conformational flexibility and molecular chaperone activity
-
Yang H, Huang S, Dai H, et al. The Mycobacterium tuberculosis small heat shock protein HSP16.3 exposes hydrophobic surfaces at mild conditions: conformational flexibility and molecular chaperone activity. Protein Science, 1999, 8: 174-179.
-
(1999)
Protein Science
, vol.8
, pp. 174-179
-
-
Yang, H.1
Huang, S.2
Dai, H.3
-
59
-
-
0034809339
-
Preheat treatment for mycobacterium tuberculosis Hsp16.3: Correlation between a structural phase change at 60°C and a dramatic increase in chaperone-like activity
-
Mao Q, Ke D, Feng X, et al. Preheat treatment for mycobacterium tuberculosis Hsp16.3: correlation between a structural phase change at 60°C and a dramatic increase in chaperone-like activity. Biochem Biophys Res Commun, 2001, 284: 942-947.
-
(2001)
Biochem Biophys Res Commun
, vol.284
, pp. 942-947
-
-
Mao, Q.1
Ke, D.2
Feng, X.3
-
60
-
-
0036306310
-
Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisit for chaperone-like activity
-
Gu L, Abulimiti A, Li W, et al. Monodisperse Hsp16.3 nonamer exhibits dynamic dissociation and reassociation, with the nonamer dissociation prerequisit for chaperone-like activity. J Mol Biol, 2002, 319: 517-526.
-
(2002)
J Mol Biol
, vol.319
, pp. 517-526
-
-
Gu, L.1
Abulimiti, A.2
Li, W.3
-
61
-
-
0141682090
-
Small Heat Shock Protein Hsp16.3 Modulates Its Chaperone Activity by Adjusting the Rate of Oligomeric Dissociation
-
Fu X, Liu C, Liu Y, et al. Small Heat Shock Protein Hsp16.3 Modulates Its Chaperone Activity by Adjusting the Rate of Oligomeric Dissociation. Biochem Biophys Res Commun, 2003, 310: 412-420.
-
(2003)
Biochem Biophys Res Commun
, vol.310
, pp. 412-420
-
-
Fu, X.1
Liu, C.2
Liu, Y.3
-
62
-
-
1542617030
-
Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis
-
Fu X, Chang Z. Temperature-dependent subunit exchange and chaperone-like activities of Hsp16.3, a small heat shock protein from Mycobacterium tuberculosis. Biochem Biophys Res Commun, 2004, 316: 291-299.
-
(2004)
Biochem Biophys Res Commun
, vol.316
, pp. 291-299
-
-
Fu, X.1
Chang, Z.2
-
63
-
-
14844355848
-
The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli
-
Jiao W, Qian M, Li P, et al. The essential role of the flexible termini in the temperature-responsiveness of the oligomeric state and chaperone-like activity for the polydisperse small heat shock protein IbpB from Escherichia coli. J Mol Biol, 2005, 347(4): 871-884.
-
(2005)
J Mol Biol
, vol.347
, Issue.4
, pp. 871-884
-
-
Jiao, W.1
Qian, M.2
Li, P.3
-
64
-
-
14844292563
-
A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins
-
Fu X, Zhang H, Zhang X, et al. A dual role for the N-terminal region of Mycobacterium tuberculosis Hsp16.3 in self-oligomerization and binding denaturing substrate proteins. J Biol Chem, 2005, 280: 6337-6348.
-
(2005)
J Biol Chem
, vol.280
, pp. 6337-6348
-
-
Fu, X.1
Zhang, H.2
Zhang, X.3
-
65
-
-
39749148886
-
The dramatically increased chaperone activity of small heat shock protein IbpB is retained for an extended period of time after the stress condition is removed
-
Jiao W, Hong W, Li P, et al. The dramatically increased chaperone activity of small heat shock protein IbpB is retained for an extended period of time after the stress condition is removed. Biochem J, 2008, 410: 63-70.
-
(2008)
Biochem J
, vol.410
, pp. 63-70
-
-
Jiao, W.1
Hong, W.2
Li, P.3
-
66
-
-
0031589203
-
GroES binding regulates GroEL chaperonin activity under heat shock
-
Goloubinoff P, Diamant S, Weiss C, et al. GroES binding regulates GroEL chaperonin activity under heat shock. FEBS Lett, 1997, 407: 215-219.
-
(1997)
FEBS Lett
, vol.407
, pp. 215-219
-
-
Goloubinoff, P.1
Diamant, S.2
Weiss, C.3
-
67
-
-
0032483997
-
GroEL under heat-shock: Switching from a folding to a storing function
-
Llorca O, Galán A, Carrascosa J L, et al. GroEL under heat-shock: Switching from a folding to a storing function. J Biol Chem, 1998, 273: 32587-32594.
-
(1998)
J Biol Chem
, vol.273
, pp. 32587-32594
-
-
Llorca, O.1
Galán, A.2
Carrascosa, J.L.3
-
68
-
-
0035794207
-
Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system
-
Grimshaw J P, Jelesarov I, Schönfeld H J, et al. Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J Biol Chem, 2001, 276: 6098-6104.
-
(2001)
J Biol Chem
, vol.276
, pp. 6098-6104
-
-
Grimshaw, J.P.1
Jelesarov, I.2
Schönfeld, H.J.3
-
69
-
-
22844435320
-
Periplasmic protein hdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation
-
Hong W, Jiao W, Hu J, et al. Periplasmic protein hdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation. J Biol Chem, 2005, 280: 27029-27034.
-
(2005)
J Biol Chem
, vol.280
, pp. 27029-27034
-
-
Hong, W.1
Jiao, W.2
Hu, J.3
-
70
-
-
44449168124
-
Conserved amphiphilic feature Is essential for periplasmic chaperone HdeA to support acid resistance in enteric bacteria
-
Wu Y, Hong W, Zhang L, et al. Conserved amphiphilic feature Is essential for periplasmic chaperone HdeA to support acid resistance in enteric bacteria. Biochem J, 2008, 412: 389-397.
-
(2008)
Biochem J
, vol.412
, pp. 389-397
-
-
Wu, Y.1
Hong, W.2
Zhang, L.3
-
71
-
-
50149107174
-
Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins
-
Jiang J, Zhang X, Chen Y, et al. Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins. Proc Natl Acad Sci USA, 2008, 105: 11939-11944.
-
(2008)
Proc Natl Acad Sci USA
, vol.105
, pp. 11939-11944
-
-
Jiang, J.1
Zhang, X.2
Chen, Y.3
|