-
1
-
-
0034607644
-
GroEL binds artificial proteins with random sequences
-
Aoki, K., Motojima, F., Taguchi, H., Yomo, T., and Yoshida, M. (2000). GroEL binds artificial proteins with random sequences. J. Biol. Chem. 275, 13755-13758.
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 13755-13758
-
-
Aoki, K.1
Motojima, F.2
Taguchi, H.3
Yomo, T.4
Yoshida, M.5
-
2
-
-
39349083915
-
Adapting proteostasis for disease intervention
-
Balch, W.E., Morimoto, R.I., Dillin, A., and Kelly, J.W. (2008). Adapting proteostasis for disease intervention. Science 319, 916-919.
-
(2008)
Science
, vol.319
, pp. 916-919
-
-
Balch, W.E.1
Morimoto, R.I.2
Dillin, A.3
Kelly, J.W.4
-
3
-
-
0024044382
-
Ancient heat shock gene is dispensable
-
Bardwell, J.C., and Craig, E.A. (1988). Ancient heat shock gene is dispensable. J. Bacteriol. 170, 2977-2983.
-
(1988)
J. Bacteriol.
, vol.170
, pp. 2977-2983
-
-
Bardwell, J.C.1
Craig, E.A.2
-
4
-
-
84872272432
-
Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness
-
Bershtein, S., Mu, W., Serohijos, A.W., Zhou, J., and Shakhnovich, E.I. (2013). Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness. Mol. Cell 49, 133-144.
-
(2013)
Mol. Cell
, vol.49
, pp. 133-144
-
-
Bershtein, S.1
Mu, W.2
Serohijos, A.W.3
Zhou, J.4
Shakhnovich, E.I.5
-
5
-
-
84890857259
-
Exploration of alternate catalytic mechanisms and optimization strategies for retroaldolase design
-
Bjelic, S., Kipnis, Y., Wang, L., Pianowski, Z., Vorobiev, S., Su, M., Seetharaman, J., Xiao, R., Kornhaber, G., Hunt, J.F., et al. (2014). Exploration of alternate catalytic mechanisms and optimization strategies for retroaldolase design. J. Mol. Biol. 426, 256-271.
-
(2014)
J. Mol. Biol.
, vol.426
, pp. 256-271
-
-
Bjelic, S.1
Kipnis, Y.2
Wang, L.3
Pianowski, Z.4
Vorobiev, S.5
Su, M.6
Seetharaman, J.7
Xiao, R.8
Kornhaber, G.9
Hunt, J.F.10
-
6
-
-
84871267951
-
Cumulative impact of chaperone-mediated folding on genome evolution
-
Bogumil, D., and Dagan, T. (2012). Cumulative impact of chaperone-mediated folding on genome evolution. Biochemistry 51, 9941-9953.
-
(2012)
Biochemistry
, vol.51
, pp. 9941-9953
-
-
Bogumil, D.1
Dagan, T.2
-
7
-
-
84874943923
-
Early folding events protect aggregation-prone regions of a β-rich protein
-
Budyak, I.L., Krishnan, B., Marcelino-Cruz, A.M., Ferrolino, M.C., Zhuravleva, A., and Gierasch, L.M. (2013). Early folding events protect aggregation-prone regions of a β-rich protein. Structure 21, 476-485.
-
(2013)
Structure
, vol.21
, pp. 476-485
-
-
Budyak, I.L.1
Krishnan, B.2
Marcelino-Cruz, A.M.3
Ferrolino, M.C.4
Zhuravleva, A.5
Gierasch, L.M.6
-
8
-
-
84861139210
-
DnaK functions as a central hub in the E. coli chaperone network
-
Calloni, G., Chen, T., Schermann, S.M., Chang, H.C., Genevaux, P., Agostini, F., Tartaglia, G.G., Hayer-Hartl, M., and Hartl, F.U. (2012). DnaK functions as a central hub in the E. coli chaperone network. Cell Rep. 1, 251-264.
-
(2012)
Cell Rep.
, vol.1
, pp. 251-264
-
-
Calloni, G.1
Chen, T.2
Schermann, S.M.3
Chang, H.C.4
Genevaux, P.5
Agostini, F.6
Tartaglia, G.G.7
Hayer-Hartl, M.8
Hartl, F.U.9
-
9
-
-
33750489742
-
Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL
-
Chapman, E., Farr, G.W., Usaite, R., Furtak, K., Fenton, W.A., Chaudhuri, T.K., Hondorp, E.R., Matthews, R.G., Wolf, S.G., Yates, J.R., et al. (2006). Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Proc. Natl. Acad. Sci. USA 103, 15800-15805.
-
(2006)
Proc. Natl. Acad. Sci. USA
, vol.103
, pp. 15800-15805
-
-
Chapman, E.1
Farr, G.W.2
Usaite, R.3
Furtak, K.4
Fenton, W.A.5
Chaudhuri, T.K.6
Hondorp, E.R.7
Matthews, R.G.8
Wolf, S.G.9
Yates, J.R.10
-
10
-
-
38449092312
-
Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli
-
de Marco, A. (2007). Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. Nat. Protoc. 2, 2632-2639.
-
(2007)
Nat. Protoc.
, vol.2
, pp. 2632-2639
-
-
de Marco, A.1
-
11
-
-
34347374452
-
Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli
-
de Marco, A., Deuerling, E., Mogk, A., Tomoyasu, T., and Bukau, B. (2007). Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli. BMC Biotechnol. 7, 32.
-
(2007)
BMC Biotechnol.
, vol.7
, pp. 32
-
-
de Marco, A.1
Deuerling, E.2
Mogk, A.3
Tomoyasu, T.4
Bukau, B.5
-
12
-
-
84888218153
-
Quantifying chaperone-mediated transitions in the proteostasis network of E. coli
-
Dickson, A., and Brooks, C.L., 3rd. (2013). Quantifying chaperone-mediated transitions in the proteostasis network of E. coli. PLoS Comput. Biol. 9, e1003324.
-
(2013)
PLoS Comput. Biol.
, vol.9
-
-
Dickson, A.1
Brooks, C.L.2
-
13
-
-
84886446627
-
Protein rescue from aggregates by powerful molecular chaperone machines
-
Doyle, S.M., Genest, O., and Wickner, S. (2013). Protein rescue from aggregates by powerful molecular chaperone machines. Nat. Rev. Mol. Cell Biol. 14, 617-629.
-
(2013)
Nat. Rev. Mol. Cell Biol.
, vol.14
, pp. 617-629
-
-
Doyle, S.M.1
Genest, O.2
Wickner, S.3
-
14
-
-
0030217968
-
Effect of engineering Hsp70 copy number on Hsp70 expression and tolerance of ecologically relevant heat shock in larvae and pupae of Drosophila melanogaster
-
Feder, M.E., Cartaño, N.V., Milos, L., Krebs, R.A., and Lindquist, S.L. (1996). Effect of engineering Hsp70 copy number on Hsp70 expression and tolerance of ecologically relevant heat shock in larvae and pupae of Drosophila melanogaster. J. Exp. Biol. 199, 1837-1844.
-
(1996)
J. Exp. Biol.
, vol.199
, pp. 1837-1844
-
-
Feder, M.E.1
Cartaño, N.V.2
Milos, L.3
Krebs, R.A.4
Lindquist, S.L.5
-
15
-
-
0025373255
-
Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites
-
Frieden, C. (1990). Refolding of Escherichia coli dihydrofolate reductase: sequential formation of substrate binding sites. Proc. Natl. Acad. Sci. USA 87, 4413-4416.
-
(1990)
Proc. Natl. Acad. Sci. USA
, vol.87
, pp. 4413-4416
-
-
Frieden, C.1
-
16
-
-
42549105668
-
Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview
-
Gasser, B., Saloheimo, M., Rinas, U., Dragosits, M., Rodríguez-Carmona, E., Baumann, K., Giuliani, M., Parrilli, E., Branduardi, P., Lang, C., et al. (2008). Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview. Microb. Cell Fact. 7, 11.
-
(2008)
Microb. Cell Fact.
, vol.7
, pp. 11
-
-
Gasser, B.1
Saloheimo, M.2
Rinas, U.3
Dragosits, M.4
Rodríguez-Carmona, E.5
Baumann, K.6
Giuliani, M.7
Parrilli, E.8
Branduardi, P.9
Lang, C.10
-
17
-
-
79957730170
-
Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling
-
Genest, O., Hoskins, J.R., Camberg, J.L., Doyle, S.M., and Wickner, S. (2011). Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc. Natl. Acad. Sci. USA 108, 8206-8211.
-
(2011)
Proc. Natl. Acad. Sci. USA
, vol.108
, pp. 8206-8211
-
-
Genest, O.1
Hoskins, J.R.2
Camberg, J.L.3
Doyle, S.M.4
Wickner, S.5
-
18
-
-
33644850056
-
Progressive disruption of cellular protein folding in models of polyglutamine diseases
-
Gidalevitz, T., Ben-Zvi, A., Ho, K.H., Brignull, H.R., and Morimoto, R.I. (2006). Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311, 1471-1474.
-
(2006)
Science
, vol.311
, pp. 1471-1474
-
-
Gidalevitz, T.1
Ben-Zvi, A.2
Ho, K.H.3
Brignull, H.R.4
Morimoto, R.I.5
-
19
-
-
0030444320
-
Proteases and their targets in Escherichia coli
-
Gottesman, S. (1996). Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30, 465-506.
-
(1996)
Annu. Rev. Genet.
, vol.30
, pp. 465-506
-
-
Gottesman, S.1
-
20
-
-
51949087754
-
Convergence of molecular, modeling, and systems approaches for an understanding of the Escherichia coli heat shock response
-
Guisbert, E., Yura, T., Rhodius, V.A., and Gross, C.A. (2008). Convergence of molecular, modeling, and systems approaches for an understanding of the Escherichia coli heat shock response. Microbiol. Mol. Biol. Rev. 72, 545-554.
-
(2008)
Microbiol. Mol. Biol. Rev.
, vol.72
, pp. 545-554
-
-
Guisbert, E.1
Yura, T.2
Rhodius, V.A.3
Gross, C.A.4
-
21
-
-
50049083221
-
Recognition of misfolded proteins by Lon, a AAA(+) protease
-
Gur, E., and Sauer, R.T. (2008). Recognition of misfolded proteins by Lon, a AAA(+) protease. Genes Dev. 22, 2267-2277.
-
(2008)
Genes Dev.
, vol.22
, pp. 2267-2277
-
-
Gur, E.1
Sauer, R.T.2
-
22
-
-
84892475033
-
Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge
-
Hingorani, K.S., and Gierasch, L.M. (2014). Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge. Curr. Opin. Struct. Biol. 24, 81-90.
-
(2014)
Curr. Opin. Struct. Biol.
, vol.24
, pp. 81-90
-
-
Hingorani, K.S.1
Gierasch, L.M.2
-
23
-
-
2942755215
-
Stress induced by recombinant protein production in Escherichia coli
-
Hoffmann, F., and Rinas, U. (2004). Stress induced by recombinant protein production in Escherichia coli. Adv. Biochem. Eng. Biotechnol. 89, 73-92.
-
(2004)
Adv. Biochem. Eng. Biotechnol.
, vol.89
, pp. 73-92
-
-
Hoffmann, F.1
Rinas, U.2
-
24
-
-
70350020881
-
Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding
-
Horwich, A.L., and Fenton, W.A. (2009). Chaperonin-mediated protein folding: using a central cavity to kinetically assist polypeptide chain folding. Q. Rev. Biophys. 42, 83-116.
-
(2009)
Q. Rev. Biophys.
, vol.42
, pp. 83-116
-
-
Horwich, A.L.1
Fenton, W.A.2
-
25
-
-
84878948560
-
Molecular chaperone functions in protein folding and proteostasis
-
Kim, Y.E., Hipp, M.S., Bracher, A., Hayer-Hartl, M., and Hartl, F.U. (2013). Molecular chaperone functions in protein folding and proteostasis. Annu. Rev. Biochem. 82, 323-355.
-
(2013)
Annu. Rev. Biochem.
, vol.82
, pp. 323-355
-
-
Kim, Y.E.1
Hipp, M.S.2
Bracher, A.3
Hayer-Hartl, M.4
Hartl, F.U.5
-
26
-
-
0028774713
-
Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid
-
Kleywegt, G.J., Bergfors, T., Senn, H., Le Motte, P., Gsell, B., Shudo, K., and Jones, T.A. (1994). Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid. Structure 2, 1241-1258.
-
(1994)
Structure
, vol.2
, pp. 1241-1258
-
-
Kleywegt, G.J.1
Bergfors, T.2
Senn, H.3
Le Motte, P.4
Gsell, B.5
Shudo, K.6
Jones, T.A.7
-
27
-
-
0035987265
-
The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
-
Kuczyńska-Wiśnik, D., Kedzierska, S., Matuszewska, E., Lund, P., Taylor, A., Lipińska, B., and Laskowska, E. (2002). The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock. Microbiology 148, 1757-1765.
-
(2002)
Microbiology
, vol.148
, pp. 1757-1765
-
-
Kuczyńska-Wiśnik, D.1
Kedzierska, S.2
Matuszewska, E.3
Lund, P.4
Taylor, A.5
Lipińska, B.6
Laskowska, E.7
-
28
-
-
0025840379
-
The chaperonin GroEL binds a polypeptide in an a-helical conformation
-
Landry, S.J., and Gierasch, L.M. (1991). The chaperonin GroEL binds a polypeptide in an a-helical conformation. Biochemistry 30, 7359-7362.
-
(1991)
Biochemistry
, vol.30
, pp. 7359-7362
-
-
Landry, S.J.1
Gierasch, L.M.2
-
29
-
-
0026596223
-
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperonemediated protein folding
-
Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M.K., and Hartl, F.U. (1992). Successive action of DnaK, DnaJ and GroEL along the pathway of chaperonemediated protein folding. Nature 356, 683-689.
-
(1992)
Nature
, vol.356
, pp. 683-689
-
-
Langer, T.1
Lu, C.2
Echols, H.3
Flanagan, J.4
Hayer, M.K.5
Hartl, F.U.6
-
30
-
-
84896923527
-
Small molecule probes to quantify the functional fraction of a specific protein in a cell with minimal folding equilibrium shifts
-
Liu, Y., Tan, Y.L., Zhang, X., Bhabha, G., Ekiert, D.C., Genereux, J.C., Cho, Y., Kipnis, Y., Bjelic, S., Baker, D., and Kelly, J.W. (2014). Small molecule probes to quantify the functional fraction of a specific protein in a cell with minimal folding equilibrium shifts. Proc. Natl. Acad. Sci. USA 111, 4449-4454.
-
(2014)
Proc. Natl. Acad. Sci. USA
, vol.111
, pp. 4449-4454
-
-
Liu, Y.1
Tan, Y.L.2
Zhang, X.3
Bhabha, G.4
Ekiert, D.C.5
Genereux, J.C.6
Cho, Y.7
Kipnis, Y.8
Bjelic, S.9
Baker, D.10
Kelly, J.W.11
-
31
-
-
79955813920
-
Strain engineering for improved expression of recombinant proteins in bacteria
-
Makino, T., Skretas, G., and Georgiou, G. (2011). Strain engineering for improved expression of recombinant proteins in bacteria. Microb. Cell Fact. 10, 32.
-
(2011)
Microb. Cell Fact.
, vol.10
, pp. 32
-
-
Makino, T.1
Skretas, G.2
Georgiou, G.3
-
32
-
-
17044387386
-
Hsp70 chaperones: cellular functions and molecular mechanism
-
Mayer, M.P., and Bukau, B. (2005). Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670-684.
-
(2005)
Cell. Mol. Life Sci.
, vol.62
, pp. 670-684
-
-
Mayer, M.P.1
Bukau, B.2
-
33
-
-
84896846203
-
Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins
-
Nakamoto, H., Fujita, K., Ohtaki, A., Watanabe, S., Narumi, S., Maruyama, T., Suenaga, E., Misono, T.S., Kumar, P.K., Goloubinoff, P., and Yoshikawa, H. (2014). Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins. J. Biol. Chem. 289, 6110-6119.
-
(2014)
J. Biol. Chem.
, vol.289
, pp. 6110-6119
-
-
Nakamoto, H.1
Fujita, K.2
Ohtaki, A.3
Watanabe, S.4
Narumi, S.5
Maruyama, T.6
Suenaga, E.7
Misono, T.S.8
Kumar, P.K.9
Goloubinoff, P.10
Yoshikawa, H.11
-
34
-
-
78650963274
-
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
-
Olzscha, H., Schermann, S.M., Woerner, A.C., Pinkert, S., Hecht, M.H., Tartaglia, G.G., Vendruscolo, M., Hayer-Hartl, M., Hartl, F.U., and Vabulas, R.M. (2011). Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144, 67-78.
-
(2011)
Cell
, vol.144
, pp. 67-78
-
-
Olzscha, H.1
Schermann, S.M.2
Woerner, A.C.3
Pinkert, S.4
Hecht, M.H.5
Tartaglia, G.G.6
Vendruscolo, M.7
Hayer-Hartl, M.8
Hartl, F.U.9
Vabulas, R.M.10
-
35
-
-
33746364784
-
Structure and mechanism of the Hsp90 molecular chaperone machinery
-
Pearl, L.H., and Prodromou, C. (2006). Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu. Rev. Biochem. 75, 271-294.
-
(2006)
Annu. Rev. Biochem.
, vol.75
, pp. 271-294
-
-
Pearl, L.H.1
Prodromou, C.2
-
36
-
-
84875461582
-
Diversity in the origins of proteostasis networks-a driver for protein function in evolution
-
Powers, E.T., and Balch, W.E. (2013). Diversity in the origins of proteostasis networks-a driver for protein function in evolution. Nat. Rev. Mol. Cell Biol. 14, 237-248.
-
(2013)
Nat. Rev. Mol. Cell Biol.
, vol.14
, pp. 237-248
-
-
Powers, E.T.1
Balch, W.E.2
-
37
-
-
67650410543
-
Biological and chemical approaches to diseases of proteostasis deficiency
-
Powers, E.T., Morimoto, R.I., Dillin, A., Kelly, J.W., and Balch, W.E. (2009). Biological and chemical approaches to diseases of proteostasis deficiency. Annu. Rev. Biochem. 78, 959-991.
-
(2009)
Annu. Rev. Biochem.
, vol.78
, pp. 959-991
-
-
Powers, E.T.1
Morimoto, R.I.2
Dillin, A.3
Kelly, J.W.4
Balch, W.E.5
-
38
-
-
84861161529
-
FoldEco: a model for proteostasis in E. coli
-
Powers, E.T., Powers, D.L., and Gierasch, L.M. (2012). FoldEco: a model for proteostasis in E. coli. Cell Rep. 1, 265-276.
-
(2012)
Cell Rep.
, vol.1
, pp. 265-276
-
-
Powers, E.T.1
Powers, D.L.2
Gierasch, L.M.3
-
39
-
-
0037315208
-
Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery
-
Pratt, W.B., and Toft, D.O. (2003). Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery. Exp. Biol. Med. (Maywood) 228, 111-133.
-
(2003)
Exp. Biol. Med. (Maywood)
, vol.228
, pp. 111-133
-
-
Pratt, W.B.1
Toft, D.O.2
-
40
-
-
0037030713
-
Hsp90 as a capacitor of phenotypic variation
-
Queitsch, C., Sangster, T.A., and Lindquist, S. (2002). Hsp90 as a capacitor of phenotypic variation. Nature 417, 618-624.
-
(2002)
Nature
, vol.417
, pp. 618-624
-
-
Queitsch, C.1
Sangster, T.A.2
Lindquist, S.3
-
41
-
-
0030976048
-
Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
-
Rüdiger, S., Germeroth, L., Schneider-Mergener, J., and Bukau, B. (1997). Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16, 1501-1507.
-
(1997)
EMBO J.
, vol.16
, pp. 1501-1507
-
-
Rüdiger, S.1
Germeroth, L.2
Schneider-Mergener, J.3
Bukau, B.4
-
42
-
-
0031015737
-
Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence
-
Sawaya, M.R., and Kraut, J. (1997). Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence. Biochemistry 36, 586-603.
-
(1997)
Biochemistry
, vol.36
, pp. 586-603
-
-
Sawaya, M.R.1
Kraut, J.2
-
43
-
-
78649309029
-
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
-
Sharma, S.K., De los Rios, P., Christen, P., Lustig, A., and Goloubinoff, P. (2010). The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat. Chem. Biol. 6, 914-920.
-
(2010)
Nat. Chem. Biol.
, vol.6
, pp. 914-920
-
-
Sharma, S.K.1
De los Rios, P.2
Christen, P.3
Lustig, A.4
Goloubinoff, P.5
-
44
-
-
0026540796
-
Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli
-
Sherman, MYu, and Goldberg, A.L. (1992). Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli. EMBO J. 11, 71-77.
-
(1992)
EMBO J.
, vol.11
, pp. 71-77
-
-
Sherman, M.Y.1
Goldberg, A.L.2
-
45
-
-
0025799542
-
ClpB is the Escherichia coli heat shock protein F84.1
-
Squires, C.L., Pedersen, S., Ross, B.M., and Squires, C. (1991). ClpB is the Escherichia coli heat shock protein F84.1. J. Bacteriol. 173, 4254-4262.
-
(1991)
J. Bacteriol.
, vol.173
, pp. 4254-4262
-
-
Squires, C.L.1
Pedersen, S.2
Ross, B.M.3
Squires, C.4
-
46
-
-
0031705810
-
Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivo
-
Thomas, J.G., and Baneyx, F. (1998). Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivo. J. Bacteriol. 180, 5165-5172.
-
(1998)
J. Bacteriol.
, vol.180
, pp. 5165-5172
-
-
Thomas, J.G.1
Baneyx, F.2
-
47
-
-
66649132872
-
Chaperonin overexpression promotes genetic variation and enzyme evolution
-
Tokuriki, N., and Tawfik, D.S. (2009). Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 459, 668-673.
-
(2009)
Nature
, vol.459
, pp. 668-673
-
-
Tokuriki, N.1
Tawfik, D.S.2
-
48
-
-
0033613206
-
Basis of substrate binding by the chaperonin GroEL
-
Wang, Z., Feng, Hp., Landry, S.J., Maxwell, J., and Gierasch, L.M. (1999). Basis of substrate binding by the chaperonin GroEL. Biochemistry 38, 12537-12546.
-
(1999)
Biochemistry
, vol.38
, pp. 12537-12546
-
-
Wang, Z.1
Feng, H.P.2
Landry, S.J.3
Maxwell, J.4
Gierasch, L.M.5
-
49
-
-
31344453190
-
Substrate transfer from the chaperone Hsp70 to Hsp90
-
Wegele, H., Wandinger, S.K., Schmid, A.B., Reinstein, J., and Buchner, J. (2006). Substrate transfer from the chaperone Hsp70 to Hsp90. J. Mol. Biol. 356, 802-811.
-
(2006)
J. Mol. Biol.
, vol.356
, pp. 802-811
-
-
Wegele, H.1
Wandinger, S.K.2
Schmid, A.B.3
Reinstein, J.4
Buchner, J.5
-
50
-
-
8844251486
-
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
-
Weibezahn, J., Tessarz, P., Schlieker, C., Zahn, R., Maglica, Z., Lee, S., Zentgraf, H., Weber-Ban, E.U., Dougan, D.A., Tsai, F.T., et al. (2004). Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119, 653-665.
-
(2004)
Cell
, vol.119
, pp. 653-665
-
-
Weibezahn, J.1
Tessarz, P.2
Schlieker, C.3
Zahn, R.4
Maglica, Z.5
Lee, S.6
Zentgraf, H.7
Weber-Ban, E.U.8
Dougan, D.A.9
Tsai, F.T.10
-
51
-
-
84905976213
-
Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity
-
Weinstock, M.T., Jacobsen, M.T., and Kay, M.S. (2014). Synthesis and folding of a mirror-image enzyme reveals ambidextrous chaperone activity. Proc. Natl. Acad. Sci. USA 111, 11679-11684.
-
(2014)
Proc. Natl. Acad. Sci. USA
, vol.111
, pp. 11679-11684
-
-
Weinstock, M.T.1
Jacobsen, M.T.2
Kay, M.S.3
-
52
-
-
0027144416
-
A new method for manipulating transgenes: engineering heat tolerance in a complex, multicellular organism
-
Welte, M.A., Tetrault, J.M., Dellavalle, R.P., and Lindquist, S.L. (1993). A new method for manipulating transgenes: engineering heat tolerance in a complex, multicellular organism. Curr. Biol. 3, 842-853.
-
(1993)
Curr. Biol.
, vol.3
, pp. 842-853
-
-
Welte, M.A.1
Tetrault, J.M.2
Dellavalle, R.P.3
Lindquist, S.L.4
-
53
-
-
36049032748
-
An adaptable standard for protein export from the endoplasmic reticulum
-
Wiseman, R.L., Powers, E.T., Buxbaum, J.N., Kelly, J.W., and Balch, W.E. (2007). An adaptable standard for protein export from the endoplasmic reticulum. Cell 131, 809-821.
-
(2007)
Cell
, vol.131
, pp. 809-821
-
-
Wiseman, R.L.1
Powers, E.T.2
Buxbaum, J.N.3
Kelly, J.W.4
Balch, W.E.5
-
54
-
-
84055178649
-
High-temperature protein G is essential for activity of the Escherichia coli clustered regularly interspaced short palindromic repeats (CRISPR)/Cas system
-
Yosef, I., Goren, M.G., Kiro, R., Edgar, R., and Qimron, U. (2011). High-temperature protein G is essential for activity of the Escherichia coli clustered regularly interspaced short palindromic repeats (CRISPR)/Cas system. Proc. Natl. Acad. Sci. USA 108, 20136-20141.
-
(2011)
Proc. Natl. Acad. Sci. USA
, vol.108
, pp. 20136-20141
-
-
Yosef, I.1
Goren, M.G.2
Kiro, R.3
Edgar, R.4
Qimron, U.5
-
56
-
-
84912562059
-
Heat-shock response transcriptional program enables high-yield and highquality recombinant protein production in Escherichia coli
-
Zhang, X., Liu, Y., Genereux, J.C., Nolan, C., Singh, M., and Kelly, J.W. (2014). Heat-shock response transcriptional program enables high-yield and highquality recombinant protein production in Escherichia coli. ACS Chem. Biol. 9, 1945-1949.
-
(2014)
ACS Chem. Biol.
, vol.9
, pp. 1945-1949
-
-
Zhang, X.1
Liu, Y.2
Genereux, J.C.3
Nolan, C.4
Singh, M.5
Kelly, J.W.6
|