-
1
-
-
58849143814
-
From hatching to dispatching: The multiple cellular roles of the Hsp70 molecular chaperone machinery
-
Meimaridou, E., Gooljar, S. B. & Chapple, J. P. From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery. J. Mol. Endocrinol. 42, 1-9 (2009).
-
(2009)
J. Mol. Endocrinol.
, vol.42
, pp. 1-9
-
-
Meimaridou, E.1
Gooljar, S.B.2
Chapple, J.P.3
-
2
-
-
17044387386
-
Hsp70 chaperones: Cellular functions and molecular mechanism
-
Mayer, M. P. & Bukau, B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670-684 (2005).
-
(2005)
Cell. Mol. Life Sci.
, vol.62
, pp. 670-684
-
-
Mayer, M.P.1
Bukau, B.2
-
3
-
-
0037040541
-
Molecular chaperones in the cytosol: From nascent chain to folded protein
-
Hartl, F. U. & Hayer-Hartl, M. Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295, 1852-1858 (2002).
-
(2002)
Science
, vol.295
, pp. 1852-1858
-
-
Hartl, F.U.1
Hayer-Hartl, M.2
-
4
-
-
11444271010
-
Chaperone-assisted folding of newly synthesized proteins in the cytosol
-
Deuerling, E. & Bukau, B. Chaperone-assisted folding of newly synthesized proteins in the cytosol. Crit. Rev. Biochem. Mol. Biol. 39, 261-277 (2004).
-
(2004)
Crit. Rev. Biochem. Mol. Biol.
, vol.39
, pp. 261-277
-
-
Deuerling, E.1
Bukau, B.2
-
5
-
-
0032503968
-
Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
-
Glover, J. R. & Lindquist, S. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82 (1998).
-
(1998)
Cell
, vol.94
, pp. 73-82
-
-
Glover, J.R.1
Lindquist, S.2
-
6
-
-
0033598703
-
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
-
Goloubinoff, P., Mogk, A., Zvi, A. P., Tomoyasu, T. & Bukau, B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl Acad. Sci. USA 96, 13732-13737 (1999).
-
(1999)
Proc. Natl Acad. Sci. USA
, vol.96
, pp. 13732-13737
-
-
Goloubinoff, P.1
Mogk, A.2
Zvi, A.P.3
Tomoyasu, T.4
Bukau, B.5
-
7
-
-
84868525116
-
Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
-
Rampelt, H. et al. Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J. 31, 4221-4235 (2012).
-
(2012)
EMBO J
, vol.31
, pp. 4221-4235
-
-
Rampelt, H.1
-
8
-
-
84884589727
-
Hsp70 chaperone dynamics and molecular mechanism
-
Mayer, M. P. Hsp70 chaperone dynamics and molecular mechanism. Trends Biochem. Sci. 38, 507-514 (2013).
-
(2013)
Trends Biochem. Sci.
, vol.38
, pp. 507-514
-
-
Mayer, M.P.1
-
9
-
-
64649094781
-
Solution conformation of wild-type E. Coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
-
Bertelsen, E. B., Chang, L., Gestwicki, J. E. & Zuiderweg, E. R. P. Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc. Natl Acad. Sci. USA 106, 8471-8476 (2009).
-
(2009)
Proc. Natl Acad. Sci. USA
, vol.106
, pp. 8471-8476
-
-
Bertelsen, E.B.1
Chang, L.2
Gestwicki, J.E.3
Zuiderweg, E.R.P.4
-
10
-
-
34047268015
-
Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
-
Swain, J. F. et al. Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker. Mol. Cell 26, 27-39 (2007).
-
(2007)
Mol. Cell
, vol.26
, pp. 27-39
-
-
Swain, J.F.1
-
11
-
-
27944436648
-
Structural basis of interdomain communication in the Hsc70 chaperone
-
Jiang, J., Prasad, K., Lafer, E. M. & Sousa, R. Structural basis of interdomain communication in the Hsc70 chaperone. Mol. Cell 20, 513-524 (2005).
-
(2005)
Mol. Cell
, vol.20
, pp. 513-524
-
-
Jiang, J.1
Prasad, K.2
Lafer, E.M.3
Sousa, R.4
-
12
-
-
0033936317
-
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
-
Mayer, M. P. et al. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat. Struct. Biol. 7, 586-593 (2000).
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 586-593
-
-
Mayer, M.P.1
-
13
-
-
2442444156
-
The lid subdomain of DnaK is required for the stabilization of the substrate-binding site
-
Moro, F., Fernandez-Saiz, V. & Muga, A. The lid subdomain of DnaK is required for the stabilization of the substrate-binding site. J. Biol. Chem. 279, 19600-19606 (2004).
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 19600-19606
-
-
Moro, F.1
Fernandez-Saiz, V.2
Muga, A.3
-
14
-
-
0035920236
-
Characterization of a lidless form of the molecular chaperone DnaK: Deletion of the lid increases peptide on- and off-rate constants
-
Buczynski, G., Slepenkov, S. V., Sehorn, M. G. & Witt, S. N. Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants. J. Biol. Chem. 276, 27231-27236 (2001).
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 27231-27236
-
-
Buczynski, G.1
Slepenkov, S.V.2
Sehorn, M.G.3
Witt, S.N.4
-
15
-
-
84871689599
-
Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones
-
Kityk, R., Kopp, J., Sinning, I. & Mayer, M. P. Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Mol. Cell 48, 863-874 (2012).
-
(2012)
Mol. Cell
, vol.48
, pp. 863-874
-
-
Kityk, R.1
Kopp, J.2
Sinning, I.3
Mayer, M.P.4
-
16
-
-
84880167772
-
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
-
Qi, R. et al. Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP. Nat. Struct. Mol. Biol. 20, 900-907 (2013).
-
(2013)
Nat. Struct. Mol. Biol.
, vol.20
, pp. 900-907
-
-
Qi, R.1
-
17
-
-
0028268243
-
Kinetics of molecular chaperone action
-
Schmid, D., Baici, A., Gehring, H. & Christen, P. Kinetics of molecular chaperone action. Science 263, 971-973 (1994).
-
(1994)
Science
, vol.263
, pp. 971-973
-
-
Schmid, D.1
Baici, A.2
Gehring, H.3
Christen, P.4
-
18
-
-
84902326560
-
Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption
-
De Los Rios, P. & Barducci, A. Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption. Elife. 3, e02218 (2014).
-
(2014)
Elife
, vol.3
-
-
De Los Rios, P.1
Barducci, A.2
-
19
-
-
0025730978
-
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
-
Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C. & Zylicz, M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl Acad. Sci. USA 88, 2874-2878 (1991).
-
(1991)
Proc. Natl Acad. Sci. USA
, vol.88
, pp. 2874-2878
-
-
Liberek, K.1
Marszalek, J.2
Ang, D.3
Georgopoulos, C.4
Zylicz, M.5
-
20
-
-
0026684855
-
Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis
-
Wild, J. et al. Partial loss of function mutations in DnaK, the Escherichia coli homologue of the 70-kDa heat shock proteins, affect highly conserved amino acids implicated in ATP binding and hydrolysis. Proc. Natl Acad. Sci. USA 89, 7139-7143 (1992).
-
(1992)
Proc. Natl Acad. Sci. USA
, vol.89
, pp. 7139-7143
-
-
Wild, J.1
-
21
-
-
0028297010
-
The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171
-
Buchberger, A., Valencia, A., McMacken, R., Sander, C. & Bukau, B. The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J. 13, 1687-1695 (1994).
-
(1994)
EMBO J
, vol.13
, pp. 1687-1695
-
-
Buchberger, A.1
Valencia, A.2
McMacken, R.3
Sander, C.4
Bukau, B.5
-
22
-
-
77954947810
-
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
-
Kampinga, H. H. & Craig, E. A. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11, 579-592 (2010).
-
(2010)
Nat. Rev. Mol. Cell Biol.
, vol.11
, pp. 579-592
-
-
Kampinga, H.H.1
Craig, E.A.2
-
23
-
-
15844372190
-
A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
-
Karzai, A. W. & McMacken, R. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271, 11236-11246 (1996).
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 11236-11246
-
-
Karzai, A.W.1
McMacken, R.2
-
24
-
-
0032214832
-
J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
-
Misselwitz, B., Staeck, O. & Rapoport, T. A. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences. Mol. Cell 2, 593-603 (1998).
-
(1998)
Mol. Cell
, vol.2
, pp. 593-603
-
-
Misselwitz, B.1
Staeck, O.2
Rapoport, T.A.3
-
25
-
-
0033545978
-
Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones
-
Laufen, T. et al. Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. Proc. Natl Acad. Sci. USA 96, 5452-5457 (1999).
-
(1999)
Proc. Natl Acad. Sci. USA
, vol.96
, pp. 5452-5457
-
-
Laufen, T.1
-
26
-
-
11144224094
-
Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU
-
Silberg, J. J., Tapley, T. L., Hoff, K. G. & Vickery, L. E. Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU. J. Biol. Chem. 279, 53924-53931 (2004).
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 53924-53931
-
-
Silberg, J.J.1
Tapley, T.L.2
Hoff, K.G.3
Vickery, L.E.4
-
27
-
-
0030986955
-
Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets
-
Barouch, W., Prasad, K., Greene, L. & Eisenberg, E. Auxilin-induced interaction of the molecular chaperone Hsc70 with clathrin baskets. Biochemistry 36, 4303-4308 (1997).
-
(1997)
Biochemistry
, vol.36
, pp. 4303-4308
-
-
Barouch, W.1
Prasad, K.2
Greene, L.3
Eisenberg, E.4
-
28
-
-
84874473589
-
Allostery in the Hsp70 chaperone proteins
-
Zuiderweg, E. R. P. et al. Allostery in the Hsp70 chaperone proteins. Top. Curr. Chem. 328, 99-153 (2013).
-
(2013)
Top. Curr. Chem.
, vol.328
, pp. 99-153
-
-
Zuiderweg, E.R.P.1
-
29
-
-
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. & 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, 915-932 (1999).
-
(1999)
J. Mol. Biol.
, vol.286
, pp. 915-932
-
-
Montgomery, D.L.1
Morimoto, R.I.2
Gierasch, L.M.3
-
30
-
-
31544442176
-
Allosteric regulation of Hsp70 chaperones by a proline switch
-
Vogel, M., Bukau, B. & Mayer, M. P. Allosteric regulation of Hsp70 chaperones by a proline switch. Mol. Cell 21, 359-367 (2006).
-
(2006)
Mol. Cell
, vol.21
, pp. 359-367
-
-
Vogel, M.1
Bukau, B.2
Mayer, M.P.3
-
31
-
-
33846020582
-
Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker
-
Vogel, M., Mayer, M. P. & Bukau, B. Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker. J. Biol. Chem. 281, 38705-38711 (2006).
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 38705-38711
-
-
Vogel, M.1
Mayer, M.P.2
Bukau, B.3
-
32
-
-
34848869936
-
Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1
-
Liu, Q. & Hendrickson, W. A. Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1. Cell 131, 106-120 (2007).
-
(2007)
Cell
, vol.131
, pp. 106-120
-
-
Liu, Q.1
Hendrickson, W.A.2
-
33
-
-
80051669663
-
The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles
-
Kumar, D. P. et al. The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles. J. Mol. Biol. 411, 1099-1113 (2011).
-
(2011)
J. Mol. Biol.
, vol.411
, pp. 1099-1113
-
-
Kumar, D.P.1
-
34
-
-
77957274298
-
An interdomain sector mediating allostery in Hsp70 molecular chaperones
-
Smock, R. G. et al. An interdomain sector mediating allostery in Hsp70 molecular chaperones. Mol. Syst. Biol. 6, 414 (2010).
-
(2010)
Mol. Syst. Biol.
, vol.6
, pp. 414
-
-
Smock, R.G.1
-
35
-
-
0029037015
-
Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication
-
Buchberger, A. et al. Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem. 270, 16903-16910 (1995).
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 16903-16910
-
-
Buchberger, A.1
-
36
-
-
0030589149
-
The second step of ATP binding to DnaK induces peptide release
-
Theyssen, H., Schuster, H. P., Packschies, L., Bukau, B. & Reinstein, J. The second step of ATP binding to DnaK induces peptide release. J. Mol. Biol. 263, 657-670 (1996).
-
(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
-
37
-
-
0037413822
-
Interdomain interaction through helices A and B of DnaK peptide binding domain
-
Moro, F., Fernández, V. & Muga, A. Interdomain interaction through helices A and B of DnaK peptide binding domain. FEBS Lett. 533, 119-123 (2003).
-
(2003)
FEBS Lett.
, vol.533
, pp. 119-123
-
-
Moro, F.1
Fernández, V.2
Muga, A.3
-
38
-
-
0029013908
-
The role of ATP in the functional cycle of the DnaK chaperone system
-
McCarty, J. S., Buchberger, A., Reinstein, J. & Bukau, B. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249, 126-137 (1995).
-
(1995)
J. Mol. Biol.
, vol.249
, pp. 126-137
-
-
McCarty, J.S.1
Buchberger, A.2
Reinstein, J.3
Bukau, B.4
-
39
-
-
0034655949
-
The morph server: A standardized system for analysing and visualizing macromolecular motions in a database framework
-
Krebs, W. G. & Gerstein, M. The morph server: a standardized system for analysing and visualizing macromolecular motions in a database framework. Nucleic Acids Res. 28, 1665-1675 (2000).
-
(2000)
Nucleic Acids Res.
, vol.28
, pp. 1665-1675
-
-
Krebs, W.G.1
Gerstein, M.2
-
40
-
-
33644873452
-
The Database of macromolecular motions: New features added at the decade mark
-
Flores, S. et al. The Database of macromolecular motions: new features added at the decade mark. Nucleic Acids Res. 34, D296-D301 (2006).
-
(2006)
Nucleic Acids Res.
, vol.34
, pp. D296-D301
-
-
Flores, S.1
-
41
-
-
0025048776
-
Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone
-
Bukau, B. & Walker, G. C. Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone. EMBO J. 9, 4027-4036 (1990).
-
(1990)
EMBO J
, vol.9
, pp. 4027-4036
-
-
Bukau, B.1
Walker, G.C.2
-
42
-
-
0028938819
-
How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site
-
Wilbanks, S. M. & McKay, D. B. How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J. Biol. Chem. 270, 2251-2257 (1995).
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 2251-2257
-
-
Wilbanks, S.M.1
McKay, D.B.2
-
43
-
-
64649089001
-
Allostery in Hsp70 chaperones is transduced by subdomain rotations
-
Bhattacharya, A. et al. Allostery in Hsp70 chaperones is transduced by subdomain rotations. J. Mol. Biol. 388, 475-490 (2009).
-
(2009)
J. Mol. Biol.
, vol.388
, pp. 475-490
-
-
Bhattacharya, A.1
-
44
-
-
84870916379
-
An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
-
Zhuravleva, A., Clerico, E. M. & Gierasch, L. M. An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones. Cell 151, 1296-1307 (2012).
-
(2012)
Cell
, vol.151
, pp. 1296-1307
-
-
Zhuravleva, A.1
Clerico, E.M.2
Gierasch, L.M.3
-
45
-
-
33745762927
-
Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
-
Dragovic, Z., Broadley, S. A., Shomura, Y., Bracher, A. & Hartl, F. U. Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J. 25, 2519-2528 (2006).
-
(2006)
EMBO J
, vol.25
, pp. 2519-2528
-
-
Dragovic, Z.1
Broadley, S.A.2
Shomura, Y.3
Bracher, A.4
Hartl, F.U.5
-
46
-
-
84930939681
-
Substrate-binding domain conformational dynamics mediate Hsp70 allostery
-
Zhuravleva, A. & Gierasch, L. M. Substrate-binding domain conformational dynamics mediate Hsp70 allostery. Proc. Natl Acad. Sci. USA 112, E2865-E2873 (2015).
-
(2015)
Proc. Natl Acad. Sci. USA
, vol.112
, pp. E2865-E2873
-
-
Zhuravleva, A.1
Gierasch, L.M.2
-
47
-
-
0034127485
-
Structural insights into substrate binding by the molecular chaperone DnaK
-
Pellecchia, M. et al. Structural insights into substrate binding by the molecular chaperone DnaK. Nat. Struct. Biol. 7, 298-303 (2000).
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 298-303
-
-
Pellecchia, M.1
-
48
-
-
33745183353
-
Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation
-
Rist, W., Graf, C., Bukau, B. & Mayer, M. P. Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation. J. Biol. Chem. 281, 16493-16501 (2006).
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 16493-16501
-
-
Rist, W.1
Graf, C.2
Bukau, B.3
Mayer, M.P.4
-
49
-
-
0142148040
-
The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG
-
Stevens, S. Y., Cai, S., Pellecchia, M. & Zuiderweg, E. R. P. The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide NRLLLTG. Protein Sci. 12, 2588-2596 (2003).
-
(2003)
Protein Sci.
, vol.12
, pp. 2588-2596
-
-
Stevens, S.Y.1
Cai, S.2
Pellecchia, M.3
Zuiderweg, E.R.P.4
-
50
-
-
0033783190
-
Molecular basis for interactions of the DnaK chaperone with substrates
-
Mayer, M. P., Rüdiger, S. & Bukau, B. Molecular basis for interactions of the DnaK chaperone with substrates. Biol. Chem. 381, 877-885 (2000).
-
(2000)
Biol. Chem.
, vol.381
, pp. 877-885
-
-
Mayer, M.P.1
Rüdiger, S.2
Bukau, B.3
-
51
-
-
77950431096
-
The conformational dynamics of the mitochondrial Hsp70 chaperone
-
Mapa, K. et al. The conformational dynamics of the mitochondrial Hsp70 chaperone. Mol. Cell 38, 89-100 (2010).
-
(2010)
Mol. Cell
, vol.38
, pp. 89-100
-
-
Mapa, K.1
-
52
-
-
79551632223
-
Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions
-
Marcinowski, M. et al. Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nat. Struct. Mol. Biol. 18, 150-158 (2011).
-
(2011)
Nat. Struct. Mol. Biol.
, vol.18
, pp. 150-158
-
-
Marcinowski, M.1
-
53
-
-
79952364237
-
Mechanics of Hsp70 chaperones enables differential interaction with client proteins
-
Schlecht, R., Erbse, A. H., Bukau, B. & Mayer, M. P. Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat. Struct. Mol. Biol. 18, 345-351 (2011).
-
(2011)
Nat. Struct. Mol. Biol.
, vol.18
, pp. 345-351
-
-
Schlecht, R.1
Erbse, A.H.2
Bukau, B.3
Mayer, M.P.4
-
54
-
-
0032417764
-
Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone
-
Gässler, C. S. et al. Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone. Proc. Natl Acad. Sci. USA 95, 15229-15234 (1998).
-
(1998)
Proc. Natl Acad. Sci. USA
, vol.95
, pp. 15229-15234
-
-
Gässler, C.S.1
-
55
-
-
79955565642
-
Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
-
Zhuravleva, A. & Gierasch, L. M. Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones. Proc. Natl Acad. Sci. USA 108, 6987-6992 (2011).
-
(2011)
Proc. Natl Acad. Sci. USA
, vol.108
, pp. 6987-6992
-
-
Zhuravleva, A.1
Gierasch, L.M.2
-
56
-
-
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. & Goloubinoff, P. The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat. Chem. Biol. 6, 914-920 (2010).
-
(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
-
57
-
-
0025888264
-
Efficient site-directed mutagenesis using uracil-containing DNA
-
Kunkel, T. A., Bebenek, K. & McClary, J. Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol. 204, 125-139 (1991).
-
(1991)
Methods Enzymol.
, vol.204
, pp. 125-139
-
-
Kunkel, T.A.1
Bebenek, K.2
McClary, J.3
-
58
-
-
0033020519
-
Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy
-
Mayer, M. P., Laufen, T., Paal, K., McCarty, J. S. & Bukau, B. Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy. J. Mol. Biol. 289, 1131-1144 (1999).
-
(1999)
J. Mol. Biol.
, vol.289
, pp. 1131-1144
-
-
Mayer, M.P.1
Laufen, T.2
Paal, K.3
McCarty, J.S.4
Bukau, B.5
-
59
-
-
0029996090
-
Regulatory region C of the E. Coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria
-
McCarty, J. S. et al. Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria. J. Mol. Biol. 256, 829-837 (1996).
-
(1996)
J. Mol. Biol.
, vol.256
, pp. 829-837
-
-
McCarty, J.S.1
-
60
-
-
0029937037
-
Structural analysis of substrate binding by the molecular chaperone DnaK
-
Zhu, X. et al. Structural analysis of substrate binding by the molecular chaperone DnaK. Science 272, 1606-1614 (1996).
-
(1996)
Science
, vol.272
, pp. 1606-1614
-
-
Zhu, X.1
|