-
1
-
-
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
-
2
-
-
0033936317
-
Multistep mechanism of substrate binding determines chaperone activity of Hsp70
-
Mayer, M. P., Schröder, H., Rüdiger, S., Paal, K., Laufen, T., and Bukau, B. (2000) Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nat. Struct. Biol. 7, 586 -593
-
(2000)
Nat. Struct. Biol.
, vol.7
, pp. 586-593
-
-
Mayer, M.P.1
Schröder, H.2
Rüdiger, S.3
Paal, K.4
Laufen, T.5
Bukau, B.6
-
3
-
-
0026320296
-
The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein
-
Liberek, K., Skowyra, D., Zylicz, M., Johnson, C., and Georgopoulos, C. (1991) The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein. J. Biol. Chem. 266, 14491-14496
-
(1991)
J. Biol. Chem.
, vol.266
, pp. 14491-14496
-
-
Liberek, K.1
Skowyra, D.2
Zylicz, M.3
Johnson, C.4
Georgopoulos, C.5
-
4
-
-
0025730978
-
Escherichia coli Dnaj and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
-
Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C., and Zylicz, M. (1991) Escherichia coli Dnaj and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. U.S.A. 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
Georgopoulos, C.4
Zylicz, M.5
-
5
-
-
0041026092
-
Interaction of Hsp70 chaperones with substrates
-
Rüdiger, S., Buchberger, A., and Bukau, B. (1997) Interaction of Hsp70 chaperones with substrates. Nat. Struct. Biol. 4, 342-349
-
(1997)
Nat. Struct. Biol.
, vol.4
, pp. 342-349
-
-
Rüdiger, S.1
Buchberger, A.2
Bukau, B.3
-
6
-
-
0028853568
-
In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis
-
Wei, J.-Y., Gaut, J. R., and Hendershot, L. M. (1995) In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis. J. Biol. Chem. 270, 26677-26682
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 26677-26682
-
-
Wei, J.-Y.1
Gaut, J.R.2
Hendershot, L.M.3
-
7
-
-
77950431096
-
The conformational dynamics of the mitochondrial Hsp70 chaperone
-
Mapa, K., Sikor, M., Kudryavtsev, V., Waegemann, K., Kalinin, S., Seidel, C. A., Neupert, W., Lamb, D. C., and Mokranjac, D. (2010) The conformational dynamics of the mitochondrial Hsp70 chaperone. Mol. Cell 38, 89-100
-
(2010)
Mol. Cell
, vol.38
, pp. 89-100
-
-
Mapa, K.1
Sikor, M.2
Kudryavtsev, V.3
Waegemann, K.4
Kalinin, S.5
Seidel, C.A.6
Neupert, W.7
Lamb, D.C.8
Mokranjac, D.9
-
8
-
-
84872870534
-
Conformational selection in substrate recognition by Hsp70 chaperones
-
Marcinowski, M., Rosam, M., Seitz, C., Elferich, J., Behnke, J., Bello, C., Feige, M. J., Becker, C. F., Antes, I., and Buchner, J. (2013) Conformational selection in substrate recognition by Hsp70 chaperones. J. Mol. Biol. 425, 466-474
-
(2013)
J. Mol. Biol.
, vol.425
, pp. 466-474
-
-
Marcinowski, M.1
Rosam, M.2
Seitz, C.3
Elferich, J.4
Behnke, J.5
Bello, C.6
Feige, M.J.7
Becker, C.F.8
Antes, I.9
Buchner, J.10
-
9
-
-
77954947810
-
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
-
Kampinga, H. H., and Craig, E. A. (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11, 579-592
-
(2010)
Nat. Rev. Mol. Cell Biol.
, vol.11
, pp. 579-592
-
-
Kampinga, H.H.1
Craig, E.A.2
-
10
-
-
0031945665
-
Structure, function and evolution of Dnaj: Conservation and adaptation of chaperone function
-
Cheetham, M. E., and Caplan, A. J. (1998) Structure, function and evolution of Dnaj: conservation and adaptation of chaperone function. Cell Stress Chaperones 3, 28-36
-
(1998)
Cell Stress Chaperones
, vol.3
, pp. 28-36
-
-
Cheetham, M.E.1
Caplan, A.J.2
-
11
-
-
0033972225
-
Bag1 functions in vivo as a negative regulator of Hsp70 chaperone activity
-
Nollen, E. A., Brunsting, J. F., Song, J., Kampinga, H. H., and Morimoto, R. I. (2000) Bag1 functions in vivo as a negative regulator of Hsp70 chaperone activity. Mol. Cell Biol. 20, 1083-1088
-
(2000)
Mol. Cell Biol.
, vol.20
, pp. 1083-1088
-
-
Nollen, E.A.1
Brunsting, J.F.2
Song, J.3
Kampinga, H.H.4
Morimoto, R.I.5
-
12
-
-
0029871766
-
A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding
-
Tsai, J., and Douglas, M. G. (1996) A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. J. Biol. Chem. 271, 9347-9354
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 9347-9354
-
-
Tsai, J.1
Douglas, M.G.2
-
13
-
-
4344590764
-
The J-protein family: Modulating protein assembly, disassembly and translocation
-
Walsh, P., Bursać, D., Law, Y. C., Cyr, D., and Lithgow, T. (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep. 5, 567-571
-
(2004)
EMBO Rep.
, vol.5
, pp. 567-571
-
-
Walsh, P.1
Bursać, D.2
Law, Y.C.3
Cyr, D.4
Lithgow, T.5
-
14
-
-
0034662746
-
The crystal structure of the peptidebinding fragment from the yeast Hsp40 protein Sis1
-
Sha, B., Lee, S., and Cyr, D. M. (2000) The crystal structure of the peptidebinding fragment from the yeast Hsp40 protein Sis1. Structure. 8, 799-807
-
(2000)
Structure
, vol.8
, pp. 799-807
-
-
Sha, B.1
Lee, S.2
Cyr, D.M.3
-
15
-
-
0345299781
-
The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate
-
Li, J., Qian, X., and Sha, B. (2003) The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure 11, 1475-1483
-
(2003)
Structure
, vol.11
, pp. 1475-1483
-
-
Li, J.1
Qian, X.2
Sha, B.3
-
16
-
-
58549098933
-
ERdj3, a luminal ER Dnaj homologue, binds directly to unfolded proteins in the mammalian ER: Identification of critical residues
-
Jin, Y., Zhuang, M., and Hendershot, L. M. (2009) ERdj3, a luminal ER Dnaj homologue, binds directly to unfolded proteins in the mammalian ER: identification of critical residues. Biochemistry 48, 41-49
-
(2009)
Biochemistry
, vol.48
, pp. 41-49
-
-
Jin, Y.1
Zhuang, M.2
Hendershot, L.M.3
-
17
-
-
15844404388
-
Structure-function analysis of the zinc finger region of the Dnaj molecular chaperone
-
Banecki, B., Liberek, K., Wall, D., Wawrzynów, A., Georgopoulos, C., Bertoli, E., Tanfani, F., and Zylicz, M. (1996) Structure-function analysis of the zinc finger region of the Dnaj molecular chaperone. J. Biol. Chem. 271, 14840-14848
-
(1996)
J. Biol. Chem.
, vol.271
, pp. 14840-14848
-
-
Banecki, B.1
Liberek, K.2
Wall, D.3
Wawrzynów, A.4
Georgopoulos, C.5
Bertoli, E.6
Tanfani, F.7
Zylicz, M.8
-
18
-
-
36148941356
-
Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions
-
Marcus, N. Y., Marcus, R. A., Schmidt, B. Z., and Haslam, D. B. (2007) Contribution of the HEDJ/ERdj3 cysteine-rich domain to substrate interactions. Arch. Biochem. Biophys. 468, 147-158
-
(2007)
Arch. Biochem. Biophys.
, vol.468
, pp. 147-158
-
-
Marcus, N.Y.1
Marcus, R.A.2
Schmidt, B.Z.3
Haslam, D.B.4
-
19
-
-
0027308741
-
Eukaryotic homologues of Escherichia coli dnaj: A diverse protein family that functions with hsp70 stress proteins
-
Caplan, A. J., Cyr, D. M., and Douglas, M. G. (1993) Eukaryotic homologues of Escherichia coli dnaj : a diverse protein family that functions with hsp70 stress proteins. Mol. Biol. Cell 4, 555-563
-
(1993)
Mol. Biol. Cell
, vol.4
, pp. 555-563
-
-
Caplan, A.J.1
Cyr, D.M.2
Douglas, M.G.3
-
20
-
-
77952580752
-
Life and death of a BiP substrate
-
Otero, J. H., Lizák, B., and Hendershot, L. M. (2010) Life and death of a BiP substrate. Semin. Cell Dev. Biol. 21, 472-478
-
(2010)
Semin. Cell Dev. Biol.
, vol.21
, pp. 472-478
-
-
Otero, J.H.1
Lizák, B.2
Hendershot, L.M.3
-
21
-
-
55549139747
-
Regulated release of ERdj3 from unfolded proteins by BiP
-
Jin, Y., Awad, W., Petrova, K., and Hendershot, L. M. (2008) Regulated release of ERdj3 from unfolded proteins by BiP. EMBO J. 27, 2873-2882
-
(2008)
EMBO J.
, vol.27
, pp. 2873-2882
-
-
Jin, Y.1
Awad, W.2
Petrova, K.3
Hendershot, L.M.4
-
22
-
-
0034637459
-
HEDJ, an Hsp40 cochaperone localized to the endoplasmic reticulum of human cells
-
Yu, M., Haslam, R. H., and Haslam, D. B. (2000) HEDJ, an Hsp40 cochaperone localized to the endoplasmic reticulum of human cells. J. Biol. Chem. 275, 24984-24992
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 24984-24992
-
-
Yu, M.1
Haslam, R.H.2
Haslam, D.B.3
-
23
-
-
0036911213
-
A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
-
Meunier, L., Usherwood, Y. K., Chung, K. T., and Hendershot, L. M. (2002) A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell 13, 4456-4469
-
(2002)
Mol. Biol. Cell
, vol.13
, pp. 4456-4469
-
-
Meunier, L.1
Usherwood, Y.K.2
Chung, K.T.3
Hendershot, L.M.4
-
24
-
-
0030030946
-
A zinc fingerlike domain of the molecular chaperone Dnaj is involved in binding to denatured protein substrates
-
Szabo, A., Korszun, R., Hartl, F. U., and Flanagan, J. (1996) A zinc fingerlike domain of the molecular chaperone Dnaj is involved in binding to denatured protein substrates. EMBO J. 15, 408 - 417
-
(1996)
EMBO J.
, vol.15
, pp. 408-417
-
-
Szabo, A.1
Korszun, R.2
Hartl, F.U.3
Flanagan, J.4
-
25
-
-
20744437430
-
The C-terminal (331-376) sequence of Escherichia coli Dnaj is essential for dimerization and chaperone activity: A small angle x-ray scattering study in solution
-
Shi, Y. Y., Hong, X. G., and Wang, C. C. (2005) The C-terminal (331-376) sequence of Escherichia coli Dnaj is essential for dimerization and chaperone activity: a small angle x-ray scattering study in solution. J. Biol. Chem. 280, 22761-22768
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 22761-22768
-
-
Shi, Y.Y.1
Hong, X.G.2
Wang, C.C.3
-
26
-
-
84878255102
-
Structural insights into the chaperone activity of the 40-kDa heat shock protein Dnaj: Binding and remodeling of a native substrate
-
Cuéllar, J., Perales-Calvo, J., Muga, A., Valpuesta, J. M., and Moro, F. (2013) Structural insights into the chaperone activity of the 40-kDa heat shock protein Dnaj: binding and remodeling of a native substrate. J. Biol. Chem. 288, 15065-15074
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 15065-15074
-
-
Cuéllar, J.1
Perales-Calvo, J.2
Muga, A.3
Valpuesta, J.M.4
Moro, F.5
-
27
-
-
13444274413
-
The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40
-
Wu, Y., Li, J., Jin, Z., Fu, Z., and Sha, B. (2005) The crystal structure of the C-terminal fragment of yeast Hsp40 Ydj1 reveals novel dimerization motif for Hsp40. J. Mol. Biol. 346, 1005-1011
-
(2005)
J. Mol. Biol.
, vol.346
, pp. 1005-1011
-
-
Wu, Y.1
Li, J.2
Jin, Z.3
Fu, Z.4
Sha, B.5
-
28
-
-
0032539619
-
The variable domain of non-assembled Ig light chains determines both their half-life and binding to BiP
-
Skowronek, M. H., Hendershot, L. M., and Haas, I. G. (1998) The variable domain of non-assembled Ig light chains determines both their half-life and binding to BiP. Proc. Natl. Acad. Sci. U.S.A. 95, 1574-1578
-
(1998)
Proc. Natl. Acad. Sci. U.S.A.
, vol.95
, pp. 1574-1578
-
-
Skowronek, M.H.1
Hendershot, L.M.2
Haas, I.G.3
-
29
-
-
0027528476
-
Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain
-
Gaut, J. R., and Hendershot, L. M. (1993) Mutations within the nucleotide binding site of immunoglobulin-binding protein inhibit ATPase activity and interfere with release of immunoglobulin heavy chain. J. Biol. Chem. 268, 7248 -7255
-
(1993)
J. Biol. Chem.
, vol.268
, pp. 7248-7255
-
-
Gaut, J.R.1
Hendershot, L.M.2
-
30
-
-
11144249887
-
ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates
-
Shen, Y., and Hendershot, L. M. (2005) ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates. Mol. Biol. Cell 16, 40-50
-
(2005)
Mol. Biol. Cell
, vol.16
, pp. 40-50
-
-
Shen, Y.1
Hendershot, L.M.2
-
31
-
-
33645021327
-
RF cloning: A restriction-free method for inserting target genes into plasmids
-
van den Ent F., and Löwe, J. (2006) RF cloning: a restriction-free method for inserting target genes into plasmids. J Biochem. Biophys. Methods 67, 67-74
-
(2006)
J Biochem. Biophys. Methods
, vol.67
, pp. 67-74
-
-
Van Den Ent, F.1
Löwe, J.2
-
32
-
-
84881272939
-
Combining crystallography and EPR: Crystal and solution structures of the multidomain cochaperone DnaJ
-
Barends, T. R., Brosi, R. W., Steinmetz, A., Scherer, A., Hartmann, E., Eschenbach, J., Lorenz, T., Seidel, R., Shoeman, R. L., Zimmermann, S., Bittl, R., Schlichting, I., and Reinstein, J. (2013) Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ. Acta Crystallogr. D. Biol. Crystallogr. 69, 1540-1552
-
(2013)
Acta Crystallogr. D. Biol. Crystallogr.
, vol.69
, pp. 1540-1552
-
-
Barends, T.R.1
Brosi, R.W.2
Steinmetz, A.3
Scherer, A.4
Hartmann, E.5
Eschenbach, J.6
Lorenz, T.7
Seidel, R.8
Shoeman, R.L.9
Zimmermann, S.10
Bittl, R.11
Schlichting, I.12
Reinstein, J.13
-
33
-
-
0028151509
-
The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system: DnaK, DnaJ, and GrpE
-
Szabo, A., Langer, T., Schröder, H., Flanagan, J., Bukau, B., and Hartl, F. U. (1994) The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system: DnaK, DnaJ, and GrpE.Proc. Natl. Acad. Sci. U.S.A. 91, 10345-10349
-
(1994)
Proc. Natl. Acad. Sci. U.S.A.
, vol.91
, pp. 10345-10349
-
-
Szabo, A.1
Langer, T.2
Schröder, H.3
Flanagan, J.4
Bukau, B.5
Hartl, F.U.6
-
34
-
-
0026739395
-
Regulation of Hsp70 function by a eukaryotic DnaJ homolog
-
Cyr, D.M., Lu, X., and Douglas, M. G. (1992) Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J. Biol. Chem. 267, 20927-20931
-
(1992)
J. Biol. Chem.
, vol.267
, pp. 20927-20931
-
-
Cyr, D.M.1
Lu, X.2
Douglas, M.G.3
-
35
-
-
0029101833
-
ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates
-
Wawrzynów, A., Banecki, B., Wall, D., Liberek, K., Georgopoulos, C., and Zylicz, M. (1995) ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates. J. Biol. Chem. 270, 19307-19311
-
(1995)
J. Biol. Chem.
, vol.270
, pp. 19307-19311
-
-
Wawrzynów, A.1
Banecki, B.2
Wall, D.3
Liberek, K.4
Georgopoulos, C.5
Zylicz, M.6
-
36
-
-
70450273171
-
The mammalian Hsp40 ERdj3 requires its Hsp70 interaction and substratebinding properties to complement various yeast Hsp40-dependent functions
-
Vembar, S. S., Jin, Y., Brodsky, J. L., and Hendershot, L. M. (2009) The mammalian Hsp40 ERdj3 requires its Hsp70 interaction and substratebinding properties to complement various yeast Hsp40-dependent functions. J. Biol. Chem. 284, 32462-32471
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 32462-32471
-
-
Vembar, S.S.1
Jin, Y.2
Brodsky, J.L.3
Hendershot, L.M.4
-
37
-
-
34249853249
-
Network of general and specialty J protein chaperones of the yeast cytosol
-
Sahi, C., and Craig, E. A. (2007) Network of general and specialty J protein chaperones of the yeast cytosol. Proc. Natl. Acad. Sci. U.S.A. 104, 7163-7168
-
(2007)
Proc. Natl. Acad. Sci. U.S.A.
, vol.104
, pp. 7163-7168
-
-
Sahi, C.1
Craig, E.A.2
-
38
-
-
34548232285
-
The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: Regulating chaperone power in the parasite and the host
-
Botha, M., Pesce, E. R., and Blatch, G. L. (2007) The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host. Int. J. Biochem. Cell Biol. 39, 1781-1803
-
(2007)
Int. J. Biochem. Cell Biol.
, vol.39
, pp. 1781-1803
-
-
Botha, M.1
Pesce, E.R.2
Blatch, G.L.3
-
39
-
-
80055108114
-
Functional analysis of the exported type IV HSP40 protein PfGECO in Plasmodium falciparum gametocytes
-
Moraban, B. J., Strobel, C., Hasan, U., Czesny, B., Mantel, P. Y., Marti, M., Eksi, S., and Williamson, K. C. (2011) Functional analysis of the exported type IV HSP40 protein PfGECO in Plasmodium falciparum gametocytes. Eukaryot. Cell 10, 1492-1503
-
(2011)
Eukaryot. Cell
, vol.10
, pp. 1492-1503
-
-
Moraban, B.J.1
Strobel, C.2
Hasan, U.3
Czesny, B.4
Mantel, P.Y.5
Marti, M.6
Eksi, S.7
Williamson, K.C.8
-
40
-
-
0033545978
-
Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones
-
Laufen, T., Mayer, M. P., Beisel, C., Klostermeier, D., Mogk, A., Reinstein, J., and Bukau, B. (1999) Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones. Proc. Natl. Acad. Sci. U.S.A. 96, 5452-5457
-
(1999)
Proc. Natl. Acad. Sci. U.S.A.
, vol.96
, pp. 5452-5457
-
-
Laufen, T.1
Mayer, M.P.2
Beisel, C.3
Klostermeier, D.4
Mogk, A.5
Reinstein, J.6
Bukau, B.7
-
41
-
-
0032417526
-
Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ
-
Suh, W. C., Burkholder, W. F., Lu, C. Z., Zhao, X., Gottesman, M. E., and Gross, C. A. (1998) Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. Proc. Natl. Acad. Sci. U.S.A. 95, 15223-15228
-
(1998)
Proc. Natl. Acad. Sci. U.S.A.
, vol.95
, pp. 15223-15228
-
-
Suh, W.C.1
Burkholder, W.F.2
Lu, C.Z.3
Zhao, X.4
Gottesman, M.E.5
Gross, C.A.6
-
42
-
-
55549141494
-
Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3
-
Petrova, K., Oyadomari, S., Hendershot, L. M., and Ron, D. (2008) Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3. EMBO J. 27, 2862-2872
-
(2008)
EMBO J.
, vol.27
, pp. 2862-2872
-
-
Petrova, K.1
Oyadomari, S.2
Hendershot, L.M.3
Ron, D.4
-
43
-
-
0029051966
-
Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1
-
Freeman, B. C., Myers, M. P., Schumacher, R., and Morimoto, R. I. (1995) Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. EMBO J. 14, 2281-2292
-
(1995)
EMBO J.
, vol.14
, pp. 2281-2292
-
-
Freeman, B.C.1
Myers, M.P.2
Schumacher, R.3
Morimoto, R.I.4
-
44
-
-
0036177548
-
Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: Yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1
-
Qian, X., Hou, W., Zhengang, L., and Sha, B. (2002) Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1. Biochem. J. 361, 27-34
-
(2002)
Biochem. J.
, vol.361
, pp. 27-34
-
-
Qian, X.1
Hou, W.2
Zhengang, L.3
Sha, B.4
-
45
-
-
33748743974
-
Crystal structure of yeast Sisl peptide-binding fragment and Hsp70 Ssal C-terminal complex
-
Li, J., Wu, Y., Qian, X., and Sha, B. (2006) Crystal structure of yeast Sisl peptide-binding fragment and Hsp70 Ssal C-terminal complex. Biochem. J 398, 353-360
-
(2006)
Biochem. J
, vol.398
, pp. 353-360
-
-
Li, J.1
Wu, Y.2
Qian, X.3
Sha, B.4
-
46
-
-
0033579518
-
Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells
-
Michels, A. A., Kanon, B., Bensaude, O., and Kampinga, H. H. (1999) Heat shock protein (Hsp) 40 mutants inhibit Hsp70 in mammalian cells. J. Biol. Chem. 274, 36757-36763
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 36757-36763
-
-
Michels, A.A.1
Kanon, B.2
Bensaude, O.3
Kampinga, H.H.4
-
47
-
-
79551632223
-
Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions
-
Marcinowski, M., Höller, M., Feige, M. J., Baerend, D., Lamb, D. C., and Buchner, J. (2011) Substrate discrimination of the chaperone BiP by autonomous and cochaperone-regulated conformational transitions. Nat. Struct. Mol. Biol. 18, 150-158
-
(2011)
Nat. Struct. Mol. Biol.
, vol.18
, pp. 150-158
-
-
Marcinowski, M.1
Höller, M.2
Feige, M.J.3
Baerend, D.4
Lamb, D.C.5
Buchner, J.6
-
48
-
-
48249155627
-
ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C
-
Dong, M., Bridges, J. P., Apsley, K., Xu, Y., and Weaver, T. E. (2008) ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein C. Mol. Biol. Cell 19, 2620 -2630
-
(2008)
Mol. Biol. Cell
, vol.19
, pp. 2620-2630
-
-
Dong, M.1
Bridges, J.P.2
Apsley, K.3
Xu, Y.4
Weaver, T.E.5
-
49
-
-
48249117110
-
ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER
-
Ushioda, R., Hoseki, J., Araki, K., Jansen, G., Thomas, D. Y., and Nagata, K. (2008) ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER. Science 321, 569 -572
-
(2008)
Science
, vol.321
, pp. 569-572
-
-
Ushioda, R.1
Hoseki, J.2
Araki, K.3
Jansen, G.4
Thomas, D.Y.5
Nagata, K.6
-
50
-
-
0034896499
-
Unassembled Ig heavy chains do not cycle from BiP in vivo, but require light chains to trigger their release
-
Vanhove, M., Usherwood, Y.-K., and Hendershot, L. M. (2001) Unassembled Ig heavy chains do not cycle from BiP in vivo, but require light chains to trigger their release. Immunity 15, 105-114
-
(2001)
Immunity
, vol.15
, pp. 105-114
-
-
Vanhove, M.1
Usherwood, Y.-K.2
Hendershot, L.M.3
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