-
1
-
-
0030868605
-
Iron-sulfur clusters: Nature's modular, multipurpose structures
-
Beinert, H., Holm, R. H., and Münck, E. (1997) Iron-sulfur clusters: Nature's modular, multipurpose structures Science 277, 653-659
-
(1997)
Science
, vol.277
, pp. 653-659
-
-
Beinert, H.1
Holm, R.H.2
Münck, E.3
-
2
-
-
68949128587
-
Function and biogenesis of iron-sulphur proteins
-
Lill, R. (2009) Function and biogenesis of iron-sulphur proteins Nature 460, 831-838
-
(2009)
Nature
, vol.460
, pp. 831-838
-
-
Lill, R.1
-
3
-
-
47249094614
-
Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
-
Lill, R. and Mühlenhoff, U. (2008) Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases Annu. Rev. Biochem. 77, 669-700
-
(2008)
Annu. Rev. Biochem.
, vol.77
, pp. 669-700
-
-
Lill, R.1
Mühlenhoff, U.2
-
4
-
-
20744446399
-
Structure, function, and formation of biological iron-sulfur clusters
-
Johnson, D. C., Dean, D. R., Smith, A. D., and Johnson, M. K. (2005) Structure, function, and formation of biological iron-sulfur clusters Annu. Rev. Biochem. 74, 247-281
-
(2005)
Annu. Rev. Biochem.
, vol.74
, pp. 247-281
-
-
Johnson, D.C.1
Dean, D.R.2
Smith, A.D.3
Johnson, M.K.4
-
5
-
-
33645065589
-
Iron-sulphur clusters and the problem with oxygen
-
Imlay, J. A. (2006) Iron-sulphur clusters and the problem with oxygen Mol. Microbiol. 59, 1073-1082
-
(2006)
Mol. Microbiol.
, vol.59
, pp. 1073-1082
-
-
Imlay, J.A.1
-
6
-
-
84864296714
-
The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism
-
Lill, R., Hoffmann, B., Molik, S., Pierik, A. J., Rietzschel, N., Stehling, O., Uzarska, M. A., Webert, H., Wilbrecht, C., and Mühlenhoff, U. (2013) The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism Biochim. Biophys. Acta 1823, 1491-1508
-
(2013)
Biochim. Biophys. Acta
, vol.1823
, pp. 1491-1508
-
-
Lill, R.1
Hoffmann, B.2
Molik, S.3
Pierik, A.J.4
Rietzschel, N.5
Stehling, O.6
Uzarska, M.A.7
Webert, H.8
Wilbrecht, C.9
Mühlenhoff, U.10
-
7
-
-
84858015433
-
Biogenesis of iron-sulfur clusters in mammalian cells: New insights and relevance to human disease
-
Rouault, T. A. (2012) Biogenesis of iron-sulfur clusters in mammalian cells: New insights and relevance to human disease Dis. Models & Mech. 5, 155-164
-
(2012)
Dis. Models & Mech.
, vol.5
, pp. 155-164
-
-
Rouault, T.A.1
-
8
-
-
77952472876
-
Iron-sulfur proteins in health and disease
-
Sheftel, A., Stehling, O., and Lill, R. (2010) Iron-sulfur proteins in health and disease Trends Endocrinol. Metab. 21, 302-314
-
(2010)
Trends Endocrinol. Metab.
, vol.21
, pp. 302-314
-
-
Sheftel, A.1
Stehling, O.2
Lill, R.3
-
9
-
-
84897949661
-
Mitochondrial iron-sulfur cluster dysfunction in neurodegenerative disease
-
Isaya, G. (2014) Mitochondrial iron-sulfur cluster dysfunction in neurodegenerative disease Front. Pharmacol. 5, 29
-
(2014)
Front. Pharmacol.
, vol.5
, pp. 29
-
-
Isaya, G.1
-
10
-
-
84876034471
-
Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery
-
Markley, J. L., Kim, J. H., Dai, Z., Bothe, J. R., Cai, K., Frederick, R. O., and Tonelli, M. (2013) Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery FEBS Lett. 587, 1172-1179
-
(2013)
FEBS Lett.
, vol.587
, pp. 1172-1179
-
-
Markley, J.L.1
Kim, J.H.2
Dai, Z.3
Bothe, J.R.4
Cai, K.5
Frederick, R.O.6
Tonelli, M.7
-
11
-
-
0032557666
-
Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
-
Zheng, L., Cash, V. L., Flint, D. H., and Dean, D. R. (1998) Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii J. Biol. Chem. 273, 13264-13272
-
(1998)
J. Biol. Chem.
, vol.273
, pp. 13264-13272
-
-
Zheng, L.1
Cash, V.L.2
Flint, D.H.3
Dean, D.R.4
-
12
-
-
57049159293
-
Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones
-
Bonomi, F., Iametti, S., Morleo, A., Ta, D., and Vickery, L. E. (2008) Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones Biochemistry 47, 12795-12801
-
(2008)
Biochemistry
, vol.47
, pp. 12795-12801
-
-
Bonomi, F.1
Iametti, S.2
Morleo, A.3
Ta, D.4
Vickery, L.E.5
-
13
-
-
0035910560
-
The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli
-
Silberg, J. J., Hoff, K. G., Tapley, T. L., and Vickery, L. E. (2001) The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli J. Biol. Chem. 276, 1696-1700
-
(2001)
J. Biol. Chem.
, vol.276
, pp. 1696-1700
-
-
Silberg, J.J.1
Hoff, K.G.2
Tapley, T.L.3
Vickery, L.E.4
-
14
-
-
0030903131
-
Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli
-
Vickery, L. E., Silberg, J. J., and Ta, D. T. (1997) Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli Protein Sci. 6, 1047-1056
-
(1997)
Protein Sci.
, vol.6
, pp. 1047-1056
-
-
Vickery, L.E.1
Silberg, J.J.2
Ta, D.T.3
-
15
-
-
3142653172
-
Preferential substrate binding orientation by the molecular chaperone HscA
-
Tapley, T. L. and Vickery, L. E. (2004) Preferential substrate binding orientation by the molecular chaperone HscA J. Biol. Chem. 279, 28435-28442
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 28435-28442
-
-
Tapley, T.L.1
Vickery, L.E.2
-
16
-
-
0037178878
-
Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU
-
Hoff, K. G., Ta, D. T., Tapley, T. L., Silberg, J. J., and Vickery, L. E. (2002) Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU J. Biol. Chem. 277, 27353-27359
-
(2002)
J. Biol. Chem.
, vol.277
, pp. 27353-27359
-
-
Hoff, K.G.1
Ta, D.T.2
Tapley, T.L.3
Silberg, J.J.4
Vickery, L.E.5
-
17
-
-
0141844533
-
Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system
-
Hoff, K. G., Cupp-Vickery, J. R., and Vickery, L. E. (2003) Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system J. Biol. Chem. 278, 37582-37589
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 37582-37589
-
-
Hoff, K.G.1
Cupp-Vickery, J.R.2
Vickery, L.E.3
-
18
-
-
4444346912
-
Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
-
Cupp-Vickery, J. R., Peterson, J. C., Ta, D. T., and Vickery, L. E. (2004) Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC J. Mol. Biol. 342, 1265-1278
-
(2004)
J. Mol. Biol.
, vol.342
, pp. 1265-1278
-
-
Cupp-Vickery, J.R.1
Peterson, J.C.2
Ta, D.T.3
Vickery, L.E.4
-
19
-
-
0034678084
-
Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli
-
Silberg, J. J. and Vickery, L. E. (2000) Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli J. Biol. Chem. 275, 7779-7786
-
(2000)
J. Biol. Chem.
, vol.275
, pp. 7779-7786
-
-
Silberg, J.J.1
Vickery, L.E.2
-
20
-
-
34247124148
-
Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
-
Vickery, L. E. and Cupp-Vickery, J. R. (2007) Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation Crit. Rev. Biochem. Mol. Biol. 42, 95-111
-
(2007)
Crit. Rev. Biochem. Mol. Biol.
, vol.42
, pp. 95-111
-
-
Vickery, L.E.1
Cupp-Vickery, J.R.2
-
21
-
-
0032414399
-
The Hsc66-Hsc20 chaperone system in Escherichia coli: Chaperone activity and interactions with the DnaK-DnaJ-grpE system
-
Silberg, J. J., Hoff, K. G., and Vickery, L. E. (1998) The Hsc66-Hsc20 chaperone system in Escherichia coli: Chaperone activity and interactions with the DnaK-DnaJ-grpE system J. Bacteriol. 180, 6617-6624
-
(1998)
J. Bacteriol.
, vol.180
, pp. 6617-6624
-
-
Silberg, J.J.1
Hoff, K.G.2
Vickery, L.E.3
-
22
-
-
0034608935
-
Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli
-
Hoff, K. G., Silberg, J. J., and Vickery, L. E. (2000) Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 97, 7790-7795
-
(2000)
Proc. Natl. Acad. Sci. U.S.A.
, vol.97
, pp. 7790-7795
-
-
Hoff, K.G.1
Silberg, J.J.2
Vickery, L.E.3
-
23
-
-
84863894674
-
Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli
-
Kim, J. H., Tonelli, M., Kim, T., and Markley, J. L. (2012) Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli Biochemistry 51, 5557-5563
-
(2012)
Biochemistry
, vol.51
, pp. 5557-5563
-
-
Kim, J.H.1
Tonelli, M.2
Kim, T.3
Markley, J.L.4
-
24
-
-
67650033430
-
Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB
-
Kim, J. H., Füzéry, A. K., Tonelli, M., Ta, D. T., Westler, W. M., Vickery, L. E., and Markley, J. L. (2009) Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB Biochemistry 48, 6062-6071
-
(2009)
Biochemistry
, vol.48
, pp. 6062-6071
-
-
Kim, J.H.1
Füzéry, A.K.2
Tonelli, M.3
Ta, D.T.4
Westler, W.M.5
Vickery, L.E.6
Markley, J.L.7
-
25
-
-
84870538240
-
Metamorphic protein IscU changes conformation by cis-trans isomerizations of two peptidyl-prolyl peptide bonds
-
Dai, Z., Tonelli, M., and Markley, J. L. (2012) Metamorphic protein IscU changes conformation by cis-trans isomerizations of two peptidyl-prolyl peptide bonds Biochemistry 51, 9595-9602
-
(2012)
Biochemistry
, vol.51
, pp. 9595-9602
-
-
Dai, Z.1
Tonelli, M.2
Markley, J.L.3
-
26
-
-
84866139470
-
Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU)
-
Kim, J. H., Tonelli, M., Frederick, R. O., Chow, D. C., and Markley, J. L. (2012) Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU) J. Biol. Chem. 287, 31406-31413
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 31406-31413
-
-
Kim, J.H.1
Tonelli, M.2
Frederick, R.O.3
Chow, D.C.4
Markley, J.L.5
-
27
-
-
84885117582
-
Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)
-
Cai, K., Frederick, R. O., Kim, J. H., Reinen, N. M., Tonelli, M., and Markley, J. L. (2013) Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU) J. Biol. Chem. 288, 28755-28770
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 28755-28770
-
-
Cai, K.1
Frederick, R.O.2
Kim, J.H.3
Reinen, N.M.4
Tonelli, M.5
Markley, J.L.6
-
28
-
-
0034911990
-
Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins
-
Tokumoto, U. and Takahashi, Y. (2001) Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins J. Biochem. 130, 63-71
-
(2001)
J. Biochem.
, vol.130
, pp. 63-71
-
-
Tokumoto, U.1
Takahashi, Y.2
-
29
-
-
33750445986
-
Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii
-
Johnson, D. C., Unciuleac, M. C., and Dean, D. R. (2006) Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii J. Bacteriol. 188, 7551-7561
-
(2006)
J. Bacteriol.
, vol.188
, pp. 7551-7561
-
-
Johnson, D.C.1
Unciuleac, M.C.2
Dean, D.R.3
-
30
-
-
34047268015
-
Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker
-
Swain, J. F., Dinler, G., Sivendran, R., Montgomery, D. L., Stotz, M., and Gierasch, L. M. (2007) Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker Mol. Cell 26, 27-39
-
(2007)
Mol. Cell
, vol.26
, pp. 27-39
-
-
Swain, J.F.1
Dinler, G.2
Sivendran, R.3
Montgomery, D.L.4
Stotz, M.5
Gierasch, L.M.6
-
31
-
-
33846020582
-
Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker
-
Vogel, M., Mayer, M. P., and Bukau, B. (2006) Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker J. Biol. Chem. 281, 38705-38711
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 38705-38711
-
-
Vogel, M.1
Mayer, M.P.2
Bukau, B.3
-
32
-
-
35649024724
-
Structural basis of J cochaperone binding and regulation of Hsp70
-
Jiang, J., Maes, E. G., Taylor, A. B., Wang, L., Hinck, A. P., Lafer, E. M., and Sousa, R. (2007) Structural basis of J cochaperone binding and regulation of Hsp70 Mol. Cell 28, 422-433
-
(2007)
Mol. Cell
, vol.28
, pp. 422-433
-
-
Jiang, J.1
Maes, E.G.2
Taylor, A.B.3
Wang, L.4
Hinck, A.P.5
Lafer, E.M.6
Sousa, R.7
-
33
-
-
79955565642
-
Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones
-
Zhuravleva, A. and Gierasch, L. M. (2011) Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones Proc. Natl. Acad. Sci. U.S.A. 108, 6987-6992
-
(2011)
Proc. Natl. Acad. Sci. U.S.A.
, vol.108
, pp. 6987-6992
-
-
Zhuravleva, A.1
Gierasch, L.M.2
-
34
-
-
84884589727
-
Hsp70 chaperone dynamics and molecular mechanism
-
Mayer, M. P. (2013) Hsp70 chaperone dynamics and molecular mechanism Trends Biochem. Sci. 38, 507-514
-
(2013)
Trends Biochem. Sci.
, vol.38
, pp. 507-514
-
-
Mayer, M.P.1
-
35
-
-
84880167772
-
Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
-
Qi, R., Sarbeng, E. B., Liu, Q., Le, K. Q., Xu, X., Xu, H., Yang, J., Wong, J. L., Vorvis, C., Hendrickson, W. A., Zhou, L., and Liu, Q. (2013) Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP Nat. Struct. Mol. Biol. 20, 900-907
-
(2013)
Nat. Struct. Mol. Biol.
, vol.20
, pp. 900-907
-
-
Qi, R.1
Sarbeng, E.B.2
Liu, Q.3
Le, K.Q.4
Xu, X.5
Xu, H.6
Yang, J.7
Wong, J.L.8
Vorvis, C.9
Hendrickson, W.A.10
Zhou, L.11
Liu, Q.12
-
36
-
-
64649094781
-
Solution conformation of wild-type E. Coli Hsp70 (DnaK) chaperone complexed with ADP and substrate
-
Bertelsen, E. B., Chang, L., Gestwicki, J. E., and Zuiderweg, E. R. (2009) Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate Proc. Natl. Acad. Sci. U.S.A. 106, 8471-8476
-
(2009)
Proc. Natl. Acad. Sci. U.S.A.
, vol.106
, pp. 8471-8476
-
-
Bertelsen, E.B.1
Chang, L.2
Gestwicki, J.E.3
Zuiderweg, E.R.4
-
37
-
-
0025100372
-
Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
-
Flaherty, K. M., DeLuca-Flaherty, C., and McKay, D. B. (1990) Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein Nature 346, 623-628
-
(1990)
Nature
, vol.346
, pp. 623-628
-
-
Flaherty, K.M.1
Deluca-Flaherty, C.2
McKay, D.B.3
-
38
-
-
0028240468
-
Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment
-
Flaherty, K. M., Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment J. Biol. Chem. 269, 12899-12907
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 12899-12907
-
-
Flaherty, K.M.1
Wilbanks, S.M.2
Deluca-Flaherty, C.3
McKay, D.B.4
-
39
-
-
84874473589
-
Allostery in the Hsp70 chaperone proteins
-
Zuiderweg, E. R., Bertelsen, E. B., Rousaki, A., Mayer, M. P., Gestwicki, J. E., and Ahmad, A. (2013) Allostery in the Hsp70 chaperone proteins Top. Curr. Chem. 328, 99-153
-
(2013)
Top. Curr. Chem.
, vol.328
, pp. 99-153
-
-
Zuiderweg, E.R.1
Bertelsen, E.B.2
Rousaki, A.3
Mayer, M.P.4
Gestwicki, J.E.5
Ahmad, A.6
-
40
-
-
4043052955
-
NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: Implications for the allosteric mechanism
-
Revington, M., Holder, T. M., and Zuiderweg, E. R. (2004) NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: Implications for the allosteric mechanism J. Biol. Chem. 279, 33958-33967
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 33958-33967
-
-
Revington, M.1
Holder, T.M.2
Zuiderweg, E.R.3
-
41
-
-
18144374138
-
NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone
-
Revington, M., Zhang, Y., Yip, G. N., Kurochkin, A. V., and Zuiderweg, E. R. (2005) NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone J. Mol. Biol. 349, 163-183
-
(2005)
J. Mol. Biol.
, vol.349
, pp. 163-183
-
-
Revington, M.1
Zhang, Y.2
Yip, G.N.3
Kurochkin, A.V.4
Zuiderweg, E.R.5
-
42
-
-
64649089001
-
Allostery in Hsp70 chaperones is transduced by subdomain rotations
-
Bhattacharya, A., Kurochkin, A. V., Yip, G. N., Zhang, Y., Bertelsen, E. B., and Zuiderweg, E. R. (2009) Allostery in Hsp70 chaperones is transduced by subdomain rotations J. Mol. Biol. 388, 475-490
-
(2009)
J. Mol. Biol.
, vol.388
, pp. 475-490
-
-
Bhattacharya, A.1
Kurochkin, A.V.2
Yip, G.N.3
Zhang, Y.4
Bertelsen, E.B.5
Zuiderweg, E.R.6
-
43
-
-
0028287525
-
Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants
-
Wilbanks, S. M., DeLuca-Flaherty, C., and McKay, D. B. (1994) Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants J. Biol. Chem. 269, 12893-12898
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 12893-12898
-
-
Wilbanks, S.M.1
Deluca-Flaherty, C.2
McKay, D.B.3
-
44
-
-
0032568541
-
Role of the J-domain in the cooperation of Hsp40 with Hsp70
-
Greene, M. K., Maskos, K., and Landry, S. J. (1998) Role of the J-domain in the cooperation of Hsp40 with Hsp70 Proc. Natl. Acad. Sci. U.S.A. 95, 6108-6113
-
(1998)
Proc. Natl. Acad. Sci. U.S.A.
, vol.95
, pp. 6108-6113
-
-
Greene, M.K.1
Maskos, K.2
Landry, S.J.3
-
45
-
-
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., and Vickery, L. E. (2004) 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)
J. Biol. Chem.
, vol.279
, pp. 53924-53931
-
-
Silberg, J.J.1
Tapley, T.L.2
Hoff, K.G.3
Vickery, L.E.4
-
46
-
-
51549120794
-
Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU
-
Füzéry, A. K., Tonelli, M., Ta, D. T., Cornilescu, G., Vickery, L. E., and Markley, J. L. (2008) Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU Biochemistry 47, 9394-9404
-
(2008)
Biochemistry
, vol.47
, pp. 9394-9404
-
-
Füzéry, A.K.1
Tonelli, M.2
Ta, D.T.3
Cornilescu, G.4
Vickery, L.E.5
Markley, J.L.6
-
47
-
-
0032570283
-
Kinetics of the reactions of the Escherichia coli molecular chaperone DnaK with ATP: Evidence that a three-step reaction precedes ATP hydrolysis
-
Slepenkov, S. V. and Witt, S. N. (1998) Kinetics of the reactions of the Escherichia coli molecular chaperone DnaK with ATP: Evidence that a three-step reaction precedes ATP hydrolysis Biochemistry 37, 1015-1024
-
(1998)
Biochemistry
, vol.37
, pp. 1015-1024
-
-
Slepenkov, S.V.1
Witt, S.N.2
-
48
-
-
0030589149
-
The second step of ATP binding to DnaK induces peptide release
-
Theyssen, H., Schuster, H. P., Packschies, L., Bukau, B., and Reinstein, J. (1996) The second step of ATP binding to DnaK induces peptide release J. Mol. Biol. 263, 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
-
49
-
-
37249005205
-
The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
-
Niesen, F. H., Berglund, H., and Vedadi, M. (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability Nat. Protoc. 2, 2212-2221
-
(2007)
Nat. Protoc.
, vol.2
, pp. 2212-2221
-
-
Niesen, F.H.1
Berglund, H.2
Vedadi, M.3
-
50
-
-
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
-
51
-
-
84886412961
-
Chaperone machines for protein folding, unfolding and disaggregation
-
Saibil, H. (2013) Chaperone machines for protein folding, unfolding and disaggregation Nat. Rev. Mol. Cell Biol. 14, 630-642
-
(2013)
Nat. Rev. Mol. Cell Biol.
, vol.14
, pp. 630-642
-
-
Saibil, H.1
-
52
-
-
78649357985
-
Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms
-
Buchberger, A., Bukau, B., and Sommer, T. (2010) Protein quality control in the cytosol and the endoplasmic reticulum: Brothers in arms Mol. Cell 40, 238-252
-
(2010)
Mol. Cell
, vol.40
, pp. 238-252
-
-
Buchberger, A.1
Bukau, B.2
Sommer, T.3
-
53
-
-
33646127577
-
Molecular chaperones and protein quality control
-
Bukau, B., Weissman, J., and Horwich, A. (2006) Molecular chaperones and protein quality control Cell 125, 443-451
-
(2006)
Cell
, vol.125
, pp. 443-451
-
-
Bukau, B.1
Weissman, J.2
Horwich, A.3
-
54
-
-
0031794743
-
Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes
-
Gupta, R. S. (1998) Protein phylogenies and signature sequences: A reappraisal of evolutionary relationships among archaebacteria, eubacteria, and eukaryotes Microbiol. Mol. Biol. Rev. 62, 1435-1491
-
(1998)
Microbiol. Mol. Biol. Rev.
, vol.62
, pp. 1435-1491
-
-
Gupta, R.S.1
-
55
-
-
80051669663
-
The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles
-
Kumar, D. P., Vorvis, C., Sarbeng, E. B., Cabra Ledesma, V. C., Willis, J. E., and Liu, Q. (2011) The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles J. Mol. Biol. 411, 1099-1113
-
(2011)
J. Mol. Biol.
, vol.411
, pp. 1099-1113
-
-
Kumar, D.P.1
Vorvis, C.2
Sarbeng, E.B.3
Cabra Ledesma, V.C.4
Willis, J.E.5
Liu, Q.6
-
56
-
-
0035907104
-
Mutations in the interdomain linker region of DnaK abolish the chaperone action of the DnaK/DnaJ/GrpE system
-
Han, W. and Christen, P. (2001) Mutations in the interdomain linker region of DnaK abolish the chaperone action of the DnaK/DnaJ/GrpE system FEBS Lett. 497, 55-58
-
(2001)
FEBS Lett.
, vol.497
, pp. 55-58
-
-
Han, W.1
Christen, P.2
-
57
-
-
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
-
58
-
-
34848869936
-
Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1
-
Liu, Q. and Hendrickson, W. A. (2007) Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1 Cell 131, 106-120
-
(2007)
Cell
, vol.131
, pp. 106-120
-
-
Liu, Q.1
Hendrickson, W.A.2
-
59
-
-
84870916379
-
An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones
-
Zhuravleva, A., Clerico, E. M., and Gierasch, L. M. (2012) An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones Cell 151, 1296-1307
-
(2012)
Cell
, vol.151
, pp. 1296-1307
-
-
Zhuravleva, A.1
Clerico, E.M.2
Gierasch, L.M.3
-
60
-
-
84902326560
-
Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption
-
De Los Rios, P. and Barducci, A. (2014) Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption eLife 3, e02218
-
(2014)
ELife
, vol.3
, pp. 02218
-
-
De Los Rios, P.1
Barducci, A.2
-
61
-
-
0030936995
-
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
-
Harrison, C. J., Hayer-Hartl, M., Di Liberto, M., Hartl, F., and Kuriyan, J. (1997) Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK Science 276, 431-435
-
(1997)
Science
, vol.276
, pp. 431-435
-
-
Harrison, C.J.1
Hayer-Hartl, M.2
Di Liberto, M.3
Hartl, F.4
Kuriyan, J.5
-
62
-
-
31544442176
-
Allosteric regulation of Hsp70 chaperones by a proline switch
-
Vogel, M., Bukau, B., and Mayer, M. P. (2006) Allosteric regulation of Hsp70 chaperones by a proline switch Mol. Cell 21, 359-367
-
(2006)
Mol. Cell
, vol.21
, pp. 359-367
-
-
Vogel, M.1
Bukau, B.2
Mayer, M.P.3
-
63
-
-
84906337399
-
Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe-S cluster biogenesis
-
Kim, J. H., Alderson, T. R., Frederick, R. O., and Markley, J. L. (2014) Nucleotide-dependent interactions within a specialized Hsp70/Hsp40 complex involved in Fe-S cluster biogenesis J. Am. Chem. Soc. 136, 11586-11589
-
(2014)
J. Am. Chem. Soc.
, vol.136
, pp. 11586-11589
-
-
Kim, J.H.1
Alderson, T.R.2
Frederick, R.O.3
Markley, J.L.4
-
64
-
-
27944436648
-
Structural basis of interdomain communication in the Hsc70 chaperone
-
Jiang, J., Prasad, K., Lafer, E. M., and Sousa, R. (2005) Structural basis of interdomain communication in the Hsc70 chaperone Mol. Cell 20, 513-524
-
(2005)
Mol. Cell
, vol.20
, pp. 513-524
-
-
Jiang, J.1
Prasad, K.2
Lafer, E.M.3
Sousa, R.4
-
65
-
-
0029400480
-
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
-
Delagio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
-
(1995)
J. Biomol. NMR
, vol.6
, pp. 277-293
-
-
Delagio, F.1
Grzesiek, S.2
Vuister, G.W.3
Zhu, G.4
Pfeifer, J.5
Bax, A.6
-
66
-
-
84871444338
-
-
University of California, San Francisco
-
Goddard, T. D. and Kneller, D. G. (2008) SPARKY 3, University of California, San Francisco.
-
(2008)
SPARKY 3
-
-
Goddard, T.D.1
Kneller, D.G.2
|