-
1
-
-
0344443774
-
BAG-1 - A nucleotide exchange factor of Hsc70 with multiple cellular functions
-
DOI 10.1379/1466-1268(2003)008<0225:BNEFOH>2.0.CO;2
-
Alberti S, Esser C, Hohfeld J (2003) BAG-1-a nucleotide exchange factor of Hsc70 with multiple cellular functions. Cell Stress Chaperones 8: 225-231 (Pubitemid 37484716)
-
(2003)
Cell Stress and Chaperones
, vol.8
, Issue.3
, pp. 225-231
-
-
Alberti, S.1
Esser, C.2
Hohfeld, J.3
-
2
-
-
0027419771
-
The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs
-
Ali JA, Jackson AP, Howells AJ, Maxwell A (1993) The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugs. Biochemistry 32: 2717-2724 (Pubitemid 23090662)
-
(1993)
Biochemistry
, vol.32
, Issue.10
, pp. 2717-2724
-
-
Ali, J.A.1
Jackson, A.P.2
Howells, A.J.3
Maxwell, A.4
-
3
-
-
55949092734
-
Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity
-
Andreasson C, Fiaux J, Rampelt H, Druffel-Augustin S, Bukau B (2008a) Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proc Natl Acad Sci USA 105: 16519-16524
-
(2008)
Proc Natl Acad Sci USA
, vol.105
, pp. 16519-16524
-
-
Andreasson, C.1
Fiaux, J.2
Rampelt, H.3
Druffel-Augustin, S.4
Bukau, B.5
-
4
-
-
44049083594
-
Hsp110 is a nucleotide-activated exchange factor for Hsp70
-
Andreasson C, Fiaux J, Rampelt H, Mayer MP, Bukau B (2008b) Hsp110 is a nucleotide-activated exchange factor for Hsp70. J Biol Chem 283: 8877-8884
-
(2008)
J Biol Chem
, vol.283
, pp. 8877-8884
-
-
Andreasson, C.1
Fiaux, J.2
Rampelt, H.3
Mayer, M.P.4
Bukau, B.5
-
5
-
-
77951229568
-
The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110
-
Andreasson C, Rampelt H, Fiaux J, Druffel-Augustin S, Bukau B (2010) The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110. J Biol Chem 285: 12445-12453
-
(2010)
J Biol Chem
, vol.285
, pp. 12445-12453
-
-
Andreasson, C.1
Rampelt, H.2
Fiaux, J.3
Druffel-Augustin, S.4
Bukau, B.5
-
7
-
-
34548495803
-
Multiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import
-
DOI 10.1091/mbc.E07-01-0088
-
Bhangoo MK, Tzankov S, Fan AC, Dejgaard K, Thomas DY, Young JC (2007) Multiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import. Mol Biol Cell 18: 3414-3428 (Pubitemid 47378681)
-
(2007)
Molecular Biology of the Cell
, vol.18
, Issue.9
, pp. 3414-3428
-
-
Bhangoo, M.K.1
Tzankov, S.2
Fan, A.C.Y.3
Dejgaard, K.4
Thomas, D.Y.5
Young, J.C.6
-
8
-
-
70350519391
-
A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis
-
Bieschke J, Cohen E, Murray A, Dillin A, Kelly JW (2009) A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis. Protein Sci 18: 2231-2241
-
(2009)
Protein Sci
, vol.18
, pp. 2231-2241
-
-
Bieschke, J.1
Cohen, E.2
Murray, A.3
Dillin, A.4
Kelly, J.W.5
-
9
-
-
0032402812
-
BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release
-
Bimston D, Song J, Winchester D, Takayama S, Reed JC, Morimoto RI (1998) BAG-1, a negative regulator of Hsp70 chaperone activity, uncouples nucleotide hydrolysis from substrate release. EMBO J 17: 6871-6878 (Pubitemid 28550281)
-
(1998)
EMBO Journal
, vol.17
, Issue.23
, pp. 6871-6878
-
-
Bimston, D.1
Song, J.2
Winchester, D.3
Takayama, S.4
Reed, J.C.5
Morimoto, R.I.6
-
10
-
-
59349113370
-
Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20
-
Bukach OV, Glukhova AE, Seit-Nebi AS, Gusev NB (2009) Heterooligomeric complexes formed by human small heat shock proteins HspB1 (Hsp27) and HspB6 (Hsp20). Biochim Biophys Acta 1794: 486-495
-
(2009)
Biochim Biophys Acta
, vol.1794
, pp. 486-495
-
-
Bukach, O.V.1
Glukhova, A.E.2
Seit-Nebi, A.S.3
Gusev, N.B.4
-
11
-
-
21244466032
-
A chaperone pathway in protein disaggregation: HSP26 alteks the nature of protein aggregates to facilitate reactivation by HSP104
-
DOI 10.1074/jbc.M502854200
-
Cashikar AG, Duennwald M, Lindquist SL (2005) A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J Biol Chem 280: 23869-23875 (Pubitemid 40884874)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.25
, pp. 23869-23875
-
-
Cashikar, A.G.1
Duennwald, M.2
Lindquist, S.L.3
-
12
-
-
33748747967
-
Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway
-
DOI 10.1074/jbc.M605417200
-
Cintron NS, Toft D (2006) Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway. J Biol Chem 281: 26235-26244 (Pubitemid 44401831)
-
(2006)
Journal of Biological Chemistry
, vol.281
, Issue.36
, pp. 26235-26244
-
-
Cintron, N.S.1
Toft, D.2
-
13
-
-
33748792821
-
Opposing activities protect against age-onset proteotoxicity
-
DOI 10.1126/science.1124646
-
Cohen E, Bieschke J, Perciavalle RM, Kelly JW, Dillin A (2006) Opposing activities protect against age-onset proteotoxicity. Science 313: 1604-1610 (Pubitemid 44414028)
-
(2006)
Science
, vol.313
, Issue.5793
, pp. 1604-1610
-
-
Cohen, E.1
Bieschke, J.2
Perciavalle, R.M.3
Kelly, J.W.4
Dillin, A.5
-
14
-
-
0034647887
-
Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
-
DOI 10.1074/jbc.M001293200
-
Diamant S, Ben-Zvi AP, Bukau B, Goloubinoff P (2000) Sizedependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J Biol Chem 275: 21107-21113 (Pubitemid 30481803)
-
(2000)
Journal of Biological Chemistry
, vol.275
, Issue.28
, pp. 21107-21113
-
-
Diamant, S.1
Peres Ben-Zvi, A.2
Bukau, B.3
Goloubinoff, P.4
-
15
-
-
33745762927
-
Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
-
DOI 10.1038/sj.emboj.7601138, PII 7601138
-
Dragovic Z, Broadley SA, Shomura Y, Bracher A, Hartl FU (2006) Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J 25: 2519-2528 (Pubitemid 44012234)
-
(2006)
EMBO Journal
, vol.25
, Issue.11
, pp. 2519-2528
-
-
Dragovic, Z.1
Broadley, S.A.2
Shomura, Y.3
Bracher, A.4
Hartl, F.U.5
-
16
-
-
0033625965
-
The hsp110 and Grp1 70 stress proteins: Newly recognized relatives of the Hsp70s
-
Easton DP, Kaneko Y, Subjeck JR (2000) The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress Chaperones 5: 276-290
-
(2000)
Cell Stress Chaperones
, vol.5
, pp. 276-290
-
-
Easton, D.P.1
Kaneko, Y.2
Subjeck, J.R.3
-
17
-
-
0343742639
-
Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
-
DOI 10.1093/emboj/16.2.221
-
Ehrnsperger M, Graber S, Gaestel M, Buchner J (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 16: 221-229 (Pubitemid 27049380)
-
(1997)
EMBO Journal
, vol.16
, Issue.2
, pp. 221-229
-
-
Ehrnsperger, M.1
Graber, S.2
Gaestel, M.3
Buchner, J.4
-
18
-
-
77956672926
-
Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta
-
Eroglu B, Moskophidis D, Mivechi NF (2010) Loss of Hsp110 leads to age-dependent tau hyperphosphorylation and early accumulation of insoluble amyloid beta. Mol Cell Biol 30: 4626-4643
-
(2010)
Mol Cell Biol
, vol.30
, pp. 4626-4643
-
-
Eroglu, B.1
Moskophidis, D.2
Mivechi, N.F.3
-
19
-
-
0742305339
-
Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function
-
DOI 10.1091/mbc.E03-03-0146
-
Fan CY, Lee S, Ren HY, Cyr DM (2004) Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol Biol Cell 15: 761-773 (Pubitemid 38146491)
-
(2004)
Molecular Biology of the Cell
, vol.15
, Issue.2
, pp. 761-773
-
-
Fan, C.-Y.1
Lee, S.2
Ren, H.-Y.3
Cyr, D.M.4
-
20
-
-
0036303981
-
Hassles with taking out the garbage: Aggravating aggresomes
-
DOI 10.1034/j.1600-0854.2002.30602.x
-
Garcia-Mata R, Gao YS, Sztul E (2002) Hassles with taking out the garbage: aggravating aggresomes. Traffic 3: 388-396 (Pubitemid 34746406)
-
(2002)
Traffic
, vol.3
, Issue.6
, pp. 388-396
-
-
Garcia-Mata, R.1
Gao, Y.-S.2
Sztul, E.3
-
21
-
-
34548719895
-
Fluorescence lifetime imaging to detect actomyosin states in mammalian muscle sarcomeres
-
DOI 10.1529/biophysj.106.096479
-
Garcia DI, Lanigan P,Webb M,West TG, Requejo-Isidro J, Auksorius E, Dunsby C, Neil M, French P, Ferenczi MA (2007) Fluorescence lifetime imaging to detect actomyosin states in mammalian muscle sarcomeres. Biophys J 93: 2091-2101 (Pubitemid 47437591)
-
(2007)
Biophysical Journal
, vol.93
, Issue.6
, pp. 2091-2101
-
-
Garcia, D.I.1
Lanigan, P.2
Webb, M.3
West, T.G.4
Requejo-Isidro, J.5
Auksorius, E.6
Dunsby, C.7
Neil, M.8
French, P.9
Ferenczi, M.A.10
-
22
-
-
0035980016
-
Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor
-
Gassler CS, Wiederkehr T, Brehmer D, Bukau B, Mayer MP (2001) Bag-1M accelerates nucleotide release for human Hsc70 and Hsp70 and can act concentration-dependent as positive and negative cofactor. J Biol Chem 276: 32538-32544
-
(2001)
J Biol Chem
, vol.276
, pp. 32538-32544
-
-
Gassler, C.S.1
Wiederkehr, T.2
Brehmer, D.3
Bukau, B.4
Mayer, M.P.5
-
23
-
-
33644850056
-
Progressive disruption of cellular protein folding in models of polyglutamine diseases
-
DOI 10.1126/science.1124514
-
Gidalevitz T, Ben-Zvi A, Ho KH, Brignull HR, Morimoto RI (2006) Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311: 1471-1474 (Pubitemid 43376703)
-
(2006)
Science
, vol.311
, Issue.5766
, pp. 1471-1474
-
-
Gidalevitz, T.1
Ben-Zvi, A.2
Ho, K.H.3
Brignull, H.R.4
Morimoto, R.I.5
-
24
-
-
62149129690
-
Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity
-
Gidalevitz T, Krupinski T, Garcia S, Morimoto RI (2009) Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity. PLoS Genet 5: e1000399
-
(2009)
PLoS Genet
, vol.5
-
-
Gidalevitz, T.1
Krupinski, T.2
Garcia, S.3
Morimoto, R.I.4
-
25
-
-
0032503968
-
Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
-
DOI 10.1016/S0092-8674(00)81223-4
-
Glover JR, Lindquist S (1998) Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94: 73-82 (Pubitemid 28347471)
-
(1998)
Cell
, vol.94
, Issue.1
, pp. 73-82
-
-
Glover, J.R.1
Lindquist, S.2
-
26
-
-
0033598703
-
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
-
Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B (1999) Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci USA 96: 13732-13737
-
(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
-
27
-
-
1342329321
-
Apg-2 has a chaperone-like activity similar to Hsp110 and is overexpressed in hepatocellular carcinomas
-
DOI 10.1016/S0014-5793(04)00034-1
-
Gotoh K, Nonoguchi K, Higashitsuji H, Kaneko Y, Sakurai T, Sumitomo Y, Itoh K, Subjeck JR, Fujita J (2004) Apg-2 has a chaperone-like activity similar to Hsp110 and is overexpressed in hepatocellular carcinomas. FEBS Lett 560: 19-24 (Pubitemid 38264286)
-
(2004)
FEBS Letters
, vol.560
, Issue.1-3
, pp. 19-24
-
-
Gotoh, K.1
Nonoguchi, K.2
Higashitsuji, H.3
Kaneko, Y.4
Sakurai, T.5
Sumitomo, Y.6
Itoh, K.7
Subjeck, J.R.8
Fujita, J.9
-
28
-
-
79952833763
-
The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities
-
Hageman J, van Waarde MA, Zylicz A, Walerych D, Kampinga HH (2011) The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities. Biochem J 435: 127-142
-
(2011)
Biochem J
, vol.435
, pp. 127-142
-
-
Hageman, J.1
Van Waarde, M.A.2
Zylicz, A.3
Walerych, D.4
Kampinga, H.H.5
-
29
-
-
79960652801
-
Molecular chaperones in protein folding and proteostasis
-
Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475: 324-332
-
(2011)
Nature
, vol.475
, pp. 324-332
-
-
Hartl, F.U.1
Bracher, A.2
Hayer-Hartl, M.3
-
30
-
-
21244497886
-
Disassembling protein aggregates in the yeast cytosol: The cooperation of HSP26 with SSA1 and HSP104
-
DOI 10.1074/jbc.M502697200
-
Haslbeck M, Miess A, Stromer T, Walter S, Buchner J (2005) Disassembling protein aggregates in the yeast cytosol. The cooperation of Hsp26 with Ssa1 and Hsp104. J Biol Chem 280: 23861-23868 (Pubitemid 40884873)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.25
, pp. 23861-23868
-
-
Haslbeck, M.1
Miess, A.2
Stromer, T.3
Walter, S.4
Buchner, J.5
-
31
-
-
0033485868
-
Hsp26: A temperature-regulated chaperone
-
Haslbeck M, Walke S, Stromer T, Ehrnsperger M, White HE, Chen S, Saibil HR, Buchner J (1999) Hsp26: a temperature-regulated chaperone. EMBO J 18: 6744-6751
-
(1999)
EMBO J
, vol.18
, pp. 6744-6751
-
-
Haslbeck, M.1
Walke, S.2
Stromer, T.3
Ehrnsperger, M.4
White, H.E.5
Chen, S.6
Saibil, H.R.7
Buchner, J.8
-
32
-
-
75349113019
-
Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation
-
Haslberger T, Bukau B, Mogk A (2010) Towards a unifying mechanism for ClpB/Hsp104-mediated protein disaggregation and prion propagation. Biochem Cell Biol 88: 63-75
-
(2010)
Biochem Cell Biol
, vol.88
, pp. 63-75
-
-
Haslberger, T.1
Bukau, B.2
Mogk, A.3
-
33
-
-
44849138934
-
Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
-
DOI 10.1038/nsmb.1425, PII NSMB1425
-
Haslberger T, Zdanowicz A, Brand I, Kirstein J, Turgay K, Mogk A, Bukau B (2008) Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat Struct Mol Biol 15: 641-650 (Pubitemid 351799133)
-
(2008)
Nature Structural and Molecular Biology
, vol.15
, Issue.6
, pp. 641-650
-
-
Haslberger, T.1
Zdanowicz, A.2
Brand, I.3
Kirstein, J.4
Turgay, K.5
Mogk, A.6
Bukau, B.7
-
34
-
-
0027311871
-
A stress-inducible 40 kDa protein (hsp40): Purification by modified two-dimensional gel electrophoresis and co-localization with hsc70(p73) in heat-shocked HeLa cells
-
Hattori H, Kaneda T, Lokeshwar B, Laszlo A, Ohtsuka K (1993) A stress-inducible 40 kDa protein (hsp40): purification by modified two-dimensional gel electrophoresis and co-localization with hsc70(p73) in heat-shocked HeLa cells. J Cell Sci 104(Pt 3): 629-638 (Pubitemid 23123456)
-
(1993)
Journal of Cell Science
, vol.104
, Issue.3
, pp. 629-638
-
-
Hattori, H.1
Kaneda, T.2
Lokeshwar, B.3
Laszlo, A.4
Ohtsuka, K.5
-
35
-
-
0042591262
-
Hsp105α Suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity
-
DOI 10.1074/jbc.M302975200
-
Ishihara K, Yamagishi N, Saito Y, Adachi H, Kobayashi Y, Sobue G, Ohtsuka K, Hatayama T (2003) Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity. J Biol Chem 278: 25143-25150 (Pubitemid 37548678)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.27
, pp. 25143-25150
-
-
Ishihara, K.1
Yamagishi, N.2
Saito, Y.3
Adachi, H.4
Kobayashi, Y.5
Sobue, G.6
Ohtsuka, K.7
Hatayama, T.8
-
36
-
-
67650151030
-
Structural and functional diversity among eukaryotic Hsp70 nucleotide exchange factors
-
Kabani M (2009) Structural and functional diversity among eukaryotic Hsp70 nucleotide exchange factors. Protein Pept Lett 16: 623-660
-
(2009)
Protein Pept Lett
, vol.16
, pp. 623-660
-
-
Kabani, M.1
-
37
-
-
0036275663
-
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
-
DOI 10.1128/MCB.22.13.4677-4689.2002
-
Kabani M, Beckerich JM, Brodsky JL (2002) Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol Cell Biol 22: 4677-4689 (Pubitemid 34620404)
-
(2002)
Molecular and Cellular Biology
, vol.22
, Issue.13
, pp. 4677-4689
-
-
Kabani, M.1
Beckerich, J.-M.2
Brodsky, J.L.3
-
38
-
-
77954947810
-
The HSP70 chaperone machinery J proteins as drivers of functional specificity
-
Kampinga HH, Craig EA (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
-
39
-
-
64549097439
-
Guidelines for the nomenclature of the human heat shock proteins
-
Kampinga HH, Hageman J, Vos MJ, Kubota H, Tanguay RM, Bruford EA, Cheetham ME, Chen B, Hightower LE (2009) Guidelines for the nomenclature of the human heat shock proteins. Cell Stress Chaperones 14: 105-111
-
(2009)
Cell Stress Chaperones
, vol.14
, pp. 105-111
-
-
Kampinga, H.H.1
Hageman, J.2
Vos, M.J.3
Kubota, H.4
Tanguay, R.M.5
Bruford, E.A.6
Cheetham, M.E.7
Chen, B.8
Hightower, L.E.9
-
40
-
-
0036797242
-
Polyglutamine protein aggregates are dynamic
-
Kim S, Nollen EA, Kitagawa K, Bindokas VP, Morimoto RI (2002) Polyglutamine protein aggregates are dynamic. Nat Cell Biol 4: 826-831
-
(2002)
Nat Cell Biol
, vol.4
, pp. 826-831
-
-
Kim, S.1
Nollen, E.A.2
Kitagawa, K.3
Bindokas, V.P.4
Morimoto, R.I.5
-
41
-
-
0031024691
-
A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
-
DOI 10.1093/emboj/16.3.659
-
Lee GJ, Roseman AM, Saibil HR, Vierling E (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J 16: 659-671 (Pubitemid 27067794)
-
(1997)
EMBO Journal
, vol.16
, Issue.3
, pp. 659-671
-
-
Lee, G.J.1
Roseman, A.M.2
Saibil, H.R.3
Vierling, E.4
-
42
-
-
34447649757
-
Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process
-
DOI 10.1016/j.jmb.2007.05.057, PII S0022283607007103
-
Lewandowska A, Matuszewska M, Liberek K (2007) Conformational properties of aggregated polypeptides determine ClpB-dependence in the disaggregation process. J Mol Biol 371: 800-811 (Pubitemid 47087823)
-
(2007)
Journal of Molecular Biology
, vol.371
, Issue.3
, pp. 800-811
-
-
Lewandowska, A.1
Matuszewska, M.2
Liberek, K.3
-
43
-
-
0032561360
-
Protein folding activity of Hsp70 is modified differentially by the Hsp40 co-chaperones Sis1 and Ydj1
-
DOI 10.1074/jbc.273.43.27824
-
Lu Z, Cyr DM (1998) Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J Biol Chem 273: 27824-27830 (Pubitemid 28496069)
-
(1998)
Journal of Biological Chemistry
, vol.273
, Issue.43
, pp. 27824-27830
-
-
Lu, Z.1
Cyr, D.M.2
-
44
-
-
79955563304
-
Species-specific collaboration of heat shock proteins (Hsp 70 and 100 in thermotolerance and protein disaggregation
-
Miot M, Reidy M, Doyle SM, Hoskins JR, Johnston DM, Genest O, Vitery MC, Masison DC, Wickner S (2011) Species-specific collaboration of heat shock proteins (Hsp) 70 and 100 in thermotolerance and protein disaggregation. Proc Natl Acad Sci USA 108: 6915-6920
-
(2011)
Proc Natl Acad Sci USA
, vol.108
, pp. 6915-6920
-
-
Miot, M.1
Reidy, M.2
Doyle, S.M.3
Hoskins, J.R.4
Johnston, D.M.5
Genest, O.6
Vitery, M.C.7
Masison, D.C.8
Wickner, S.9
-
45
-
-
0142125283
-
Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
-
DOI 10.1046/j.1365-2958.2003.03710.x
-
Mogk A, Deuerling E, Vorderwulbecke S, Vierling E, Bukau B (2003a) Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol 50: 585-595 (Pubitemid 37297136)
-
(2003)
Molecular Microbiology
, vol.50
, Issue.2
, pp. 585-595
-
-
Mogk, A.1
Deuerling, E.2
Vorderwulbecke, S.3
Vierling, E.4
Bukau, B.5
-
46
-
-
0042733148
-
Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK
-
DOI 10.1074/jbc.M303587200
-
Mogk A, Schlieker C, Friedrich KL, Schonfeld HJ, Vierling E, Bukau B (2003b) Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK. J Biol Chem 278: 31033-31042 (Pubitemid 36994617)
-
(2003)
Journal of Biological Chemistry
, vol.278
, Issue.33
, pp. 31033-31042
-
-
Mogk, A.1
Schlieker, C.2
Friedrich, K.L.3
Schonfeld, H.-J.4
Vierling, E.5
Bukau, B.6
-
47
-
-
77950239058
-
Discovery and characterization of a mammalian amyloid disaggregation activity
-
Murray AN, Solomon JP, Wang YJ, Balch WE, Kelly JW (2010) Discovery and characterization of a mammalian amyloid disaggregation activity. Protein Sci 19: 836-846
-
(2010)
Protein Sci
, vol.19
, pp. 836-846
-
-
Murray, A.N.1
Solomon, J.P.2
Wang, Y.J.3
Balch, W.E.4
Kelly, J.W.5
-
49
-
-
1542719908
-
Concerted and nonconcerted evolution of the Hsp70 gene superfamily in two sibling species of nematodes
-
DOI 10.1093/molbev/msh041
-
Nikolaidis N, Nei M (2004) Concerted and nonconcerted evolution of the Hsp70 gene superfamily in two sibling species of nematodes. Mol Biol Evol 21: 498-505 (Pubitemid 38339666)
-
(2004)
Molecular Biology and Evolution
, vol.21
, Issue.3
, pp. 498-505
-
-
Nikolaidis, N.1
Nei, M.2
-
50
-
-
0000905027
-
The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions
-
Oh HJ, Easton D, Murawski M, Kaneko Y, Subjeck JR (1999) The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions. J Biol Chem 274: 15712-15718
-
(1999)
J Biol Chem
, vol.274
, pp. 15712-15718
-
-
Oh, H.J.1
Easton, D.2
Murawski, M.3
Kaneko, Y.4
Subjeck, J.R.5
-
51
-
-
78650963274
-
Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
-
Olzscha H, Schermann SM, Woerner AC, Pinkert S, Hecht MH, Tartaglia GG, Vendruscolo M, Hayer-Hartl M, Hartl FU, Vabulas RM (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
-
52
-
-
0030945296
-
GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism
-
DOI 10.1021/bi962835l
-
Packschies L, Theyssen H, Buchberger A, Bukau B, Goody RS, Reinstein J (1997) GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry 36: 3417-3422 (Pubitemid 27143493)
-
(1997)
Biochemistry
, vol.36
, Issue.12
, pp. 3417-3422
-
-
Packschies, L.1
Theyssen, H.2
Buchberger, A.3
Bukau, B.4
Goody, R.S.5
Reinstein, J.6
-
53
-
-
0027996115
-
Protein disaggregation mediated by heat-shock protein Hsp104
-
Parsell DA, Kowal AS, Singer MA, Lindquist S (1994) Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372: 475-478
-
(1994)
Nature
, vol.372
, pp. 475-478
-
-
Parsell, D.A.1
Kowal, A.S.2
Singer, M.A.3
Lindquist, S.4
-
54
-
-
44649110104
-
Structural Basis for the Cooperation of Hsp70 and Hsp110 Chaperones in Protein Folding
-
DOI 10.1016/j.cell.2008.05.022, PII S0092867408006788
-
Polier S, Dragovic Z, Hartl FU, Bracher A (2008) Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133: 1068-1079 (Pubitemid 351787748)
-
(2008)
Cell
, vol.133
, Issue.6
, pp. 1068-1079
-
-
Polier, S.1
Dragovic, Z.2
Hartl, F.U.3
Bracher, A.4
-
55
-
-
77955559261
-
Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein
-
Polier S, Hartl FU, Bracher A (2010) Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein. J Mol Biol 401: 696-707
-
(2010)
J Mol Biol
, vol.401
, pp. 696-707
-
-
Polier, S.1
Hartl, F.U.2
Bracher, A.3
-
56
-
-
0034119621
-
Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis
-
DOI 10.1105/tpc.12.4.479
-
Queitsch C, Hong SW, Vierling E, Lindquist S (2000) Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. Plant Cell 12: 479-492 (Pubitemid 30254866)
-
(2000)
Plant Cell
, vol.12
, Issue.4
, pp. 479-492
-
-
Queitsch, C.1
Hong, S.-W.2
Vierling, E.3
Lindquist, S.4
-
57
-
-
80054740161
-
Nucleotide exchange factors for hsp70 chaperones
-
Rampelt H, Mayer MP, Bukau B (2011) Nucleotide exchange factors for hsp70 chaperones. Methods Mol Biol 787: 83-91
-
(2011)
Methods Mol Biol
, vol.787
, pp. 83-91
-
-
Rampelt, H.1
Mayer, M.P.2
Bukau, B.3
-
58
-
-
58549098512
-
Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation
-
Ratajczak E, Zietkiewicz S, Liberek K (2009) Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation. J Mol Biol 386: 178-189
-
(2009)
J Mol Biol
, vol.386
, pp. 178-189
-
-
Ratajczak, E.1
Zietkiewicz, S.2
Liberek, K.3
-
59
-
-
29344449706
-
Human and yeast Hsp110 chaperones exhibit functional differences
-
DOI 10.1016/j.febslet.2005.11.069, PII S0014579305014468
-
Raviol H, Bukau B, Mayer MP (2006a) Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett 580: 168-174 (Pubitemid 43005331)
-
(2006)
FEBS Letters
, vol.580
, Issue.1
, pp. 168-174
-
-
Raviol, H.1
Bukau, B.2
Mayer, M.P.3
-
60
-
-
33745749328
-
Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
-
DOI 10.1038/sj.emboj.7601139, PII 7601139
-
Raviol H, Sadlish H, Rodriguez F, Mayer MP, Bukau B (2006b) Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J 25: 2510-2518 (Pubitemid 44012233)
-
(2006)
EMBO Journal
, vol.25
, Issue.11
, pp. 2510-2518
-
-
Raviol, H.1
Sadlish, H.2
Rodriguez, F.3
Mayer, M.P.4
Bukau, B.5
-
61
-
-
79960928455
-
Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin
-
Sandler H, Kreth J, Timmers HT, Stoecklin G (2011) Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin. Nucleic Acids Res 39: 4373-4386
-
(2011)
Nucleic Acids Res
, vol.39
, pp. 4373-4386
-
-
Sandler, H.1
Kreth, J.2
Timmers, H.T.3
Stoecklin, G.4
-
62
-
-
0027427986
-
DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
-
Schröder H, Langer T, Hartl FU, Bukau B (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J 12: 4137-4144 (Pubitemid 23302027)
-
(1993)
EMBO Journal
, vol.12
, Issue.11
, pp. 4137-4144
-
-
Schroder, H.1
Langer, T.2
Hartl, F.-U.3
Bukau, B.4
-
63
-
-
2542435778
-
The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related Hsp70 family
-
DOI 10.1074/jbc.M313739200
-
Shaner L, Trott A, Goeckeler JL, Brodsky JL, Morano KA (2004) The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family. J Biol Chem 279: 21992-22001 (Pubitemid 38679390)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.21
, pp. 21992-22001
-
-
Shaner, L.1
Trott, A.2
Goeckeler, J.L.3
Brodsky, J.L.4
Morano, K.A.5
-
64
-
-
80054699747
-
The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system
-
Shorter J (2011) The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS ONE 6: e26319
-
(2011)
PLoS ONE
, vol.6
-
-
Shorter, J.1
-
65
-
-
84857450272
-
Structural and functional specificity of small heat shock protein HspB1 and HspB4, two cellular partners of HspB5: Role of the in vitro hetero-complex formation in chaperone activity
-
Skouri-Panet F, Michiel M, Ferard C, Duprat E, Finet S (2011) Structural and functional specificity of small heat shock protein HspB1 and HspB4, two cellular partners of HspB5: Role of the in vitro hetero-complex formation in chaperone activity. Biochimie 94: 975-984
-
(2011)
Biochimie
, vol.94
, pp. 975-984
-
-
Skouri-Panet, F.1
Michiel, M.2
Ferard, C.3
Duprat, E.4
Finet, S.5
-
66
-
-
0035936826
-
Structure of a Bag/Hsc70 complex: Convergent functional evolution of Hsp70 nucleotide exchange factors
-
DOI 10.1126/science.1057268
-
Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I (2001) Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291: 1553-1557 (Pubitemid 32179223)
-
(2001)
Science
, vol.291
, Issue.5508
, pp. 1553-1557
-
-
Sondermann, H.1
Scheufler, C.2
Schneider, C.3
Hohfeld, J.4
Hartl, F.-U.5
Moarefi, I.6
-
67
-
-
0034637603
-
Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70
-
DOI 10.1074/jbc.M002021200
-
Terada K, Mori M (2000) Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. J Biol Chem 275: 24728-24734 (Pubitemid 30626575)
-
(2000)
Journal of Biological Chemistry
, vol.275
, Issue.32
, pp. 24728-24734
-
-
Terada, K.1
Mori, M.2
-
68
-
-
40649098449
-
Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
-
DOI 10.1111/j.1365-2958.2008.06135.x
-
Tessarz P, Mogk A, Bukau B (2008) Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol Microbiol 68: 87-97 (Pubitemid 351372041)
-
(2008)
Molecular Microbiology
, vol.68
, Issue.1
, pp. 87-97
-
-
Tessarz, P.1
Mogk, A.2
Bukau, B.3
-
69
-
-
77958487260
-
Cellular strategies for controlling protein aggregation
-
Tyedmers J, Mogk A, Bukau B (2010) Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 11: 777-788
-
(2010)
Nat Rev Mol Cell Biol
, vol.11
, pp. 777-788
-
-
Tyedmers, J.1
Mogk, A.2
Bukau, B.3
-
70
-
-
55249125453
-
Functional divergence between co-chaperones of Hsc70
-
Tzankov S, Wong MJ, Shi K, Nassif C, Young JC (2008) Functional divergence between co-chaperones of Hsc70. J Biol Chem 283: 27100-27109
-
(2008)
J Biol Chem
, vol.283
, pp. 27100-27109
-
-
Tzankov, S.1
Wong, M.J.2
Shi, K.3
Nassif, C.4
Young, J.C.5
-
71
-
-
34250670010
-
Heat shock protein 40/DjB1 is required for thermotolerance in early phase
-
DOI 10.1093/jb/mvj212
-
Uchiyama Y, Takeda N, Mori M, Terada K (2006) Heat shock protein 40/DjB1 is required for thermotolerance in early phase. J Biochem 140: 805-812 (Pubitemid 46941010)
-
(2006)
Journal of Biochemistry
, vol.140
, Issue.6
, pp. 805-812
-
-
Uchiyama, Y.1
Takeda, N.2
Mori, M.3
Terada, K.4
-
73
-
-
46849116411
-
Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
-
DOI 10.1021/bi800639z
-
Vos MJ, Hageman J, Carra S, Kampinga HH (2008) Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 47: 7001-7011 (Pubitemid 351956349)
-
(2008)
Biochemistry
, vol.47
, Issue.27
, pp. 7001-7011
-
-
Vos, M.J.1
Hageman, J.2
Carra, S.3
Kampinga, H.H.4
-
74
-
-
60849126687
-
Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS
-
Wang J, Farr GW, Zeiss CJ, Rodriguez-Gil DJ, Wilson JH, Furtak K, Rutkowski DT, Kaufman RJ, Ruse CI, Yates 3rd JR, Perrin S, Feany MB, Horwich AL (2009) Progressive aggregation despite chaperone associations of a mutant SOD1-YFP in transgenic mice that develop ALS. Proc Natl Acad Sci USA 106: 1392-1397
-
(2009)
Proc Natl Acad Sci USA
, vol.106
, pp. 1392-1397
-
-
Wang, J.1
Farr, G.W.2
Zeiss, C.J.3
Rodriguez-Gil, D.J.4
Wilson, J.H.5
Furtak, K.6
Rutkowski, D.T.7
Kaufman, R.J.8
Ruse, C.I.9
Yates III, J.R.10
Perrin, S.11
Feany, M.B.12
Horwich, A.L.13
-
75
-
-
8844251486
-
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
-
DOI 10.1016/j.cell.2004.11.027, PII S0092867404010529
-
Weibezahn J, Tessarz P, Schlieker C, Zahn R, Maglica Z, Lee S, Zentgraf H, Weber-Ban EU, Dougan DA, Tsai FT, Mogk A, Bukau B (2004) Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119: 653-665 (Pubitemid 39535753)
-
(2004)
Cell
, vol.119
, Issue.5
, 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.F.10
Mogk, A.11
Bukau, B.12
-
76
-
-
0028287525
-
Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. I. Kinetic analyses of active site mutants
-
Wilbanks SM, DeLuca-Flaherty C, McKay DB (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
-
77
-
-
84866438776
-
Hsp70 target Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
-
Winkler J, Tyedmers J, Bukau B, Mogk A (2012) Hsp70 target Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198: 387-404
-
(2012)
J Cell Biol
, vol.198
, pp. 387-404
-
-
Winkler, J.1
Tyedmers, J.2
Bukau, B.3
Mogk, A.4
-
78
-
-
84863155446
-
Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity
-
Xu X, Sarbeng EB, Vorvis C, Kumar DP, Zhou L, Liu Q (2012) Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity. J Biol Chem 287: 5661-5672
-
(2012)
J Biol Chem
, vol.287
, pp. 5661-5672
-
-
Xu, X.1
Sarbeng, E.B.2
Vorvis, C.3
Kumar, D.P.4
Zhou, L.5
Liu, Q.6
-
79
-
-
4744370912
-
Hsp105α suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity
-
DOI 10.1074/jbc.M407947200
-
Yamagishi N, Ishihara K, Hatayama T (2004) Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity. J Biol Chem 279: 41727-41733 (Pubitemid 39313618)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.40
, pp. 41727-41733
-
-
Yamagishi, N.1
Ishihara, K.2
Hatayama, T.3
-
80
-
-
79956207695
-
Characterization of stress sensitivity and chaperone activity of Hsp105 in mammalian cells
-
Yamagishi N, Yokota M, Yasuda K, Saito Y, Nagata K, Hatayama T (2011) Characterization of stress sensitivity and chaperone activity of Hsp105 in mammalian cells. Biochem Biophys Res Commun 409: 90-95
-
(2011)
Biochem Biophys Res Commun
, vol.409
, pp. 90-95
-
-
Yamagishi, N.1
Yokota, M.2
Yasuda, K.3
Saito, Y.4
Nagata, K.5
Hatayama, T.6
-
81
-
-
34547893834
-
Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: Clues to a possible strategy for treating ALS
-
DOI 10.1111/j.1471-4159.2007.04534.x
-
Yamashita H, Kawamata J, Okawa K, Kanki R, Nakamizo T, Hatayama T, Yamanaka K, Takahashi R, Shimohama S (2007) Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS. J Neurochem 102: 1497-1505 (Pubitemid 47256189)
-
(2007)
Journal of Neurochemistry
, vol.102
, Issue.5
, pp. 1497-1505
-
-
Yamashita, H.1
Kawamata, J.2
Okawa, K.3
Kanki, R.4
Nakamizo, T.5
Hatayama, T.6
Yamanaka, K.7
Takahashi, R.8
Shimohama, S.9
-
82
-
-
0029564092
-
Cloning and expression of murine high molecular mass heat shock proteins, HSP105
-
DOI 10.1074/jbc.270.50.29718
-
Yasuda K, Nakai A, Hatayama T, Nagata K (1995) Cloning and expression of murine high molecular mass heat shock proteins, HSP105. J Biol Chem 270: 29718-29723 (Pubitemid 26001637)
-
(1995)
Journal of Biological Chemistry
, vol.270
, Issue.50
, pp. 29718-29723
-
-
Yasuda, K.1
Nakai, A.2
Hatayama, T.3
Nagata, K.4
-
83
-
-
77950600645
-
Mechanisms of the Hsp70 chaperone system
-
Young JC (2010) Mechanisms of the Hsp70 chaperone system. Biochem Cell Biol 88: 291-300
-
(2010)
Biochem Cell Biol
, vol.88
, pp. 291-300
-
-
Young, J.C.1
-
84
-
-
7244247277
-
Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation
-
DOI 10.1074/jbc.M402405200
-
Zietkiewicz S, Krzewska J, Liberek K (2004) Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J Biol Chem 279: 44376-44383 (Pubitemid 39430842)
-
(2004)
Journal of Biological Chemistry
, vol.279
, Issue.43
, pp. 44376-44383
-
-
Zietkiewicz, S.1
Krzewska, J.2
Liberek, K.3
-
85
-
-
33646354916
-
Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation
-
DOI 10.1074/jbc.M507893200
-
Zietkiewicz S, Lewandowska A, Stocki P, Liberek K (2006) Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100- dependent disaggregation. J Biol Chem 281: 7022-7029 (Pubitemid 43847465)
-
(2006)
Journal of Biological Chemistry
, vol.281
, Issue.11
, pp. 7022-7029
-
-
Zietkiewicz, S.1
Lewandowska, A.2
Stocki, P.3
Liberek, K.4
|