-
1
-
-
0015859467
-
Principles that govern folding of protein chains
-
Anfinsen, C. B. (1973). Principles that govern folding of protein chains. Science 181, 223-230. doi: 10.1126/science.181.4096.223
-
(1973)
Science
, vol.181
, pp. 223-230
-
-
Anfinsen, C.B.1
-
2
-
-
84865542140
-
Comparison and applications of label-free absolute proteome quantification methods on Escherichia coli
-
Arike, L., Valgepea, K., Peil, L., Nahku, R., Adamberg, K., and Vilu, R. (2012). Comparison and applications of label-free absolute proteome quantification methods on Escherichia coli. J. Proteomics 75, 5437-5448. doi: 10.1016/j.jprot.2012.06.020
-
(2012)
J. Proteomics
, vol.75
, pp. 5437-5448
-
-
Arike, L.1
Valgepea, K.2
Peil, L.3
Nahku, R.4
Adamberg, K.5
Vilu, R.6
-
3
-
-
0037890192
-
The heat shock response of Escherichia coli
-
Arsene, F., Tomoyasu, T., and Bukau, B. (2000). The heat shock response of Escherichia coli. Int. J. Food Microbiol. 55, 3-9. doi: 10.1016/S0168-1605(00)00206-3
-
(2000)
Int. J. Food Microbiol
, vol.55
, pp. 3-9
-
-
Arsene, F.1
Tomoyasu, T.2
Bukau, B.3
-
4
-
-
81855200106
-
Enhanced Hsp70 expression protects against acute lung injury by modulating apoptotic pathways
-
Aschkenasy, G., Bromberg, Z., Raj, N., Deutschman, C. S., and Weiss, Y. G. (2011). Enhanced Hsp70 expression protects against acute lung injury by modulating apoptotic pathways. PLoS ONE 6:e26956. doi: 10.1371/journal.pone.0026956
-
(2011)
PLoS ONE
, vol.6
-
-
Aschkenasy, G.1
Bromberg, Z.2
Raj, N.3
Deutschman, C.S.4
Weiss, Y.G.5
-
5
-
-
32544434839
-
Clathrin and synaptic vesicle endocytosis: studies at the squid giant synapse
-
Augustine, G. J., Morgan, J. R., Villalba-Galea, C. A., Jin, S., Prasad, K., and Lafer, E. M. (2006). Clathrin and synaptic vesicle endocytosis: studies at the squid giant synapse. Biochem. Soc. Trans. 34, 68-72. doi: 10.1042/BST0340068
-
(2006)
Biochem. Soc. Trans
, vol.34
, pp. 68-72
-
-
Augustine, G.J.1
Morgan, J.R.2
Villalba-Galea, C.A.3
Jin, S.4
Prasad, K.5
Lafer, E.M.6
-
6
-
-
57049093241
-
Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases
-
Bellotti, V., and Chiti, F. (2008). Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. Curr. Opin. Struct. Biol. 18, 771-779. doi: 10.1016/j.sbi.2008.10.001
-
(2008)
Curr. Opin. Struct. Biol
, vol.18
, pp. 771-779
-
-
Bellotti, V.1
Chiti, F.2
-
7
-
-
4444288866
-
Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones
-
Ben-Zvi, A., De Los Rios, P., Dietler, G., and Goloubinoff, P. (2004). Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual Hsp70 chaperones. J. Biol. Chem, 279, 37298-37303. doi: 10.1074/jbc. M405627200
-
(2004)
J. Biol. Chem
, vol.279
, pp. 37298-37303
-
-
Ben-Zvi, A.1
De Los Rios, P.2
Dietler, G.3
Goloubinoff, P.4
-
8
-
-
0037147221
-
Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones
-
Ben-Zvi, A. P., and Goloubinoff, P. (2002). Proteinaceous infectious behavior in non-pathogenic proteins is controlled by molecular chaperones. J. Biol. Chem. 277, 49422-49427. doi: 10.1074/jbc. M209163200
-
(2002)
J. Biol. Chem
, vol.277
, pp. 49422-49427
-
-
Ben-Zvi, A.P.1
Goloubinoff, P.2
-
9
-
-
79951837256
-
Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism
-
Chang, L., Miyata, Y., Ung, P. M., Bertelsen, E. B., Mcquade, T. J., Carlson, H. A., et al. (2011). Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism. Chem. Biol, 18, 210-221. doi: 10.1016/j.chembiol.2010.12.010
-
(2011)
Chem. Biol
, vol.18
, pp. 210-221
-
-
Chang, L.1
Miyata, Y.2
Ung, P.M.3
Bertelsen, E.B.4
Mcquade, T.J.5
Carlson, H.A.6
-
10
-
-
84929280343
-
Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli
-
Cho, Y., Zhang, X., Pobre, K. F., Liu, Y., Powers, D. L., Kelly, J. W., et al. (2015). Individual and collective contributions of chaperoning and degradation to protein homeostasis in E. coli. Cell Rep. 11, 321-333. doi: 10.1016/j.celrep.2015.03.018
-
(2015)
Cell Rep
, vol.11
, pp. 321-333
-
-
Cho, Y.1
Zhang, X.2
Pobre, K.F.3
Liu, Y.4
Powers, D.L.5
Kelly, J.W.6
-
11
-
-
84924139172
-
How Hsp70 molecular machines interact with their substrates to mediate diverse physiological functions
-
Clerico, E. M., Tilitsky, J. M., Meng, W., and Gierasch, L. M. (2015). How Hsp70 molecular machines interact with their substrates to mediate diverse physiological functions. J. Mol. Biol. 427, 1575-1588. doi: 10.1016/j.jmb.2015.02.004
-
(2015)
J. Mol. Biol
, vol.427
, pp. 1575-1588
-
-
Clerico, E.M.1
Tilitsky, J.M.2
Meng, W.3
Gierasch, L.M.4
-
12
-
-
84861653381
-
A chaperone trap contributes to the onset of cystic fibrosis
-
Coppinger, J. A., Hutt, D. M., Razvi, A., Koulov, A. V., Pankow, S., Yates, J. R. III, et al. (2012). A chaperone trap contributes to the onset of cystic fibrosis. PLoS ONE 7:e37682. doi: 10.1371/journal.pone.0037682
-
(2012)
PLoS ONE
, vol.7
-
-
Coppinger, J.A.1
Hutt, D.M.2
Razvi, A.3
Koulov, A.V.4
Pankow, S.5
Yates, J.R.6
-
13
-
-
0036629253
-
Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
-
Cyr, D. M., Hohfeld, J., and Patterson, C. (2002). Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem. Sci. 27, 368-375. doi: 10.1016/S0968-0004(02)02125-4
-
(2002)
Trends Biochem. Sci
, vol.27
, pp. 368-375
-
-
Cyr, D.M.1
Hohfeld, J.2
Patterson, C.3
-
14
-
-
33646557371
-
Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling
-
De Los Rios, P., Ben-Zvi, A., Slutsky, O., Azem, A., and Goloubinoff, P. (2006). Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc. Natl. Acad. Sci. U.S.A. 103, 6166-6171. doi: 10.1073/pnas.0510496103
-
(2006)
Proc. Natl. Acad. Sci. U.S.A
, vol.103
, pp. 6166-6171
-
-
De Los Rios, P.1
Ben-Zvi, A.2
Slutsky, O.3
Azem, A.4
Goloubinoff, P.5
-
15
-
-
0035899897
-
Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling
-
Demand, J., Alberti, S., Patterson, C., and Hohfeld, J. (2001). Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling. Curr. Biol. 11, 1569-1577. doi: 10.1016/S0960-9822(01)00487-0
-
(2001)
Curr. Biol
, vol.11
, pp. 1569-1577
-
-
Demand, J.1
Alberti, S.2
Patterson, C.3
Hohfeld, J.4
-
16
-
-
0034647887
-
Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
-
Diamant, S., Ben-Zvi, A. P., Bukau, B., and Goloubinoff, P. (2000). Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J. Biol. Chem. 275, 21107-21113. doi: 10.1074/jbc. M001293200
-
(2000)
J. Biol. Chem
, vol.275
, pp. 21107-21113
-
-
Diamant, S.1
Ben-Zvi, A.P.2
Bukau, B.3
Goloubinoff, P.4
-
17
-
-
0032493416
-
Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration
-
Diamant, S., and Goloubinoff, P. (1998). Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration. Biochemistry 37, 9688-9694. doi: 10.1021/bi980338u
-
(1998)
Biochemistry
, vol.37
, pp. 9688-9694
-
-
Diamant, S.1
Goloubinoff, P.2
-
18
-
-
0032571320
-
The role of DnaJ-like proteins in glucocorticoid receptor center dot hsp90 heterocomplex assembly by the reconstituted hsp90 center dot p60 center dot hsp70 foldosome complex
-
Dittmar, K. D., Banach, M., Galigniana, M. D., and Pratt, W. B. (1998). The role of DnaJ-like proteins in glucocorticoid receptor center dot hsp90 heterocomplex assembly by the reconstituted hsp90 center dot p60 center dot hsp70 foldosome complex. J. Biol. Chem. 273, 7358-7366. doi: 10.1074/jbc.273.13.7358
-
(1998)
J. Biol. Chem
, vol.273
, pp. 7358-7366
-
-
Dittmar, K.D.1
Banach, M.2
Galigniana, M.D.3
Pratt, W.B.4
-
19
-
-
85005900833
-
Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies
-
Ebrahimi-Fakhari, D., Saidi, L. J., and Wahlster, L. (2013). Molecular chaperones and protein folding as therapeutic targets in Parkinson's disease and other synucleinopathies. Acta Neuropathol. Commun. 1, 79. doi: 10.1186/2051-5960-1-79
-
(2013)
Acta Neuropathol. Commun
, vol.1
, pp. 79
-
-
Ebrahimi-Fakhari, D.1
Saidi, L.J.2
Wahlster, L.3
-
20
-
-
77953020807
-
Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility
-
Echeverria, P. C., and Picard, D. (2010). Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility. Biochim. Biophys. Acta 1803, 641-649. doi: 10.1016/j.bbamcr.2009.11.012
-
(2010)
Biochim. Biophys. Acta
, vol.1803
, pp. 641-649
-
-
Echeverria, P.C.1
Picard, D.2
-
21
-
-
67049108831
-
The mitochondrial protein translocation motor: structural conservation between the human and yeast Tim14/Pam18-Tim16/Pam16 co-chaperones
-
Elsner, S., Simian, D., Iosefson, O., Marom, M., and Azem, A. (2009). The mitochondrial protein translocation motor: structural conservation between the human and yeast Tim14/Pam18-Tim16/Pam16 co-chaperones. Int. J. Mol. Sci. 10, 2041-2053. doi: 10.3390/ijms10052041
-
(2009)
Int. J. Mol. Sci
, vol.10
, pp. 2041-2053
-
-
Elsner, S.1
Simian, D.2
Iosefson, O.3
Marom, M.4
Azem, A.5
-
22
-
-
77449100739
-
Structural analysis of the ribosome-associated complex (RAC) reveals an unusual Hsp70/Hsp40 interaction
-
Fiaux, J., Horst, J., Scior, A., Preissler, S., Koplin, A., Bukau, B., et al. (2010). Structural analysis of the ribosome-associated complex (RAC) reveals an unusual Hsp70/Hsp40 interaction. J. Biol. Chem. 285, 3227-3234. doi: 10.1074/jbc. M109.075804
-
(2010)
J. Biol. Chem
, vol.285
, pp. 3227-3234
-
-
Fiaux, J.1
Horst, J.2
Scior, A.3
Preissler, S.4
Koplin, A.5
Bukau, B.6
-
23
-
-
84883049362
-
Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
-
Finka, A., and Goloubinoff, P. (2013). Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis. Cell Stress Chaperones 18, 591-605. doi: 10.1007/s12192-013-0413-3
-
(2013)
Cell Stress Chaperones
, vol.18
, pp. 591-605
-
-
Finka, A.1
Goloubinoff, P.2
-
24
-
-
79951681576
-
Meta-analysis of heat-and chemically upregulated chaperone genes in plant and human cells
-
Finka, A., Mattoo, R. U., and Goloubinoff, P. (2011). Meta-analysis of heat-and chemically upregulated chaperone genes in plant and human cells. Cell Stress Chaperones 16, 15-31. doi: 10.1007/s12192-010-0216-8
-
(2011)
Cell Stress Chaperones
, vol.16
, pp. 15-31
-
-
Finka, A.1
Mattoo, R.U.2
Goloubinoff, P.3
-
25
-
-
84930864339
-
Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs
-
[Epub ahead of print]
-
Finka, A., Sood, V., Quadroni, M., Rios, P., and Goloubinoff, P. (2015). Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs. Cell Stress Chaperones. doi: 10.1007/s12192-015-0583-2. [Epub ahead of print]
-
(2015)
Cell Stress Chaperones
-
-
Finka, A.1
Sood, V.2
Quadroni, M.3
Rios, P.4
Goloubinoff, P.5
-
26
-
-
67650661943
-
The perspectives of studying multi-domain protein folding
-
Fitter, J. (2009). The perspectives of studying multi-domain protein folding. Cell. Mol. Life Sci. 66, 1672-1681. doi: 10.1007/s00018-009-8771-9
-
(2009)
Cell. Mol. Life Sci
, vol.66
, pp. 1672-1681
-
-
Fitter, J.1
-
27
-
-
0026696625
-
Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32
-
Gamer, J., Bujard, H., and Bukau, B. (1992). Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32. Cell 69, 833-842. doi: 10.1016/0092-8674(92)90294-M
-
(1992)
Cell
, vol.69
, pp. 833-842
-
-
Gamer, J.1
Bujard, H.2
Bukau, B.3
-
28
-
-
84857938446
-
Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins
-
Geiger, T., Wehner, A., Schaab, C., Cox, J., and Mann, M. (2012). Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins. Mol. Cell. Proteomics 11, M111.014050. doi: 10.1074/mcp. M111.014050
-
(2012)
Mol. Cell. Proteomics
, vol.11
-
-
Geiger, T.1
Wehner, A.2
Schaab, C.3
Cox, J.4
Mann, M.5
-
29
-
-
34547146401
-
The mechanism of Hsp70 chaperones: (entropic) pulling the models together
-
Goloubinoff, P., and De Los Rios, P. (2007). The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends Biochem. Sci. 32, 372-380. doi: 10.1016/j.tibs.2007.06.008
-
(2007)
Trends Biochem. Sci
, vol.32
, pp. 372-380
-
-
Goloubinoff, P.1
De Los Rios, P.2
-
30
-
-
0033598703
-
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
-
Goloubinoff, P., Mogk, A., Ben Zvi, A. P., Tomoyasu, T., and Bukau, B. (1999). Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. U.S.A. 96, 13732-13737. doi: 10.1073/pnas.96.24.13732
-
(1999)
Proc. Natl. Acad. Sci. U.S.A
, vol.96
, pp. 13732-13737
-
-
Goloubinoff, P.1
Mogk, A.2
Ben Zvi, A.P.3
Tomoyasu, T.4
Bukau, B.5
-
31
-
-
84905484604
-
BiP clustering facilitates protein folding in the endoplasmic reticulum
-
Griesemer, M., Young, C., Robinson, A. S., and Petzold, L. (2014). BiP clustering facilitates protein folding in the endoplasmic reticulum. PLoS Comput. Biol. 10:e1003675. doi: 10.1371/journal.pcbi.1003675
-
(2014)
PLoS Comput. Biol
, vol.10
-
-
Griesemer, M.1
Young, C.2
Robinson, A.S.3
Petzold, L.4
-
32
-
-
0035794207
-
Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system
-
Grimshaw, J. P., Jelesarov, I., Schonfeld, H. J., and Christen, P. (2001). Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J. Biol. Chem. 276, 6098-6104. doi: 10.1074/jbc. M009290200
-
(2001)
J. Biol. Chem
, vol.276
, pp. 6098-6104
-
-
Grimshaw, J.P.1
Jelesarov, I.2
Schonfeld, H.J.3
Christen, P.4
-
33
-
-
84964240132
-
Assays to characterize molecular chaperone function in vitro
-
Haslbeck, M., and Buchner, J. (2015). Assays to characterize molecular chaperone function in vitro. Methods Mol. Biol. 1292, 39-51. doi: 10.1007/978-1-4939-2522-3_3
-
(2015)
Methods Mol. Biol
, vol.1292
, pp. 39-51
-
-
Haslbeck, M.1
Buchner, J.2
-
34
-
-
34147102801
-
Chaperones and proteases-Cellular fold-controlling factors of proteins in Neurodegenerative diseases and aging
-
Hinault, M. P., Ben-Zvi, A., and Goloubinoff, P. (2006). Chaperones and proteases-Cellular fold-controlling factors of proteins in Neurodegenerative diseases and aging. J. Mol. Neurosci. 30, 249-265. doi: 10.1385/JMN:30:3:249
-
(2006)
J. Mol. Neurosci
, vol.30
, pp. 249-265
-
-
Hinault, M.P.1
Ben-Zvi, A.2
Goloubinoff, P.3
-
35
-
-
78649640867
-
Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones
-
Hinault, M. P., Cuendet, A. F., Mattoo, R. U., Mensi, M., Dietler, G., Lashuel, H. A., et al. (2010). Stable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperones. J. Biol. Chem. 285, 38173-38182. doi: 10.1074/jbc. M110.127753
-
(2010)
J. Biol. Chem
, vol.285
, pp. 38173-38182
-
-
Hinault, M.P.1
Cuendet, A.F.2
Mattoo, R.U.3
Mensi, M.4
Dietler, G.5
Lashuel, H.A.6
-
36
-
-
64549097439
-
Guidelines for the nomenclature of the human heat shock proteins
-
Kampinga, H. H., Hageman, J., Vos, M. J., Kubota, H., Tanguay, R. M., Bruford, E. A., et al. (2009). Guidelines for the nomenclature of the human heat shock proteins. Cell Stress Chaperones 14, 105-111. doi: 10.1007/s12192-008-0068-7
-
(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
-
37
-
-
77952851112
-
Chaperone-assisted degradation: multiple paths to destruction
-
Kettern, N., Dreiseidler, M., Tawo, R., and Hohfeld, J. (2010). Chaperone-assisted degradation: multiple paths to destruction. Biol. Chem. 391, 481-489. doi: 10.1515/bc.2010.058
-
(2010)
Biol. Chem
, vol.391
, pp. 481-489
-
-
Kettern, N.1
Dreiseidler, M.2
Tawo, R.3
Hohfeld, J.4
-
38
-
-
77950562866
-
A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes
-
Koplin, A., Preissler, S., Ilina, Y., Koch, M., Scior, A., Erhardt, M., et al. (2010). A dual function for chaperones SSB-RAC and the NAC nascent polypeptide-associated complex on ribosomes. J. Cell Biol. 189, 57-68. doi: 10.1083/jcb.200910074
-
(2010)
J. Cell Biol
, vol.189
, pp. 57-68
-
-
Koplin, A.1
Preissler, S.2
Ilina, Y.3
Koch, M.4
Scior, A.5
Erhardt, M.6
-
39
-
-
0033545978
-
Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones
-
Laufen, T., Mayer, M. P., Beisel, C., Klostermeier, D., Mogk, A., Reinstein, J., et al. (1999). Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones. Proc. Natl. Acad. Sci. U.S.A. 96, 5452-5457. doi: 10.1073/pnas.96.10.5452
-
(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
-
40
-
-
0344500848
-
The archaeal molecular chaperone machine: peculiarities and paradoxes
-
Macario, A. J. L., and De Macario, E. C. (1999). The archaeal molecular chaperone machine: peculiarities and paradoxes. Genetics 152, 1277-1283
-
(1999)
Genetics
, vol.152
, pp. 1277-1283
-
-
Macario, A.J.L.1
De Macario, E.C.2
-
41
-
-
0030764015
-
Protein transport by purified yeast sec complex and Kar2p without membranes
-
Matlack, K. E. S., Plath, K., Misselwitz, B., and Rapoport, T. A. (1997). Protein transport by purified yeast sec complex and Kar2p without membranes. Science 277, 938-941. doi: 10.1126/science.277.5328.938
-
(1997)
Science
, vol.277
, pp. 938-941
-
-
Matlack, K.E.S.1
Plath, K.2
Misselwitz, B.3
Rapoport, T.A.4
-
42
-
-
84906096557
-
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins
-
Mattoo, R. H., and Goloubinoff, P. (2014). Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins. Cell. Mol. Life Sci. 71, 3311-3325. doi: 10.1007/s00018-014-1627-y
-
(2014)
Cell. Mol. Life Sci
, vol.71
, pp. 3311-3325
-
-
Mattoo, R.H.1
Goloubinoff, P.2
-
43
-
-
84880515581
-
Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates
-
Mattoo, R. U., Sharma, S. K., Priya, S., Finka, A., and Goloubinoff, P. (2013). Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J. Biol. Chem. 288, 21399-21411. doi: 10.1074/jbc. M113.479253
-
(2013)
J. Biol. Chem
, vol.288
, pp. 21399-21411
-
-
Mattoo, R.U.1
Sharma, S.K.2
Priya, S.3
Finka, A.4
Goloubinoff, P.5
-
44
-
-
85010847663
-
Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK
-
Mattoo, R. U. H., Farina Henriquez Cuendet, A., Sujatha, S., Finka, A., Priya, S., Sharma, S. K., et al. (2014). Synergism between a foldase and an unfoldase: reciprocal dependence between the thioredoxin-like activity of DnaJ and the polypeptide-unfolding activity of DnaK. Front. Mol. Biosci. 1:7. doi: 10.3389/fmolb.2014.00007
-
(2014)
Front. Mol. Biosci
, vol.1
, pp. 7
-
-
Mattoo, R.U.H.1
Farina Henriquez Cuendet, A.2
Sujatha, S.3
Finka, A.4
Priya, S.5
Sharma, S.K.6
-
45
-
-
84884589727
-
Hsp70 chaperone dynamics and molecular mechanism
-
Mayer, M. P. (2013). Hsp70 chaperone dynamics and molecular mechanism. Trends Biochem. Sci. 38, 507-514. doi: 10.1016/j.tibs.2013.08.001
-
(2013)
Trends Biochem. Sci
, vol.38
, pp. 507-514
-
-
Mayer, M.P.1
-
46
-
-
84930197013
-
Co-chaperones of the mammalian endoplasmic reticulum
-
Melnyk, A., Rieger, H., and Zimmermann, R. (2015). Co-chaperones of the mammalian endoplasmic reticulum. Subcell. Biochem. 78, 179-200. doi: 10.1007/978-3-319-11731-7_9
-
(2015)
Subcell. Biochem
, vol.78
, pp. 179-200
-
-
Melnyk, A.1
Rieger, H.2
Zimmermann, R.3
-
47
-
-
84877154316
-
A Role for an Hsp70 nucleotide exchange factor in the regulation of synaptic vesicle endocytosis
-
Morgan, J. R., Jiang, J. W., Oliphint, P. A., Jin, S. P., Gimenez, L. E., Busch, D. J., et al. (2013). A Role for an Hsp70 nucleotide exchange factor in the regulation of synaptic vesicle endocytosis. J. Neurosci. 33, 8009-8021. doi: 10.1523/JNEUROSCI.4505-12.2013
-
(2013)
J. Neurosci
, vol.33
, pp. 8009-8021
-
-
Morgan, J.R.1
Jiang, J.W.2
Oliphint, P.A.3
Jin, S.P.4
Gimenez, L.E.5
Busch, D.J.6
-
48
-
-
0027984270
-
Isolation of the stable hexameric DnaK. DnaJ complex from Thermus thermophilus
-
Motohashi, K., Taguchi, H., Ishii, N., and Yoshida, M. (1994). Isolation of the stable hexameric DnaK. DnaJ complex from Thermus thermophilus. J. Biol. Chem. 269, 27074-27079
-
(1994)
J. Biol. Chem
, vol.269
, pp. 27074-27079
-
-
Motohashi, K.1
Taguchi, H.2
Ishii, N.3
Yoshida, M.4
-
49
-
-
84875212796
-
Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates
-
Natalello, A., Mattoo, R. U. H., Priya, S., Sharma, S. K., Goloubinoff, P., and Doglia, S. M. (2013). Biophysical characterization of two different stable misfolded monomeric polypeptides that are chaperone-amenable substrates. J. Mol. Biol. 425, 1158-1171. doi: 10.1016/j.jmb.2012.12.025
-
(2013)
J. Mol. Biol
, vol.425
, pp. 1158-1171
-
-
Natalello, A.1
Mattoo, R.U.H.2
Priya, S.3
Sharma, S.K.4
Goloubinoff, P.5
Doglia, S.M.6
-
50
-
-
22544445528
-
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex
-
Otto, H., Conz, C., Maier, P., Wolfle, T., Suzuki, C. K., Jeno, P., et al. (2005). The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. Proc. Nat. Acad. Sci. U.S.A. 102, 10064-10069. doi: 10.1073/pnas.0504400102
-
(2005)
Proc. Nat. Acad. Sci. U.S.A
, vol.102
, pp. 10064-10069
-
-
Otto, H.1
Conz, C.2
Maier, P.3
Wolfle, T.4
Suzuki, C.K.5
Jeno, P.6
-
51
-
-
74249097474
-
Pharmacological targeting of the Hsp70 chaperone
-
Patury, S., Miyata, Y., and Gestwicki, J. E. (2009). Pharmacological targeting of the Hsp70 chaperone. Curr. Top. Med. Chem. 9, 1337-1351. doi: 10.2174/156802609789895674
-
(2009)
Curr. Top. Med. Chem
, vol.9
, pp. 1337-1351
-
-
Patury, S.1
Miyata, Y.2
Gestwicki, J.E.3
-
52
-
-
0032549525
-
Control of the DnaK chaperone cycle by substoichiometric concentrations of the co-chaperones DnaJ and GrpE
-
Pierpaoli, E. V., Sandmeier, E., Schonfeld, H. J., and Christen, P. (1998). Control of the DnaK chaperone cycle by substoichiometric concentrations of the co-chaperones DnaJ and GrpE. J. Biol. Chem. 273, 6643-6649. doi: 10.1074/jbc.273.12.6643
-
(1998)
J. Biol. Chem
, vol.273
, pp. 6643-6649
-
-
Pierpaoli, E.V.1
Sandmeier, E.2
Schonfeld, H.J.3
Christen, P.4
-
53
-
-
84878901297
-
Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides
-
Priya, S., Sharma, S. K., and Goloubinoff, P. (2013). Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides. FEBS Lett. 587, 1981-1987. doi: 10.1016/j.febslet.2013.05.014
-
(2013)
FEBS Lett
, vol.587
, pp. 1981-1987
-
-
Priya, S.1
Sharma, S.K.2
Goloubinoff, P.3
-
54
-
-
84868525116
-
Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
-
Rampelt, H., Kirstein-Miles, J., Nillegoda, N. B., Chi, K., Scholz, S. R., Morimoto, R. I., et al. (2012). Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. Embo J. 31, 4221-4235. doi: 10.1038/emboj.2012.264
-
(2012)
Embo J
, vol.31
, pp. 4221-4235
-
-
Rampelt, H.1
Kirstein-Miles, J.2
Nillegoda, N.B.3
Chi, K.4
Scholz, S.R.5
Morimoto, R.I.6
-
55
-
-
55249108963
-
Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones
-
Rodriguez, F., Arsene-Ploetze, F., Rist, W., Rudiger, S., Schneider-Mergener, J., Mayer, M. P., et al. (2008). Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones. Mol. Cell 32, 347-358. doi: 10.1016/j.molcel.2008.09.016
-
(2008)
Mol. Cell
, vol.32
, pp. 347-358
-
-
Rodriguez, F.1
Arsene-Ploetze, F.2
Rist, W.3
Rudiger, S.4
Schneider-Mergener, J.5
Mayer, M.P.6
-
56
-
-
0030976048
-
Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
-
Rudiger, S., Germeroth, L., Schneider-Mergener, J., and Bukau, B. (1997). Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16, 1501-1507. doi: 10.1093/emboj/16.7.1501
-
(1997)
EMBO J
, vol.16
, pp. 1501-1507
-
-
Rudiger, S.1
Germeroth, L.2
Schneider-Mergener, J.3
Bukau, B.4
-
57
-
-
0034397884
-
Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch
-
Rudiger, S., Mayer, M. P., Schneider-Mergener, J., and Bukau, B. (2000). Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch. J. Mol. Biol. 304, 245-251. doi: 10.1006/jmbi.2000.4193
-
(2000)
J. Mol. Biol
, vol.304
, pp. 245-251
-
-
Rudiger, S.1
Mayer, M.P.2
Schneider-Mergener, J.3
Bukau, B.4
-
58
-
-
84878873024
-
Targeting unfolded protein response signaling pathways to ameliorate protein misfolding diseases
-
Ryno, L. M., Wiseman, R. L., and Kelly, J. W. (2013). Targeting unfolded protein response signaling pathways to ameliorate protein misfolding diseases. Curr. Opin. Chem. Biol. 17, 346-352. doi: 10.1016/j.cbpa.2013.04.009
-
(2013)
Curr. Opin. Chem. Biol
, vol.17
, pp. 346-352
-
-
Ryno, L.M.1
Wiseman, R.L.2
Kelly, J.W.3
-
59
-
-
84867581392
-
Over-expression of HSP70 attenuates caspase-dependent and caspase-independent pathways and inhibits neuronal apoptosis
-
Sabirzhanov, B., Stoica, B. A., Hanscom, M., Piao, C. S., and Faden, A. I. (2012). Over-expression of HSP70 attenuates caspase-dependent and caspase-independent pathways and inhibits neuronal apoptosis. J. Neurochem. 123, 542-554. doi: 10.1111/j.1471-4159.2012.07927.x
-
(2012)
J. Neurochem
, vol.123
, pp. 542-554
-
-
Sabirzhanov, B.1
Stoica, B.A.2
Hanscom, M.3
Piao, C.S.4
Faden, A.I.5
-
60
-
-
34247589657
-
Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants
-
Saidi, Y., Domini, M., Choy, F., Zryd, J. P., Schwitzguebel, J. P., and Goloubinoff, P. (2007). Activation of the heat shock response in plants by chlorophenols: transgenic Physcomitrella patens as a sensitive biosensor for organic pollutants. Plant Cell Environ. 30, 753-763. doi: 10.1111/j.1365-3040.2007.01664.x
-
(2007)
Plant Cell Environ
, vol.30
, pp. 753-763
-
-
Saidi, Y.1
Domini, M.2
Choy, F.3
Zryd, J.P.4
Schwitzguebel, J.P.5
Goloubinoff, P.6
-
61
-
-
84926432180
-
A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein
-
Sarbeng, E. B., Liu, Q., Tian, X., Yang, J., Li, H., Wong, J. L., et al. (2015). A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein. J. Biol. Chem. 290, 8849-8862. doi: 10.1074/jbc. M114.596288
-
(2015)
J. Biol. Chem
, vol.290
, pp. 8849-8862
-
-
Sarbeng, E.B.1
Liu, Q.2
Tian, X.3
Yang, J.4
Li, H.5
Wong, J.L.6
-
62
-
-
0036263966
-
The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase
-
Schiene-Fischer, C., Habazettl, J., Schmid, F. X., and Fischer, G. (2002). The hsp70 chaperone DnaK is a secondary amide peptide bond cis-trans isomerase. Nat. Struct. Biol. 9, 419-424. doi: 10.1038/nsb804
-
(2002)
Nat. Struct. Biol
, vol.9
, pp. 419-424
-
-
Schiene-Fischer, C.1
Habazettl, J.2
Schmid, F.X.3
Fischer, G.4
-
63
-
-
84924914911
-
Sensitizing tumor cells to radiation by targeting the heat shock response
-
Schilling, D., Kuhnel, A., Konrad, S., Tetzlaff, F., Bayer, C., Yaglom, J., et al. (2015). Sensitizing tumor cells to radiation by targeting the heat shock response. Cancer Lett. 360, 294-301. doi: 10.1016/j.canlet.2015.02.033
-
(2015)
Cancer Lett
, vol.360
, pp. 294-301
-
-
Schilling, D.1
Kuhnel, A.2
Konrad, S.3
Tetzlaff, F.4
Bayer, C.5
Yaglom, J.6
-
64
-
-
79952364237
-
Mechanics of Hsp70 chaperones enables differential interaction with client proteins
-
Schlecht, R., Erbse, A. H., Bukau, B., and Mayer, M. P. (2011). Mechanics of Hsp70 chaperones enables differential interaction with client proteins. Nat. Struct. Mol. Biol. 18, 345-U135. doi: 10.1038/nsmb.2006
-
(2011)
Nat. Struct. Mol. Biol
, vol.18
, pp. 345-U135
-
-
Schlecht, R.1
Erbse, A.H.2
Bukau, B.3
Mayer, M.P.4
-
65
-
-
0030026850
-
Molecular chaperones are present in the thylakoid lumen of pea chloroplasts
-
Schlicher, T., and Soll, J. (1996). Molecular chaperones are present in the thylakoid lumen of pea chloroplasts. Febs Lett. 379, 302-304. doi: 10.1016/0014-5793(95)01534-5
-
(1996)
Febs Lett
, vol.379
, pp. 302-304
-
-
Schlicher, T.1
Soll, J.2
-
66
-
-
45849091944
-
Structure of the Hsp110: Hsc70 nucleotide exchange machine
-
Schuermann, J. P., Jiang, J. W., Cuellar, J., Llorca, O., Wang, L. P., Gimenez, L. E., et al. (2008). Structure of the Hsp110: Hsc70 nucleotide exchange machine. Mol. Cell 31, 232-243. doi: 10.1016/j.molcel.2008.05.006
-
(2008)
Mol. Cell
, vol.31
, pp. 232-243
-
-
Schuermann, J.P.1
Jiang, J.W.2
Cuellar, J.3
Llorca, O.4
Wang, L.P.5
Gimenez, L.E.6
-
67
-
-
84873442839
-
Widespread regulation of translation by elongation pausing in heat shock
-
Shalgi, R., Hurt, J. A., Krykbaeva, I., Taipale, M., Lindquist, S., and Burge, C. B. (2013). Widespread regulation of translation by elongation pausing in heat shock. Mol. Cell 49, 439-452. doi: 10.1016/j.molcel.2012.11.028
-
(2013)
Mol. Cell
, vol.49
, pp. 439-452
-
-
Shalgi, R.1
Hurt, J.A.2
Krykbaeva, I.3
Taipale, M.4
Lindquist, S.5
Burge, C.B.6
-
68
-
-
84902334317
-
Widespread inhibition of posttranscriptional splicing shapes the cellular transcriptome following heat shock
-
Shalgi, R., Hurt, J. A., Lindquist, S., and Burge, C. B. (2014). Widespread inhibition of posttranscriptional splicing shapes the cellular transcriptome following heat shock. Cell Rep. 7, 1362-1370. doi: 10.1016/j.celrep.2014.04.044
-
(2014)
Cell Rep
, vol.7
, pp. 1362-1370
-
-
Shalgi, R.1
Hurt, J.A.2
Lindquist, S.3
Burge, C.B.4
-
69
-
-
78649309029
-
The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase
-
Sharma, S. K., De Los Rios, P., Christen, P., Lustig, A., and Goloubinoff, P. (2010). The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase. Nat. Chem. Biol. 6, 914-920. doi: 10.1038/nchembio.455
-
(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
-
70
-
-
79955724860
-
Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate
-
Sharma, S. K., De Los Rios, P., and Goloubinoff, P. (2011). Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate. Proteins 79, 1991-1998. doi: 10.1002/prot.23024
-
(2011)
Proteins
, vol.79
, pp. 1991-1998
-
-
Sharma, S.K.1
De Los Rios, P.2
Goloubinoff, P.3
-
71
-
-
80052576118
-
The motors of protein import into chloroplasts
-
Shi, L. X., and Theg, S. M. (2011). The motors of protein import into chloroplasts. Plant Signal. Behav. 6, 1397-1401. doi: 10.4161/psb.6.9.16916
-
(2011)
Plant Signal. Behav
, vol.6
, pp. 1397-1401
-
-
Shi, L.X.1
Theg, S.M.2
-
72
-
-
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. doi: 10.1371/journal.pone.0026319
-
(2011)
PLoS ONE
, vol.6
-
-
Shorter, J.1
-
73
-
-
0036049850
-
The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?
-
Slepenkov, S. V., and Witt, S. N. (2002). The unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase? Mol. Microbiol. 45, 1197-1206. doi: 10.1046/j.1365-2958.2002.03093.x
-
(2002)
Mol. Microbiol
, vol.45
, pp. 1197-1206
-
-
Slepenkov, S.V.1
Witt, S.N.2
-
74
-
-
36349010951
-
The interplay between components of the mitochondrial protein translocation motor studied using purified components
-
Slutsky-Leiderman, O., Marom, M., Iosefson, O., Levy, R., Maoz, S., and Azem, A. (2007). The interplay between components of the mitochondrial protein translocation motor studied using purified components. J. Biol. Chem. 282, 33935-33942. doi: 10.1074/jbc. M704435200
-
(2007)
J. Biol. Chem
, vol.282
, pp. 33935-33942
-
-
Slutsky-Leiderman, O.1
Marom, M.2
Iosefson, O.3
Levy, R.4
Maoz, S.5
Azem, A.6
-
75
-
-
84871681173
-
A dancer caught midstep: the structure of ATP-bound Hsp70
-
Sousa, R. (2012). A dancer caught midstep: the structure of ATP-bound Hsp70. Mol. Cell 48, 821-823. doi: 10.1016/j.molcel.2012.12.008
-
(2012)
Mol. Cell
, vol.48
, pp. 821-823
-
-
Sousa, R.1
-
76
-
-
23344453615
-
Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues
-
Tytell, M. (2005). Release of heat shock proteins (Hsps) and the effects of extracellular Hsps on neural cells and tissues. Int. J. Hyperthermia 21, 445-455. doi: 10.1080/02656730500041921
-
(2005)
Int. J. Hyperthermia
, vol.21
, pp. 445-455
-
-
Tytell, M.1
-
77
-
-
84934440933
-
'Chaperone regulation of the heat shock protein response'
-
eds P. Csermely and L. Vígh, (New York, NY: Springer)
-
Voellmy, R., and Boellmann, F. (2007a). "Chaperone regulation of the heat shock protein response". in Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks, eds P. Csermely and L. Vígh, (New York, NY: Springer), 89-99
-
(2007)
Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks
, pp. 89-99
-
-
Voellmy, R.1
Boellmann, F.2
-
78
-
-
84934440933
-
Chaperone regulation of the heat shock protein response
-
Voellmy, R., and Boellmann, F. (2007b). Chaperone regulation of the heat shock protein response. Adv. Exp. Med. Biol. 594, 89-99. doi: 10.1007/978-0-387-39975-1_9
-
(2007)
Adv. Exp. Med. Biol
, vol.594
, pp. 89-99
-
-
Voellmy, R.1
Boellmann, F.2
-
79
-
-
84867750231
-
Loss of the DnaK-DnaJ-GrpE chaperone system among the Aquificales
-
Warnecke, T. (2012). Loss of the DnaK-DnaJ-GrpE chaperone system among the Aquificales. Mol. Biol. Evol. 29, 3485-3495. doi: 10.1093/molbev/mss152
-
(2012)
Mol. Biol. Evol
, vol.29
, pp. 3485-3495
-
-
Warnecke, T.1
-
80
-
-
34548292474
-
Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome
-
Weiss, Y. G., Bromberg, Z., Raj, N., Raphael, J., Goloubinoff. P., Ben-Neriah, Y., et al. (2007). Enhanced heat shock protein 70 expression alters proteasomal degradation of IkappaB kinase in experimental acute respiratory distress syndrome. Crit. Care Med. 35, 2128-2138. doi: 10.1097/01.CCM.0000278915.78030.74
-
(2007)
Crit. Care Med
, vol.35
, pp. 2128-2138
-
-
Weiss, Y.G.1
Bromberg, Z.2
Raj, N.3
Raphael, J.4
Goloubinoff, P.5
Ben-Neriah, Y.6
-
81
-
-
0031443640
-
The glyoxysomal and plastid molecular chaperones (70-kDa heat shock protein) of watermelon cotyledons are encoded by a single gene
-
Wimmer, B., Lottspeich, F., Vanderklei, I., Veenhuis, M., and Gietl, C. (1997). The glyoxysomal and plastid molecular chaperones (70-kDa heat shock protein) of watermelon cotyledons are encoded by a single gene. Proc. Natl. Acad. Sci. U.S.A. 94, 13624-13629. doi: 10.1073/pnas.94.25.13624
-
(1997)
Proc. Natl. Acad. Sci. U.S.A
, vol.94
, pp. 13624-13629
-
-
Wimmer, B.1
Lottspeich, F.2
Vanderklei, I.3
Veenhuis, M.4
Gietl, C.5
-
82
-
-
84864387363
-
Chaperone networks in protein disaggregation and prion propagation
-
Winkler, J., Tyedmers, J., Bukau, B., and Mogk, A. (2012). Chaperone networks in protein disaggregation and prion propagation. J. Struct. Biol. 179, 152-160. doi: 10.1016/j.jsb.2012.05.002
-
(2012)
J. Struct. Biol
, vol.179
, pp. 152-160
-
-
Winkler, J.1
Tyedmers, J.2
Bukau, B.3
Mogk, A.4
-
83
-
-
84927056252
-
Structural basis for interaction of a cotranslational chaperone with the eukaryotic ribosome
-
Zhang, Y., Ma, C., Yuan, Y., Zhu, J., Li, N., Chen, C., et al. (2014). Structural basis for interaction of a cotranslational chaperone with the eukaryotic ribosome. Nat. Struct. Mol. Biol. 21, 1042-1046. doi: 10.1038/nsmb.2908
-
(2014)
Nat. Struct. Mol. Biol
, vol.21
, pp. 1042-1046
-
-
Zhang, Y.1
Ma, C.2
Yuan, Y.3
Zhu, J.4
Li, N.5
Chen, C.6
-
84
-
-
78349308634
-
Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assembly
-
Zhuo, Y., Ilangovan, U., Schirf, V., Demeler, B., Sousa, R., Hinck, A. P., et al. (2010). Dynamic interactions between clathrin and locally structured elements in a disordered protein mediate clathrin lattice assembly. J. Mol. Biol. 404, 274-290. doi: 10.1016/j.jmb.2010.09.044
-
(2010)
J. Mol. Biol
, vol.404
, pp. 274-290
-
-
Zhuo, Y.1
Ilangovan, U.2
Schirf, V.3
Demeler, B.4
Sousa, R.5
Hinck, A.P.6
|