-
1
-
-
0242540367
-
Protein folding: Importance of the Anfinsen cage
-
Ellis RJ (2003) Protein folding: Importance of the Anfinsen cage. Curr Biol 13(22): R881-R883.
-
(2003)
Curr Biol
, vol.13
, Issue.22
-
-
Ellis, R.J.1
-
2
-
-
79551687316
-
Protein folding in the cell: Challenges and progress
-
Gershenson A, Gierasch LM (2011) Protein folding in the cell: Challenges and progress. Curr Opin Struct Biol 21(1):32-41.
-
(2011)
Curr Opin Struct Biol
, vol.21
, Issue.1
, pp. 32-41
-
-
Gershenson, A.1
Gierasch, L.M.2
-
3
-
-
0029992278
-
Molecular chaperones in cellular protein folding
-
Hartl FU (1996) Molecular chaperones in cellular protein folding. Nature 381(6583): 571-579.
-
(1996)
Nature
, vol.381
, Issue.6583
, pp. 571-579
-
-
Hartl, F.U.1
-
5
-
-
0034924812
-
Folding of newly translated proteins in vivo: The role of molecular chaperones
-
Frydman J (2001) Folding of newly translated proteins in vivo: The role of molecular chaperones. Annu Rev Biochem 70:603-647.
-
(2001)
Annu Rev Biochem
, vol.70
, pp. 603-647
-
-
Frydman, J.1
-
6
-
-
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(7356):324-332.
-
(2011)
Nature
, vol.475
, Issue.7356
, pp. 324-332
-
-
Hartl, F.U.1
Bracher, A.2
Hayer-Hartl, M.3
-
7
-
-
0036899202
-
The chaperonin folding machine
-
DOI 10.1016/S0968-0004(02)02211-9, PII S0968000402022119
-
Saibil HR, Ranson NA (2002) The chaperonin folding machine. Trends Biochem Sci 27 (12):627-632. (Pubitemid 35435312)
-
(2002)
Trends in Biochemical Sciences
, vol.27
, Issue.12
, pp. 627-632
-
-
Saibil, H.R.1
Ranson, N.A.2
-
8
-
-
58149229533
-
Chaperonin complex with a newly folded protein encapsulated in the folding chamber
-
Clare DK, Bakkes PJ, van Heerikhuizen H, van der Vies SM, Saibil HR (2009) Chaperonin complex with a newly folded protein encapsulated in the folding chamber. Nature 457(7225):107-110.
-
(2009)
Nature
, vol.457
, Issue.7225
, pp. 107-110
-
-
Clare, D.K.1
Bakkes, P.J.2
Van Heerikhuizen, H.3
Van Der Vies, S.M.4
Saibil, H.R.5
-
9
-
-
0030870719
-
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
-
DOI 10.1038/41944
-
Xu Z, Horwich AL, Sigler PB (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388(6644):741-750. (Pubitemid 27375147)
-
(1997)
Nature
, vol.388
, Issue.6644
, pp. 741-750
-
-
Xu, Z.1
Horwich, A.L.2
Sigler, P.B.3
-
10
-
-
77951974784
-
A systematic survey of in vivo obligate chaperonin-dependent substrates
-
Fujiwara K, Ishihama Y, Nakahigashi K, Soga T, Taguchi H (2010) A systematic survey of in vivo obligate chaperonin-dependent substrates. EMBO J 29(9):1552-1564.
-
(2010)
EMBO J
, vol.29
, Issue.9
, pp. 1552-1564
-
-
Fujiwara, K.1
Ishihama, Y.2
Nakahigashi, K.3
Soga, T.4
Taguchi, H.5
-
11
-
-
0033547324
-
Identification of in vivo substrates of the chaperonin GroEL
-
Houry WA, Frishman D, Eckerskorn C, Lottspeich F, Hartl FU (1999) Identification of in vivo substrates of the chaperonin GroEL. Nature 402(6758):147-154.
-
(1999)
Nature
, vol.402
, Issue.6758
, pp. 147-154
-
-
Houry, W.A.1
Frishman, D.2
Eckerskorn, C.3
Lottspeich, F.4
Hartl, F.U.5
-
12
-
-
22744447508
-
Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
-
DOI 10.1016/j.cell.2005.05.028, PII S0092867405005441
-
Kerner MJ, et al. (2005) Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122(2):209-220. (Pubitemid 41032985)
-
(2005)
Cell
, vol.122
, Issue.2
, pp. 209-220
-
-
Kerner, M.J.1
Naylor, D.J.2
Ishihama, Y.3
Maier, T.4
Chang, H.-C.5
Stines, A.P.6
Georgopoulos, C.7
Frishman, D.8
Hayer-Hartl, M.9
Mann, M.10
Hartl, F.U.11
-
13
-
-
0035913910
-
GroEL/GroES-mediated folding of a protein too large to be encapsulated
-
DOI 10.1016/S0092-8674(01)00523-2
-
Chaudhuri TK, Farr GW, Fenton WA, Rospert S, Horwich AL (2001) GroEL/GroES-mediated folding of a protein too large to be encapsulated. Cell 107(2):235-246. (Pubitemid 33035949)
-
(2001)
Cell
, vol.107
, Issue.2
, pp. 235-246
-
-
Chaudhuri, T.K.1
Farr, G.W.2
Fenton, W.A.3
Rospert, S.4
Horwich, A.L.5
-
14
-
-
0030844281
-
Recombination of protein domains facilitated by co-translational folding in eukaryotes
-
DOI 10.1038/41024
-
Netzer WJ, Hartl FU (1997) Recombination of protein domains facilitated by cotranslational folding in eukaryotes. Nature 388(6640):343-349. (Pubitemid 27334805)
-
(1997)
Nature
, vol.388
, Issue.6640
, pp. 343-349
-
-
Netzer, W.J.1
Hartl, F.U.2
-
15
-
-
34547830871
-
Different mechanistic requirements for prokaryotic and eukaryotic chaperonins: A lattice study
-
DOI 10.1093/bioinformatics/btm180
-
Jacob E, Horovitz A, Unger R (2007) Different mechanistic requirements for prokaryotic and eukaryotic chaperonins: a lattice study. Bioinformatics 23(13):i240-i248. (Pubitemid 47244406)
-
(2007)
Bioinformatics
, vol.23
, Issue.13
-
-
Jacob, E.1
Horovitz, A.2
Unger, R.3
-
16
-
-
0032005026
-
Protein folding in the cytosol: Chaperonin-dependent and -independent mechanisms
-
DOI 10.1016/S0968-0004(97)01171-7, PII S0968000497011717
-
Netzer WJ, Hartl FU (1998) Protein folding in the cytosol: Chaperonin-dependent and -independent mechanisms. Trends Biochem Sci 23(2):68-73. (Pubitemid 28085230)
-
(1998)
Trends in Biochemical Sciences
, vol.23
, Issue.2
, pp. 68-73
-
-
Netzer, W.J.1
Hartl, F.U.2
-
17
-
-
46949104585
-
The interaction network of the chaperonin CCT
-
DOI 10.1038/emboj.2008.108, PII EMBOJ2008108
-
Dekker C, et al. (2008) The interaction network of the chaperonin CCT. EMBO J 27(13):1827-1839. (Pubitemid 351960205)
-
(2008)
EMBO Journal
, vol.27
, Issue.13
, pp. 1827-1839
-
-
Dekker, C.1
Stirling, P.C.2
McCormack, E.A.3
Filmore, H.4
Paul, A.5
Brost, R.L.6
Costanzo, M.7
Boone, C.8
Leroux, M.R.9
Willison, K.R.10
-
18
-
-
57149098022
-
Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies
-
Yam AY, et al. (2008) Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies. Nat Struct Mol Biol 15 (12):1255-1262.
-
(2008)
Nat Struct Mol Biol
, vol.15
, Issue.12
, pp. 1255-1262
-
-
Yam, A.Y.1
-
19
-
-
77950456761
-
4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement
-
Cong Y, et al. (2010) 4.0-A resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement. Proc Natl Acad Sci USA 107(11):4967-4972.
-
(2010)
Proc Natl Acad Sci USA
, vol.107
, Issue.11
, pp. 4967-4972
-
-
Cong, Y.1
-
20
-
-
84856509221
-
Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
-
Cong Y, et al. (2012) Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle. EMBO J 31(3):720-730.
-
(2012)
EMBO J
, vol.31
, Issue.3
, pp. 720-730
-
-
Cong, Y.1
-
21
-
-
79961026866
-
The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins
-
Dekker C, et al. (2011) The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins. EMBO J 30(15):3078-3090.
-
(2011)
EMBO J
, vol.30
, Issue.15
, pp. 3078-3090
-
-
Dekker, C.1
-
22
-
-
84857385799
-
Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling
-
Kalisman N, Adams CM, Levitt M (2012) Subunit order of eukaryotic TRiC/CCT chaperonin by cross-linking, mass spectrometry, and combinatorial homology modeling. Proc Natl Acad Sci USA 109(8):2884-2889.
-
(2012)
Proc Natl Acad Sci USA
, vol.109
, Issue.8
, pp. 2884-2889
-
-
Kalisman, N.1
Adams, C.M.2
Levitt, M.3
-
23
-
-
84861102204
-
The molecular architecture of the eukaryotic chaperonin TRiC/CCT
-
Leitner A, et al. (2012) The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure 20(5):814-825.
-
(2012)
Structure
, vol.20
, Issue.5
, pp. 814-825
-
-
Leitner, A.1
-
24
-
-
0035783161
-
Gene duplication and the evolution of group II chaperonins: Implications for structure and function
-
Archibald JM, Blouin C, Doolittle WF (2001) Gene duplication and the evolution of group II chaperonins: implications for structure and function. J Struct Biol 135(2):157-169.
-
(2001)
J Struct Biol
, vol.135
, Issue.2
, pp. 157-169
-
-
Archibald, J.M.1
Blouin, C.2
Doolittle, W.F.3
-
25
-
-
77955282609
-
Equivalent mutations in the eight subunits of the chaperonin CCT produce dramatically different cellular and gene expression phenotypes
-
Amit M, et al. (2010) Equivalent mutations in the eight subunits of the chaperonin CCT produce dramatically different cellular and gene expression phenotypes. J Mol Biol 401(3):532-543.
-
(2010)
J Mol Biol
, vol.401
, Issue.3
, pp. 532-543
-
-
Amit, M.1
-
26
-
-
33749080319
-
Identification of the TRiC/CCT Substrate Binding Sites Uncovers the Function of Subunit Diversity in Eukaryotic Chaperonins
-
DOI 10.1016/j.molcel.2006.09.003, PII S1097276506006319
-
Spiess C, Miller EJ, McClellan AJ, Frydman J (2006) Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins. Mol Cell 24(1):25-37. (Pubitemid 44466686)
-
(2006)
Molecular Cell
, vol.24
, Issue.1
, pp. 25-37
-
-
Spiess, C.1
Miller, E.J.2
McClellan, A.J.3
Frydman, J.4
-
27
-
-
0027077442
-
Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits
-
Frydman J, et al. (1992) Function in protein folding of TRiC, a cytosolic ring complex containing TCP-1 and structurally related subunits. EMBO J 11(13):4767-4778. (Pubitemid 23023419)
-
(1992)
EMBO Journal
, vol.11
, Issue.13
, pp. 4767-4778
-
-
Frydman, J.1
Nimmesgern, E.2
Erdjument-Bromage, H.3
Wall, J.S.4
Tempst, P.5
Hartl, F.-U.6
-
28
-
-
0026776331
-
A cytoplasmic chaperonin that catalyzes beta-actin folding
-
Gao Y, Thomas JO, Chow RL, Lee GH, Cowan NJ (1992) A cytoplasmic chaperonin that catalyzes beta-actin folding. Cell 69(6):1043-1050.
-
(1992)
Cell
, vol.69
, Issue.6
, pp. 1043-1050
-
-
Gao, Y.1
Thomas, J.O.2
Chow, R.L.3
Lee, G.H.4
Cowan, N.J.5
-
29
-
-
7444231693
-
Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets
-
DOI 10.1016/j.tcb.2004.09.015, PII S0962892404002661
-
Spiess C, Meyer AS, Reissmann S, Frydman J (2004) Mechanism of the eukaryotic chaperonin: Protein folding in the chamber of secrets. Trends Cell Biol 14(11):598-604. (Pubitemid 39440608)
-
(2004)
Trends in Cell Biology
, vol.14
, Issue.11
, pp. 598-604
-
-
Spiess, C.1
Meyer, A.S.2
Reissmann, S.3
Frydman, J.4
-
30
-
-
0026650749
-
TCP1 complex is a molecular chaperone in tubulin biogenesis
-
Yaffe MB, et al. (1992) TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 358(6383):245-248.
-
(1992)
Nature
, vol.358
, Issue.6383
, pp. 245-248
-
-
Yaffe, M.B.1
-
31
-
-
70450219488
-
Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei
-
Hirtreiter AM, et al. (2009) Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei. Mol Microbiol 74(5):1152-1168.
-
(2009)
Mol Microbiol
, vol.74
, Issue.5
, pp. 1152-1168
-
-
Hirtreiter, A.M.1
-
32
-
-
46449109112
-
Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT
-
DOI 10.1038/nsmb.1436, PII NSMB1436
-
Booth CR, et al. (2008) Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT. Nat Struct Mol Biol 15(7):746-753. (Pubitemid 351931999)
-
(2008)
Nature Structural and Molecular Biology
, vol.15
, Issue.7
, pp. 746-753
-
-
Booth, C.R.1
Meyer, A.S.2
Cong, Y.3
Topf, M.4
Sali, A.5
Ludtke, S.J.6
Chiu, W.7
Frydman, J.8
-
33
-
-
0038737003
-
Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis
-
DOI 10.1016/S0092-8674(03)00307-6
-
Meyer AS, et al. (2003) Closing the folding chamber of the eukaryotic chaperonin requires the transition state of ATP hydrolysis. Cell 113(3):369-381. (Pubitemid 36556118)
-
(2003)
Cell
, vol.113
, Issue.3
, pp. 369-381
-
-
Meyer, A.S.1
Gillespie, J.R.2
Walther, D.3
Millet, I.S.4
Doniach, S.5
Frydman, J.6
-
34
-
-
78650980445
-
Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin
-
Muñoz IG, et al. (2011) Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin. Nat Struct Mol Biol 18(1):14-19.
-
(2011)
Nat Struct Mol Biol
, vol.18
, Issue.1
, pp. 14-19
-
-
Muñoz, I.G.1
-
35
-
-
17844378217
-
Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis
-
DOI 10.1038/nsmb901
-
Rivenzon-Segal D, Wolf SG, Shimon L, Willison KR, Horovitz A (2005) Sequential ATP-induced allosteric transitions of the cytoplasmic chaperonin containing TCP-1 revealed by EM analysis. Nat Struct Mol Biol 12(3):233-237. (Pubitemid 43079364)
-
(2005)
Nature Structural and Molecular Biology
, vol.12
, Issue.3
, pp. 233-237
-
-
Rivenzon-Segal, D.1
Wolf, S.G.2
Shimon, L.3
Willison, K.R.4
Horovitz, A.5
-
36
-
-
40049109706
-
ATP-induced allostery in the eukaryotic chaperonin CCT is abolished by the mutation G345D in CCT4 that renders yeast temperature-sensitive for growth
-
Shimon L, Hynes GM, McCormack EA, Willison KR, Horovitz A (2008) ATP-induced allostery in the eukaryotic chaperonin CCT is abolished by the mutation G345D in CCT4 that renders yeast temperature-sensitive for growth. J Mol Biol 377(2):469-477.
-
(2008)
J Mol Biol
, vol.377
, Issue.2
, pp. 469-477
-
-
Shimon, L.1
Hynes, G.M.2
McCormack, E.A.3
Willison, K.R.4
Horovitz, A.5
-
37
-
-
34247635168
-
Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins
-
DOI 10.1038/nsmb1236, PII NSMB1236
-
Reissmann S, Parnot C, Booth CR, Chiu W, Frydman J (2007) Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins. Nat Struct Mol Biol 14(5):432-440. (Pubitemid 46685886)
-
(2007)
Nature Structural and Molecular Biology
, vol.14
, Issue.5
, pp. 432-440
-
-
Reissmann, S.1
Parnot, C.2
Booth, C.R.3
Chiu, W.4
Frydman, J.5
-
38
-
-
0028586011
-
Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo
-
Chen X, Sullivan DS, Huffaker TC (1994) Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo. Proc Natl Acad Sci USA 91(19):9111-9115.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, Issue.19
, pp. 9111-9115
-
-
Chen, X.1
Sullivan, D.S.2
Huffaker, T.C.3
-
39
-
-
26844472785
-
Efficient production of native actin upon translation in a bacterial lysate supplemented with the eukaryotic chaperonin TRiC
-
DOI 10.1515/BC.2005.088
-
Stemp MJ, Guha S, Hartl FU, Barral JM (2005) Efficient production of native actin upon translation in a bacterial lysate supplemented with the eukaryotic chaperonin TRiC. Biol Chem 386(8):753-757. (Pubitemid 41448156)
-
(2005)
Biological Chemistry
, vol.386
, Issue.8
, pp. 753-757
-
-
Stemp, M.J.1
Guha, S.2
Hartl, F.U.3
Barral, J.M.4
-
40
-
-
0028587244
-
A yeast TCP-1-like protein is required for actin function in vivo
-
Vinh DB, Drubin DG (1994) A yeast TCP-1-like protein is required for actin function in vivo. Proc Natl Acad Sci USA 91(19):9116-9120.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, Issue.19
, pp. 9116-9120
-
-
Vinh, D.B.1
Drubin, D.G.2
-
41
-
-
0024988340
-
Atomic structure of the actin:DNase I complex
-
Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC (1990) Atomic structure of the actin:DNase I complex. Nature 347(6288):37-44.
-
(1990)
Nature
, vol.347
, Issue.6288
, pp. 37-44
-
-
Kabsch, W.1
Mannherz, H.G.2
Suck, D.3
Pai, E.F.4
Holmes, K.C.5
-
42
-
-
0016361516
-
Actin is the naturally occurring inhibitor of deoxyribonuclease I
-
Lazarides E, Lindberg U (1974) Actin is the naturally occurring inhibitor of deoxyribonuclease I. Proc Natl Acad Sci USA 71(12):4742-4746.
-
(1974)
Proc Natl Acad Sci USA
, vol.71
, Issue.12
, pp. 4742-4746
-
-
Lazarides, E.1
Lindberg, U.2
-
43
-
-
0032733718
-
Effect of self-association on the structural organization of partially folded proteins: Inactivated actin
-
Kuznetsova IM, et al. (1999) Effect of self-association on the structural organization of partially folded proteins: Inactivated actin. Biophys J 77(5):2788-2800. (Pubitemid 29519522)
-
(1999)
Biophysical Journal
, vol.77
, Issue.5
, pp. 2788-2800
-
-
Kuznetsova, I.M.1
Biktashev, A.G.2
Khaitlina, S.Yu.3
Vassilenko, K.S.4
Turoverov, K.K.5
Uversky, V.N.6
-
44
-
-
0035783276
-
Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT
-
McCormack EA, Llorca O, Carrascosa JL, Valpuesta JM, Willison KR (2001) Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT. J Struct Biol 135(2):198-204.
-
(2001)
J Struct Biol
, vol.135
, Issue.2
, pp. 198-204
-
-
McCormack, E.A.1
Llorca, O.2
Carrascosa, J.L.3
Valpuesta, J.M.4
Willison, K.R.5
-
47
-
-
0032078861
-
Rapid actin-based plasticity in dendritic spines
-
DOI 10.1016/S0896-6273(00)80467-5
-
Fischer M, Kaech S, Knutti D, Matus A (1998) Rapid actin-based plasticity in dendritic spines. Neuron 20(5):847-854. (Pubitemid 28247391)
-
(1998)
Neuron
, vol.20
, Issue.5
, pp. 847-854
-
-
Fischer, M.1
Kaech, S.2
Knutti, D.3
Matus, A.4
-
48
-
-
0028944687
-
The actin fold
-
Kabsch W, Holmes KC (1995) The actin fold. FASEB J 9(2):167-174.
-
(1995)
FASEB J
, vol.9
, Issue.2
, pp. 167-174
-
-
Kabsch, W.1
Holmes, K.C.2
-
49
-
-
84863141713
-
Exploring the role of topological frustration in actin refolding with molecular simulations
-
Lee JY, Duan L, Iverson TM, Dima RI (2012) Exploring the role of topological frustration in actin refolding with molecular simulations. J Phys Chem B 116(5):1677-1686.
-
(2012)
J Phys Chem B
, vol.116
, Issue.5
, pp. 1677-1686
-
-
Lee, J.Y.1
Duan, L.2
Iverson, T.M.3
Dima, R.I.4
-
50
-
-
28844496012
-
Actin interacts with CCT via discrete binding sites: A binding transition-release model for CCT-mediated actin folding
-
DOI 10.1016/j.jmb.2005.10.051, PII S0022283605012982
-
Neirynck K, Waterschoot D, Vandekerckhove J, Ampe C, Rommelaere H (2006) Actin interacts with CCT via discrete binding sites: A binding transition-release model for CCT-mediated actin folding. J Mol Biol 355(1):124-138. (Pubitemid 41774144)
-
(2006)
Journal of Molecular Biology
, vol.355
, Issue.1
, pp. 124-138
-
-
Neirynck, K.1
Waterschoot, D.2
Vandekerckhove, J.3
Ampe, C.4
Rommelaere, H.5
-
51
-
-
0037062473
-
Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex
-
DOI 10.1073/pnas.112075699
-
McLaughlin JN, et al. (2002) Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex. Proc Natl Acad Sci USA 99(12):7962-7967. (Pubitemid 34650988)
-
(2002)
Proceedings of the National Academy of Sciences of the United States of America
, vol.99
, Issue.12
, pp. 7962-7967
-
-
McLaughlin, J.N.1
Thulin, C.D.2
Hart, S.J.3
Resing, K.A.4
Ahn, N.G.5
Willardson, B.M.6
-
52
-
-
0028196813
-
Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
-
Melki R, Cowan NJ (1994) Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates. Mol Cell Biol 14(5):2895-2904.
-
(1994)
Mol Cell Biol
, vol.14
, Issue.5
, pp. 2895-2904
-
-
Melki, R.1
Cowan, N.J.2
-
53
-
-
0031825279
-
MgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains
-
Szpikowska BK, Swiderek KM, Sherman MA, Mas MT (1998) MgATP binding to the nucleotide-binding domains of the eukaryotic cytoplasmic chaperonin induces conformational changes in the putative substrate-binding domains. Protein Sci 7(7):1524-1530. (Pubitemid 28331271)
-
(1998)
Protein Science
, vol.7
, Issue.7
, pp. 1524-1530
-
-
Szpikowska, B.K.1
Swiderek, K.M.2
Sherman, M.A.3
Mas, M.T.4
-
54
-
-
0029980091
-
Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
-
Frydman J, Hartl FU (1996) Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms. Science 272(5267):1497-1502. (Pubitemid 26200004)
-
(1996)
Science
, vol.272
, Issue.5267
, pp. 1497-1502
-
-
Frydman, J.1
Hartl, F.U.2
-
55
-
-
0030976931
-
An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2
-
DOI 10.1093/emboj/16.13.4092
-
Fabrizio P, Laggerbauer B, Lauber J, Lane WS, Lührmann R (1997) An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2. EMBO J 16(13):4092-4106. (Pubitemid 27281024)
-
(1997)
EMBO Journal
, vol.16
, Issue.13
, pp. 4092-4106
-
-
Fabrizio, P.1
Laggerbauer, B.2
Lauber, J.3
Lane, W.S.4
Luhrmann, R.5
-
56
-
-
0242516080
-
Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase
-
DOI 10.1038/nsb923
-
Jørgensen R, et al. (2003) Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase. Nat Struct Biol 10(5):379-385. (Pubitemid 36523273)
-
(2003)
Nature Structural Biology
, vol.10
, Issue.5
, pp. 379-385
-
-
Jorgensen, R.1
Ortiz, P.A.2
Carr-Schmid, A.3
Nissen, P.4
Kinzy, T.G.5
Andersen, G.R.6
-
57
-
-
28644437048
-
The importance of sequence diversity in the aggregation and evolution of proteins
-
DOI 10.1038/nature04195
-
Wright CF, Teichmann SA, Clarke J, Dobson CM (2005) The importance of sequence diversity in the aggregation and evolution of proteins. Nature 438(7069):878-881. (Pubitemid 41753072)
-
(2005)
Nature
, vol.438
, Issue.7069
, pp. 878-881
-
-
Wright, C.F.1
Teichmann, S.A.2
Clarke, J.3
Dobson, C.M.4
-
58
-
-
0032983520
-
Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase
-
DOI 10.1038/10754
-
Frydman J, Erdjument-Bromage H, Tempst P, Hartl FU (1999) Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase. Nat Struct Biol 6(7):697-705. (Pubitemid 29318962)
-
(1999)
Nature Structural Biology
, vol.6
, Issue.7
, pp. 697-705
-
-
Frydman, J.1
Erdjument-Bromage, H.2
Tempst, P.3
Ulrich, H.F.4
-
59
-
-
0028361309
-
Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
-
DOI 10.1038/370111a0
-
Frydman J, Nimmesgern E, Ohtsuka K, Hartl FU (1994) Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature 370 (6485):111-117. (Pubitemid 24229115)
-
(1994)
Nature
, vol.370
, Issue.6485
, pp. 111-117
-
-
Frydman, J.1
Nimmesgern, E.2
Ohtsuka, K.3
Hartl, F.U.4
-
60
-
-
23044445800
-
The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking
-
DOI 10.1074/jbc.M504110200
-
Etchells SA, et al. (2005) The cotranslational contacts between ribosome-bound nascent polypeptides and the subunits of the hetero-oligomeric chaperonin TRiC probed by photocross-linking. J Biol Chem 280(30):28118-28126. (Pubitemid 41076930)
-
(2005)
Journal of Biological Chemistry
, vol.280
, Issue.30
, pp. 28118-28126
-
-
Etchells, S.A.1
Meyer, A.S.2
Yam, A.Y.3
Roobol, A.4
Miao, Y.5
Shao, Y.6
Carden, M.J.7
Skach, W.R.8
Frydman, J.9
Johnson, A.E.10
-
61
-
-
75149145980
-
Mechanism of folding chamber closure in a group II chaperonin
-
Zhang J, et al. (2010) Mechanism of folding chamber closure in a group II chaperonin. Nature 463(7279):379-383.
-
(2010)
Nature
, vol.463
, Issue.7279
, pp. 379-383
-
-
Zhang, J.1
-
62
-
-
79955798700
-
Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure
-
Zhang J, et al. (2011) Cryo-EM structure of a group II chaperonin in the prehydrolysis ATP-bound state leading to lid closure. Structure 19(5):633-639.
-
(2011)
Structure
, vol.19
, Issue.5
, pp. 633-639
-
-
Zhang, J.1
-
63
-
-
0030930753
-
The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex
-
DOI 10.1073/pnas.94.20.10780
-
Lin P, Sherman F (1997) The unique hetero-oligomeric nature of the subunits in the catalytic cooperativity of the yeast Cct chaperonin complex. Proc Natl Acad Sci USA 94(20):10780-10785. (Pubitemid 27430811)
-
(1997)
Proceedings of the National Academy of Sciences of the United States of America
, vol.94
, Issue.20
, pp. 10780-10785
-
-
Lin, P.1
Sherman, F.2
-
64
-
-
84868137417
-
A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle
-
Reissmann S, et al. (2012) A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle. Cell Rep 2(4):866-877.
-
(2012)
Cell Rep
, vol.2
, Issue.4
, pp. 866-877
-
-
Reissmann, S.1
-
65
-
-
33748561495
-
Chaperonin TRiC Promotes the Assembly of polyQ Expansion Proteins into Nontoxic Oligomers
-
DOI 10.1016/j.molcel.2006.08.017, PII S1097276506005983
-
Behrends C, et al. (2006) Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol Cell 23(6):887-897. (Pubitemid 44363048)
-
(2006)
Molecular Cell
, vol.23
, Issue.6
, pp. 887-897
-
-
Behrends, C.1
Langer, C.A.2
Boteva, R.3
Bottcher, U.M.4
Stemp, M.J.5
Schaffar, G.6
Rao, B.V.7
Giese, A.8
Kretzschmar, H.9
Siegers, K.10
Hartl, F.U.11
-
66
-
-
33749176269
-
Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state
-
DOI 10.1038/ncb1478, PII NCB1478
-
Kitamura A, et al. (2006) Cytosolic chaperonin prevents polyglutamine toxicity with altering the aggregation state. Nat Cell Biol 8(10):1163-1170. (Pubitemid 44473613)
-
(2006)
Nature Cell Biology
, vol.8
, Issue.10
, pp. 1163-1170
-
-
Kitamura, A.1
Kubota, H.2
Pack, C.-G.3
Matsumoto, G.4
Hirayama, S.5
Takahashi, Y.6
Kimura, H.7
Kinjo, M.8
Morimoto, R.I.9
Nagata, K.10
-
67
-
-
33749177252
-
The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions
-
DOI 10.1038/ncb1477, PII NCB1477
-
Tam S, Geller R, Spiess C, Frydman J (2006) The chaperonin TRiC controls polyglutamine aggregation and toxicity through subunit-specific interactions. Nat Cell Biol 8(10):1155-1162. (Pubitemid 44473612)
-
(2006)
Nature Cell Biology
, vol.8
, Issue.10
, pp. 1155-1162
-
-
Tam, S.1
Geller, R.2
Spiess, C.3
Frydman, J.4
-
68
-
-
49449105092
-
The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin
-
Cuéllar J, et al. (2008) The structure of CCT-Hsc70 NBD suggests a mechanism for Hsp70 delivery of substrates to the chaperonin. Nat Struct Mol Biol 15(8):858-864.
-
(2008)
Nat Struct Mol Biol
, vol.15
, Issue.8
, pp. 858-864
-
-
Cuéllar, J.1
-
69
-
-
58149193233
-
The SWISS-MODEL Repository and associated resources
-
Kiefer F, Arnold K, Künzli M, Bordoli L, Schwede T (2009) The SWISS-MODEL Repository and associated resources. Nucleic Acids Res 37(Database issue):D387-D392.
-
(2009)
Nucleic Acids Res
, vol.37
, Issue.DATABASE ISSUE
-
-
Kiefer, F.1
Arnold, K.2
Künzli, M.3
Bordoli, L.4
Schwede, T.5
-
70
-
-
66849109240
-
The ribosome as a platform for cotranslational processing, folding and targeting of newly synthesized proteins
-
Kramer G, Boehringer D, Ban N, Bukau B (2009) The ribosome as a platform for cotranslational processing, folding and targeting of newly synthesized proteins. Nat Struct Mol Biol 16(6):589-597.
-
(2009)
Nat Struct Mol Biol
, vol.16
, Issue.6
, pp. 589-597
-
-
Kramer, G.1
Boehringer, D.2
Ban, N.3
Bukau, B.4
|