-
1
-
-
0015859467
-
Principles that govern the folding of protein chains
-
Anfinsen CB (1973) Principles that govern the folding of protein chains. Science 181: 223-230
-
(1973)
Science
, vol.181
, pp. 223-230
-
-
Anfinsen, C.B.1
-
2
-
-
0031436142
-
Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction
-
Aoki K, Taguchi H, Shindo Y, Yoshida M, Ogasahara K, Yutani K, Tanaka N (1997) Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction. J Biol Chem 272: 32158-32162
-
(1997)
J Biol Chem
, vol.272
, pp. 32158-32162
-
-
Aoki, K.1
Taguchi, H.2
Shindo, Y.3
Yoshida, M.4
Ogasahara, K.5
Yutani, K.6
Tanaka, N.7
-
3
-
-
31544450286
-
Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: The Keio collection
-
Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006) Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection. Mol Syst Biol 2: 2006.0008
-
(2006)
Mol Syst Biol
, vol.2
, pp. 20060008
-
-
Baba, T.1
Ara, T.2
Hasegawa, M.3
Takai, Y.4
Okumura, Y.5
Baba, M.6
Datsenko, K.A.7
Tomita, M.8
Wanner, B.L.9
Mori, H.10
-
4
-
-
0035913902
-
Dual function of protein confinement in chaperonin-assisted protein folding
-
Brinker A, Pfeifer G, Kerner MJ, Naylor DJ, Hartl FU, Hayer-Hartl M (2001) Dual function of protein confinement in chaperonin-assisted protein folding. Cell 107: 223-233
-
(2001)
Cell
, vol.107
, pp. 223-233
-
-
Brinker, A.1
Pfeifer, G.2
Kerner, M.J.3
Naylor, D.J.4
Hartl, F.U.5
Hayer-Hartl, M.6
-
5
-
-
33750489742
-
Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL
-
Chapman E, Farr GW, Usaite R, Furtak K, Fenton WA, Chaudhuri TK, Hondorp ER, Matthews RG, Wolf SG, Yates JR, Pypaert M, Horwich AL (2006) Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Proc Natl Acad Sci USA 103: 15800-15805
-
(2006)
Proc Natl Acad Sci USA
, vol.103
, pp. 15800-15805
-
-
Chapman, E.1
Farr, G.W.2
Usaite, R.3
Furtak, K.4
Fenton, W.A.5
Chaudhuri, T.K.6
Hondorp, E.R.7
Matthews, R.G.8
Wolf, S.G.9
Yates, J.R.10
Pypaert, M.11
Horwich, A.L.12
-
6
-
-
33845985292
-
Discovery of a new prokaryotic type i GTP cyclohydrolase family
-
El Yacoubi B, Bonnett S, Anderson JN, Swairjo MA, Iwata-Reuyl D, de Crecy-Lagard V (2006) Discovery of a new prokaryotic type I GTP cyclohydrolase family. J Biol Chem 281: 37586-37593
-
(2006)
J Biol Chem
, vol.281
, pp. 37586-37593
-
-
El Yacoubi, B.1
Bonnett, S.2
Anderson, J.N.3
Swairjo, M.A.4
Iwata-Reuyl, D.5
De Crecy-Lagard, V.6
-
7
-
-
0030750584
-
In vivo observation of polypeptide flux through the bacterial chaperonin system
-
Ewalt KL, Hendrick JP, Houry WA, Hartl FU (1997) In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 90: 491-500
-
(1997)
Cell
, vol.90
, pp. 491-500
-
-
Ewalt, K.L.1
Hendrick, J.P.2
Houry, W.A.3
Hartl, F.U.4
-
8
-
-
0037161813
-
Endosymbiotic bacteria: GroEL buffers against deleterious mutations
-
Fares MA, Ruiz-Gonzalez MX, Moya A, Elena SF, Barrio E (2002) Endosymbiotic bacteria: groEL buffers against deleterious mutations. Nature 417: 398
-
(2002)
Nature
, vol.417
, pp. 398
-
-
Fares, M.A.1
Ruiz-Gonzalez, M.X.2
Moya, A.3
Elena, S.F.4
Barrio, E.5
-
9
-
-
0024554107
-
The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures
-
Fayet O, Ziegelhoffer T, Georgopoulos C (1989) The groES and groEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures. J Bacteriol 171: 1379-1385
-
(1989)
J Bacteriol
, vol.171
, pp. 1379-1385
-
-
Fayet, O.1
Ziegelhoffer, T.2
Georgopoulos, C.3
-
10
-
-
0344738987
-
Chaperonin-mediated protein folding: Fate of substrate polypeptide
-
Fenton WA, Horwich AL (2003) Chaperonin-mediated protein folding: fate of substrate polypeptide. Q Rev Biophys 36: 229-256
-
(2003)
Q Rev Biophys
, vol.36
, pp. 229-256
-
-
Fenton, W.A.1
Horwich, A.L.2
-
11
-
-
34547743871
-
Filamentous morphology in GroE-depleted Escherichia coli induced by impaired folding of FtsE
-
Fujiwara K, Taguchi H (2007) Filamentous morphology in GroE-depleted Escherichia coli induced by impaired folding of FtsE. J Bacteriol 189: 5860-5866
-
(2007)
J Bacteriol
, vol.189
, pp. 5860-5866
-
-
Fujiwara, K.1
Taguchi, H.2
-
12
-
-
0034641917
-
The complete sequence of the mucosal pathogen Ureaplasma urealyticum
-
Glass JI, Lefkowitz EJ, Glass JS, Heiner CR, Chen EY, Cassell GH (2000) The complete sequence of the mucosal pathogen Ureaplasma urealyticum. Nature 407: 757-762
-
(2000)
Nature
, vol.407
, pp. 757-762
-
-
Glass, J.I.1
Lefkowitz, E.J.2
Glass, J.S.3
Heiner, C.R.4
Chen, E.Y.5
Cassell, G.H.6
-
13
-
-
0037040541
-
Molecular chaperones in the cytosol: From nascent chain to folded protein
-
Hartl FU, Hayer-Hartl M (2002) Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295: 1852-1858
-
(2002)
Science
, vol.295
, pp. 1852-1858
-
-
Hartl, F.U.1
Hayer-Hartl, M.2
-
14
-
-
66849143696
-
Converging concepts of protein folding in vitro and in vivo
-
Hartl FU, Hayer-Hartl M (2009) Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 16: 574-581
-
(2009)
Nat Struct Mol Biol
, vol.16
, pp. 574-581
-
-
Hartl, F.U.1
Hayer-Hartl, M.2
-
15
-
-
0027214204
-
Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
-
Horwich AL, Low KB, Fenton WA, Hirshfield IN, Furtak K (1993) Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 74: 909-917
-
(1993)
Cell
, vol.74
, pp. 909-917
-
-
Horwich, A.L.1
Low, K.B.2
Fenton, W.A.3
Hirshfield, I.N.4
Furtak, K.5
-
16
-
-
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: 147-154
-
(1999)
Nature
, vol.402
, pp. 147-154
-
-
Houry, W.A.1
Frishman, D.2
Eckerskorn, C.3
Lottspeich, F.4
Hartl, F.U.5
-
17
-
-
26844559000
-
Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
-
Ishihama Y, Oda Y, Tabata T, Sato T, Nagasu T, Rappsilber J, Mann M (2005) Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 4: 1265-1272
-
(2005)
Mol Cell Proteomics
, vol.4
, pp. 1265-1272
-
-
Ishihama, Y.1
Oda, Y.2
Tabata, T.3
Sato, T.4
Nagasu, T.5
Rappsilber, J.6
Mann, M.7
-
18
-
-
42049108914
-
Protein abundance profiling of the Escherichia coli cytosol
-
Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9: 102
-
(2008)
BMC Genomics
, vol.9
, pp. 102
-
-
Ishihama, Y.1
Schmidt, T.2
Rappsilber, J.3
Mann, M.4
Hartl, F.U.5
Kerner, M.J.6
Frishman, D.7
-
19
-
-
34247612307
-
Multiple high-throughput analyses monitor the response of E. coli to perturbations
-
Ishii N, Nakahigashi K, Baba T, Robert M, Soga T, Kanai A, Hirasawa T, Naba M, Hirai K, Hoque A, Ho PY, Kakazu Y, Sugawara K, Igarashi S, Harada S, Masuda T, Sugiyama N, Togashi T, Hasegawa M, Takai Y et al (2007) Multiple high-throughput analyses monitor the response of E. coli to perturbations. Science 316: 593-597
-
(2007)
Science
, vol.316
, pp. 593-597
-
-
Ishii, N.1
Nakahigashi, K.2
Baba, T.3
Robert, M.4
Soga, T.5
Kanai, A.6
Hirasawa, T.7
Naba, M.8
Hirai, K.9
Hoque, A.10
Ho, P.Y.11
Kakazu, Y.12
Sugawara, K.13
Igarashi, S.14
Harada, S.15
Masuda, T.16
Sugiyama, N.17
Togashi, T.18
Hasegawa, M.19
Takai, Y.20
more..
-
20
-
-
67049110207
-
Chemical cleavage-assisted tryptic digestion for membrane proteome analysis
-
Iwasaki M, Masuda T, Tomita M, Ishihama Y (2009) Chemical cleavage-assisted tryptic digestion for membrane proteome analysis. J Proteome Res 8: 3169-3175
-
(2009)
J Proteome Res
, vol.8
, pp. 3169-3175
-
-
Iwasaki, M.1
Masuda, T.2
Tomita, M.3
Ishihama, Y.4
-
21
-
-
0022569969
-
A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene
-
Jenkins AJ, March JB, Oliver IR, Masters M (1986) A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene. Mol Gen Genet 202: 446-454
-
(1986)
Mol Gen Genet
, vol.202
, pp. 446-454
-
-
Jenkins, A.J.1
March, J.B.2
Oliver, I.R.3
Masters, M.4
-
22
-
-
73849149481
-
Reconciling theories of chaperonin accelerated folding with experimental evidence
-
Jewett AI, Shea JE (2010) Reconciling theories of chaperonin accelerated folding with experimental evidence. Cell Mol Life Sci 67: 255-276
-
(2010)
Cell Mol Life Sci
, vol.67
, pp. 255-276
-
-
Jewett, A.I.1
Shea, J.E.2
-
23
-
-
22744447508
-
Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli
-
Kerner MJ, Naylor DJ, Ishihama Y, Maier T, Chang HC, Stines AP, Georgopoulos C, Frishman D, Hayer-Hartl M, Mann M, Hartl FU (2005) Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell 122: 209-220
-
(2005)
Cell
, vol.122
, 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
-
24
-
-
33644868758
-
Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL
-
Koike-Takeshita A, Shimamura T, Yokoyama K, Yoshida M, Taguchi H (2006) Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL. J Biol Chem 281: 962-967
-
(2006)
J Biol Chem
, vol.281
, pp. 962-967
-
-
Koike-Takeshita, A.1
Shimamura, T.2
Yokoyama, K.3
Yoshida, M.4
Taguchi, H.5
-
25
-
-
0020475449
-
A simple method for displaying the hydropathic character of a protein
-
Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157: 105-132
-
(1982)
J Mol Biol
, vol.157
, pp. 105-132
-
-
Kyte, J.1
Doolittle, R.F.2
-
26
-
-
67349171092
-
Protein folding in Escherichia coli: The chaperonin GroE and its substrates
-
Masters M, Blakely G, Coulson A, McLennan N, Yerko V, Acord J (2009) Protein folding in Escherichia coli: the chaperonin GroE and its substrates. Res Microbiol 160: 267-277
-
(2009)
Res Microbiol
, vol.160
, pp. 267-277
-
-
Masters, M.1
Blakely, G.2
Coulson, A.3
McLennan, N.4
Yerko, V.5
Acord, J.6
-
27
-
-
2642659387
-
GroE is vital for cell-wall synthesis
-
McLennan N, Masters M (1998) GroE is vital for cell-wall synthesis. Nature 392: 139
-
(1998)
Nature
, vol.392
, pp. 139
-
-
McLennan, N.1
Masters, M.2
-
28
-
-
0028961335
-
SCOP: A structural classification of proteins database for the investigation of sequences and structures
-
Murzin AG, Brenner SE, Hubbard T, Chothia C (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures. J Mol Biol 247: 536-540
-
(1995)
J Mol Biol
, vol.247
, pp. 536-540
-
-
Murzin, A.G.1
Brenner, S.E.2
Hubbard, T.3
Chothia, C.4
-
29
-
-
63149130741
-
Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins
-
Niwa T, Ying BW, Saito K, Jin W, Takada S, Ueda T, Taguchi H (2009) Bimodal protein solubility distribution revealed by an aggregation analysis of the entire ensemble of Escherichia coli proteins. Proc Natl Acad Sci USA 106: 4201-4206
-
(2009)
Proc Natl Acad Sci USA
, vol.106
, pp. 4201-4206
-
-
Niwa, T.1
Ying, B.W.2
Saito, K.3
Jin, W.4
Takada, S.5
Ueda, T.6
Taguchi, H.7
-
30
-
-
36949006280
-
Low folding propensity and high translation efficiency distinguish in vivo substrates of GroEL from other Escherichia coli proteins
-
Noivirt-Brik O, Unger R, Horovitz A (2007) Low folding propensity and high translation efficiency distinguish in vivo substrates of GroEL from other Escherichia coli proteins. Bioinformatics 23: 3276-3279
-
(2007)
Bioinformatics
, vol.23
, pp. 3276-3279
-
-
Noivirt-Brik, O.1
Unger, R.2
Horovitz, A.3
-
31
-
-
24044515001
-
FoldIndex: A simple tool to predict whether a given protein sequence is intrinsically unfolded
-
Prilusky J, Felder CE, Zeev-Ben-Mordehai T, Rydberg EH, Man O, Beckmann JS, Silman I, Sussman JL (2005) FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded. Bioinformatics 21: 3435-3438
-
(2005)
Bioinformatics
, vol.21
, pp. 3435-3438
-
-
Prilusky, J.1
Felder, C.E.2
Zeev-Ben-Mordehai, T.3
Rydberg, E.H.4
Man, O.5
Beckmann, J.S.6
Silman, I.7
Sussman, J.L.8
-
32
-
-
0037030713
-
Hsp90 as a capacitor of phenotypic variation
-
Queitsch C, Sangster TA, Lindquist S (2002) Hsp90 as a capacitor of phenotypic variation. Nature 417: 618-624
-
(2002)
Nature
, vol.417
, pp. 618-624
-
-
Queitsch, C.1
Sangster, T.A.2
Lindquist, S.3
-
33
-
-
0032569851
-
Hsp90 as a capacitor for morphological evolution
-
Rutherford SL, Lindquist S (1998) Hsp90 as a capacitor for morphological evolution. Nature 396: 336-342
-
(1998)
Nature
, vol.396
, pp. 336-342
-
-
Rutherford, S.L.1
Lindquist, S.2
-
34
-
-
0033597834
-
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES
-
Sakikawa C, Taguchi H, Makino Y, Yoshida M (1999) On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES. J Biol Chem 274: 21251-21256
-
(1999)
J Biol Chem
, vol.274
, pp. 21251-21256
-
-
Sakikawa, C.1
Taguchi, H.2
Makino, Y.3
Yoshida, M.4
-
35
-
-
4143134164
-
Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity
-
Shimamura T, Koike-Takeshita A, Yokoyama K, Masui R, Murai N, Yoshida M, Taguchi H, Iwata S (2004) Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity. Structure 12: 1471-1480
-
(2004)
Structure
, vol.12
, pp. 1471-1480
-
-
Shimamura, T.1
Koike-Takeshita, A.2
Yokoyama, K.3
Masui, R.4
Murai, N.5
Yoshida, M.6
Taguchi, H.7
Iwata, S.8
-
36
-
-
0034904102
-
Cell-free translation reconstituted with purified components
-
Shimizu Y, Inoue A, Tomari Y, Suzuki T, Yokogawa T, Nishikawa K, Ueda T (2001) Cell-free translation reconstituted with purified components. Nat Biotechnol 19: 751-755
-
(2001)
Nat Biotechnol
, vol.19
, pp. 751-755
-
-
Shimizu, Y.1
Inoue, A.2
Tomari, Y.3
Suzuki, T.4
Yokogawa, T.5
Nishikawa, K.6
Ueda, T.7
-
37
-
-
44349090822
-
Essential role of the chaperonin folding compartment in vivo
-
Tang YC, Chang HC, Chakraborty K, Hartl FU, Hayer-Hartl M (2008) Essential role of the chaperonin folding compartment in vivo. EMBO J 27: 1458-1468
-
(2008)
EMBO J
, vol.27
, pp. 1458-1468
-
-
Tang, Y.C.1
Chang, H.C.2
Chakraborty, K.3
Hartl, F.U.4
Hayer-Hartl, M.5
-
38
-
-
33646897305
-
Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein
-
Tang YC, Chang HC, Roeben A, Wischnewski D, Wischnewski N, Kerner MJ, Hartl FU, Hayer-Hartl M (2006) Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell 125: 903-914
-
(2006)
Cell
, vol.125
, pp. 903-914
-
-
Tang, Y.C.1
Chang, H.C.2
Roeben, A.3
Wischnewski, D.4
Wischnewski, N.5
Kerner, M.J.6
Hartl, F.U.7
Hayer-Hartl, M.8
-
39
-
-
59649108762
-
Do viral proteins possess unique biophysical features?
-
Tokuriki N, Oldfield CJ, Uversky VN, Berezovsky IN, Tawfik DS (2009) Do viral proteins possess unique biophysical features? Trends Biochem Sci 34: 53-59
-
(2009)
Trends Biochem Sci
, vol.34
, pp. 53-59
-
-
Tokuriki, N.1
Oldfield, C.J.2
Uversky, V.N.3
Berezovsky, I.N.4
Tawfik, D.S.5
-
40
-
-
0024439338
-
Demonstration by genetic suppression of interaction of GroE products with many proteins
-
Van Dyk TK, Gatenby AA, LaRossa RA (1989) Demonstration by genetic suppression of interaction of GroE products with many proteins. Nature 342: 451-453
-
(1989)
Nature
, vol.342
, pp. 451-453
-
-
Van Dyk, T.K.1
Gatenby, A.A.2
Larossa, R.A.3
-
41
-
-
0027065105
-
Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
-
Viitanen PV, Gatenby AA, Lorimer GH (1992) Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins. Protein Sci 1: 363-369
-
(1992)
Protein Sci
, vol.1
, pp. 363-369
-
-
Viitanen, P.V.1
Gatenby, A.A.2
Lorimer, G.H.3
-
42
-
-
0030870719
-
The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
-
Xu Z, Horwich AL, Sigler PB (1997) The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 388: 741-750
-
(1997)
Nature
, vol.388
, pp. 741-750
-
-
Xu, Z.1
Horwich, A.L.2
Sigler, P.B.3
-
43
-
-
15744367738
-
Co-translational involvement of the chaperonin GroEL in the folding of newly translated polypeptides
-
Ying BW, Taguchi H, Kondo M, Ueda T (2005) Co-translational involvement of the chaperonin GroEL in the folding of newly translated polypeptides. J Biol Chem 280: 12035-12040
-
(2005)
J Biol Chem
, vol.280
, pp. 12035-12040
-
-
Ying, B.W.1
Taguchi, H.2
Kondo, M.3
Ueda, T.4
|