185 related articles for article (PubMed ID: 10764571)
41. The slow folding reaction of barstar: the core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain.
Sridevi K; Juneja J; Bhuyan AK; Krishnamoorthy G; Udgaonkar JB
J Mol Biol; 2000 Sep; 302(2):479-95. PubMed ID: 10970747
[TBL] [Abstract][Full Text] [Related]
42. Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. I. GroEL recognizes the signal sequences of beta-lactamase precursor.
Zahn R; Axmann SE; Rücknagel KP; Jaeger E; Laminet AA; Plückthun A
J Mol Biol; 1994 Sep; 242(2):150-64. PubMed ID: 7916381
[TBL] [Abstract][Full Text] [Related]
43. Refolding of bovine mitochondrial rhodanese by chaperonins GroEL and GroES.
Weber F; Hayer-Hartl M
Methods Mol Biol; 2000; 140():117-26. PubMed ID: 11484478
[No Abstract] [Full Text] [Related]
44. A simple model of chaperonin-mediated protein folding.
Chan HS; Dill KA
Proteins; 1996 Mar; 24(3):345-51. PubMed ID: 8778781
[TBL] [Abstract][Full Text] [Related]
45. Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states.
Chaudhry C; Horwich AL; Brunger AT; Adams PD
J Mol Biol; 2004 Sep; 342(1):229-45. PubMed ID: 15313620
[TBL] [Abstract][Full Text] [Related]
46. Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.
Gupta P; Aggarwal N; Batra P; Mishra S; Chaudhuri TK
Int J Biochem Cell Biol; 2006; 38(11):1975-85. PubMed ID: 16822698
[TBL] [Abstract][Full Text] [Related]
47. No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange.
Park ES; Fenton WA; Horwich AL
FEBS Lett; 2005 Feb; 579(5):1183-6. PubMed ID: 15710410
[TBL] [Abstract][Full Text] [Related]
48. Refolding of thioredoxin reductase assisted by groEL and PDI.
Cheung PY; Churchich JE; Lee KS
Biochem Biophys Res Commun; 1999 Feb; 255(1):17-22. PubMed ID: 10082648
[TBL] [Abstract][Full Text] [Related]
49. Transient kinetic analysis of adenosine 5'-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL.
Yifrach O; Horovitz A
Biochemistry; 1998 May; 37(20):7083-8. PubMed ID: 9585518
[TBL] [Abstract][Full Text] [Related]
50. Identification of native and non-native structure in kinetic folding intermediates of apomyoglobin.
Nishimura C; Dyson HJ; Wright PE
J Mol Biol; 2006 Jan; 355(1):139-56. PubMed ID: 16300787
[TBL] [Abstract][Full Text] [Related]
51. Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL.
Katsumata K; Okazaki A; Tsurupa GP; Kuwajima K
J Mol Biol; 1996 Dec; 264(4):643-9. PubMed ID: 8980675
[TBL] [Abstract][Full Text] [Related]
52. Protein folding: how the mechanism of GroEL action is defined by kinetics.
Frieden C; Clark AC
Proc Natl Acad Sci U S A; 1997 May; 94(11):5535-8. PubMed ID: 9159107
[TBL] [Abstract][Full Text] [Related]
53. Folding of maltose binding protein outside of and in GroEL.
Ye X; Mayne L; Kan ZY; Englander SW
Proc Natl Acad Sci U S A; 2018 Jan; 115(3):519-524. PubMed ID: 29295923
[TBL] [Abstract][Full Text] [Related]
54. Phi value analysis of an allosteric transition of GroEL based on a single-pathway model.
Inobe T; Kuwajima K
J Mol Biol; 2004 May; 339(1):199-205. PubMed ID: 15123431
[TBL] [Abstract][Full Text] [Related]
55. Recovery and reuse of the molecular chaperone GroEL for in vitro protein refolding.
Guise AD; Chaudhuri JB
Biotechnol Prog; 1998; 14(2):343-6. PubMed ID: 9548790
[TBL] [Abstract][Full Text] [Related]
56. Investigation of the unfolding pathway of Bacillus thuringiensis Cyt2Aa2 toxin reveals an unfolding intermediate.
Sangcharoen A; Tepanant W; Kidsanguan S; Promdonkoy B; Krittanai C
J Biotechnol; 2009 May; 141(3-4):137-41. PubMed ID: 19433217
[TBL] [Abstract][Full Text] [Related]
57. Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds.
Ranson NA; Dunster NJ; Burston SG; Clarke AR
J Mol Biol; 1995 Jul; 250(5):581-6. PubMed ID: 7623376
[TBL] [Abstract][Full Text] [Related]
58. Direct refolding of inclusion bodies using reversed micelles.
Sakono M; Kawashima YM; Ichinose H; Maruyama T; Kamiya N; Goto M
Biotechnol Prog; 2004; 20(6):1783-7. PubMed ID: 15575712
[TBL] [Abstract][Full Text] [Related]
59. Dependence of the size of the initially collapsed form during the refolding of barstar on denaturant concentration: evidence for a continuous transition.
Sinha KK; Udgaonkar JB
J Mol Biol; 2005 Oct; 353(3):704-18. PubMed ID: 16188274
[TBL] [Abstract][Full Text] [Related]
60. Protein folding: inside the cage.
Ellis RJ
Nature; 2006 Jul; 442(7101):360-2. PubMed ID: 16871196
[No Abstract] [Full Text] [Related]
[Previous] [Next] [New Search]
