112 related articles for article (PubMed ID: 9534172)
1. Photoincorporation of fluorescent probe into GroEL: defining site of interaction.
Seale JW; Brazil BT; Horowitz PM
Methods Enzymol; 1998; 290():318-23. PubMed ID: 9534172
[TBL] [Abstract][Full Text] [Related]
2. Photoincorporation of 4,4'-bis(1-anilino-8-naphthalenesulfonic acid) into the apical domain of GroEL: specific information from a nonspecific probe.
Seale JW; Martinez JL; Horowitz PM
Biochemistry; 1995 Jun; 34(22):7443-9. PubMed ID: 7779787
[TBL] [Abstract][Full Text] [Related]
3. Residual structure in urea-denatured chaperonin GroEL.
Gorovits BM; Seale JW; Horowitz PM
Biochemistry; 1995 Oct; 34(42):13928-33. PubMed ID: 7577988
[TBL] [Abstract][Full Text] [Related]
4. The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL.
Smoot AL; Panda M; Brazil BT; Buckle AM; Fersht AR; Horowitz PM
Biochemistry; 2001 Apr; 40(14):4484-92. PubMed ID: 11284705
[TBL] [Abstract][Full Text] [Related]
5. Hydrophobic surfaces that are hidden in chaperonin Cpn60 can be exposed by formation of assembly-competent monomers or by ionic perturbation of the oligomer.
Horowitz PM; Hua S; Gibbons DL
J Biol Chem; 1995 Jan; 270(4):1535-42. PubMed ID: 7829481
[TBL] [Abstract][Full Text] [Related]
6. Application of fluorescence resonance energy transfer to the GroEL-GroES chaperonin reaction.
Rye HS
Methods; 2001 Jul; 24(3):278-88. PubMed ID: 11403576
[TBL] [Abstract][Full Text] [Related]
7. The folded conformation of phage P22 coat protein is affected by amino acid substitutions that lead to a cold-sensitive phenotype.
Fong DG; Doyle SM; Teschke CM
Biochemistry; 1997 Apr; 36(13):3971-80. PubMed ID: 9092827
[TBL] [Abstract][Full Text] [Related]
8. Hydrophilic residues at the apical domain of GroEL contribute to GroES binding but attenuate polypeptide binding.
Motojima F; Makio T; Aoki K; Makino Y; Kuwajima K; Yoshida M
Biochem Biophys Res Commun; 2000 Jan; 267(3):842-9. PubMed ID: 10673379
[TBL] [Abstract][Full Text] [Related]
9. Exposure of hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401.
Gibbons DL; Horowitz PM
J Biol Chem; 1995 Mar; 270(13):7335-40. PubMed ID: 7706275
[TBL] [Abstract][Full Text] [Related]
10. Reaction Cycle of Chaperonin GroEL via Symmetric "Football" Intermediate.
Taguchi H
J Mol Biol; 2015 Sep; 427(18):2912-8. PubMed ID: 25900372
[TBL] [Abstract][Full Text] [Related]
11. Apomyoglobin folding intermediates characterized by the hydrophobic fluorescent probe 8-anilino-1-naphthalene sulfonate.
Sirangelo I; Bismuto E; Tavassi S; Irace G
Biochim Biophys Acta; 1998 Jun; 1385(1):69-77. PubMed ID: 9630524
[TBL] [Abstract][Full Text] [Related]
12. GroEL walks the fine line: the subtle balance of substrate and co-chaperonin binding by GroEL. A combinatorial investigation by design, selection and screening.
Kawe M; Plückthun A
J Mol Biol; 2006 Mar; 357(2):411-26. PubMed ID: 16427651
[TBL] [Abstract][Full Text] [Related]
13. Identification of amino acid residues at nucleotide-binding sites of chaperonin GroEL/GroES and cpn10 by photoaffinity labeling with 2-azido-adenosine 5'-triphosphate.
Bramhall EA; Cross RL; Rospert S; Steede NK; Landry SJ
Eur J Biochem; 1997 Mar; 244(2):627-34. PubMed ID: 9119033
[TBL] [Abstract][Full Text] [Related]
14. ATP hydrolysis is critical for induction of conformational changes in GroEL that expose hydrophobic surfaces.
Gorovits BM; Ybarra J; Horowitz PM
J Biol Chem; 1997 Mar; 272(11):6842-5. PubMed ID: 9054367
[TBL] [Abstract][Full Text] [Related]
15. Chaperonin-Assisted Protein Folding: Relative Population of Asymmetric and Symmetric GroEL:GroES Complexes.
Haldar S; Gupta AJ; Yan X; Miličić G; Hartl FU; Hayer-Hartl M
J Mol Biol; 2015 Jun; 427(12):2244-55. PubMed ID: 25912285
[TBL] [Abstract][Full Text] [Related]
16. The hydrophobic probe 4,4'-bis(1-anilino-8-naphthalene sulfonic acid) is specifically photoincorporated into the N-terminal domain of alpha B-crystallin.
Smulders RH; de Jong WW
FEBS Lett; 1997 Jun; 409(1):101-4. PubMed ID: 9199512
[TBL] [Abstract][Full Text] [Related]
17. Active cage mechanism of chaperonin-assisted protein folding demonstrated at single-molecule level.
Gupta AJ; Haldar S; Miličić G; Hartl FU; Hayer-Hartl M
J Mol Biol; 2014 Jul; 426(15):2739-54. PubMed ID: 24816391
[TBL] [Abstract][Full Text] [Related]
18. Binding of a burst-phase intermediate formed in the folding of denatured D-glyceraldehyde-3-phosphate dehydrogenase by chaperonin 60 and 8-anilino-1-naphthalenesulphonic acid.
Li XL; Lei XD; Cai H; Li J; Yang SL; Wang CC; Tsou CL
Biochem J; 1998 Apr; 331 ( Pt 2)(Pt 2):505-11. PubMed ID: 9531491
[TBL] [Abstract][Full Text] [Related]
19. Reversible oligomerization and denaturation of the chaperonin GroES.
Seale JW; Gorovits BM; Ybarra J; Horowitz PM
Biochemistry; 1996 Apr; 35(13):4079-83. PubMed ID: 8672442
[TBL] [Abstract][Full Text] [Related]
20. Fluorescence anisotropy method for investigation of GroEL-GroES interaction.
Gorovits BM; Horowitz PM
Methods Enzymol; 1998; 290():313-7. PubMed ID: 9534171
[No Abstract] [Full Text] [Related]
[Next] [New Search]
