145 related articles for article (PubMed ID: 11563912)
1. Crystal structure of chaperonin-60 from Paracoccus denitrificans.
Fukami TA; Yohda M; Taguchi H; Yoshida M; Miki K
J Mol Biol; 2001 Sep; 312(3):501-9. PubMed ID: 11563912
[TBL] [Abstract][Full Text] [Related]
2. A thermophilic mini-chaperonin contains a conserved polypeptide-binding surface: combined crystallographic and NMR studies of the GroEL apical domain with implications for substrate interactions.
Hua Q; Dementieva IS; Walsh MA; Hallenga K; Weiss MA; Joachimiak A
J Mol Biol; 2001 Feb; 306(3):513-25. PubMed ID: 11178910
[TBL] [Abstract][Full Text] [Related]
3. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex.
Xu Z; Horwich AL; Sigler PB
Nature; 1997 Aug; 388(6644):741-50. PubMed ID: 9285585
[TBL] [Abstract][Full Text] [Related]
4. An arginine residue (Arg101), which is conserved in many GroEL homologues, is required for interactions between the two heptameric rings.
Jones S; Wallington EJ; George R; Lund PA
J Mol Biol; 1998 Oct; 282(4):789-800. PubMed ID: 9743627
[TBL] [Abstract][Full Text] [Related]
5. The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
Braig K; Otwinowski Z; Hegde R; Boisvert DC; Joachimiak A; Horwich AL; Sigler PB
Nature; 1994 Oct; 371(6498):578-86. PubMed ID: 7935790
[TBL] [Abstract][Full Text] [Related]
6. Crystal structure of Paracoccus denitrificans electron transfer flavoprotein: structural and electrostatic analysis of a conserved flavin binding domain.
Roberts DL; Salazar D; Fulmer JP; Frerman FE; Kim JJ
Biochemistry; 1999 Feb; 38(7):1977-89. PubMed ID: 10026281
[TBL] [Abstract][Full Text] [Related]
7. Allostery wiring diagrams in the transitions that drive the GroEL reaction cycle.
Tehver R; Chen J; Thirumalai D
J Mol Biol; 2009 Mar; 387(2):390-406. PubMed ID: 19121324
[TBL] [Abstract][Full Text] [Related]
8. From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.
Chatellier J; Hill F; Fersht AR
J Mol Biol; 2000 Dec; 304(5):883-96. PubMed ID: 11124034
[TBL] [Abstract][Full Text] [Related]
9. Functional consequences of single:double ring transitions in chaperonins: life in the cold.
Ferrer M; Lünsdorf H; Chernikova TN; Yakimov M; Timmis KN; Golyshin PN
Mol Microbiol; 2004 Jul; 53(1):167-82. PubMed ID: 15225312
[TBL] [Abstract][Full Text] [Related]
10. Unliganded GroEL at 2.8 A: structure and functional implications.
Sigler PB; Horwich AL
Philos Trans R Soc Lond B Biol Sci; 1995 Apr; 348(1323):113-9. PubMed ID: 7770481
[TBL] [Abstract][Full Text] [Related]
11. Inter-ring communication is disrupted in the GroEL mutant Arg13 --> Gly; Ala126 --> Val with known crystal structure.
Aharoni A; Horovitz A
J Mol Biol; 1996 May; 258(5):732-5. PubMed ID: 8637005
[TBL] [Abstract][Full Text] [Related]
12. Structures of unliganded and ATP-bound states of the Escherichia coli chaperonin GroEL by cryoelectron microscopy.
Roseman AM; Ranson NA; Gowen B; Fuller SD; Saibil HR
J Struct Biol; 2001 Aug; 135(2):115-25. PubMed ID: 11580261
[TBL] [Abstract][Full Text] [Related]
13. From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.
Chatellier J; Hill F; Foster NW; Goloubinoff P; Fersht AR
J Mol Biol; 2000 Dec; 304(5):897-910. PubMed ID: 11124035
[TBL] [Abstract][Full Text] [Related]
14. Crystal structure of wild-type chaperonin GroEL.
Bartolucci C; Lamba D; Grazulis S; Manakova E; Heumann H
J Mol Biol; 2005 Dec; 354(4):940-51. PubMed ID: 16288915
[TBL] [Abstract][Full Text] [Related]
15. The dimeric structure of the Cpn60.2 chaperonin of Mycobacterium tuberculosis at 2.8 Å reveals possible modes of function.
Shahar A; Melamed-Frank M; Kashi Y; Shimon L; Adir N
J Mol Biol; 2011 Sep; 412(2):192-203. PubMed ID: 21802426
[TBL] [Abstract][Full Text] [Related]
16. The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy.
Falke S; Tama F; Brooks CL; Gogol EP; Fisher MT
J Mol Biol; 2005 Apr; 348(1):219-30. PubMed ID: 15808865
[TBL] [Abstract][Full Text] [Related]
17. Characterisation of mutations in GroES that allow GroEL to function as a single ring.
Liu H; Kovács E; Lund PA
FEBS Lett; 2009 Jul; 583(14):2365-71. PubMed ID: 19545569
[TBL] [Abstract][Full Text] [Related]
18. The origins and consequences of asymmetry in the chaperonin reaction cycle.
Burston SG; Ranson NA; Clarke AR
J Mol Biol; 1995 May; 249(1):138-52. PubMed ID: 7776368
[TBL] [Abstract][Full Text] [Related]
19. Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 -> Ala.
Danziger O; Rivenzon-Segal D; Wolf SG; Horovitz A
Proc Natl Acad Sci U S A; 2003 Nov; 100(24):13797-802. PubMed ID: 14615587
[TBL] [Abstract][Full Text] [Related]
20. 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
Structure; 2004 Aug; 12(8):1471-80. PubMed ID: 15296740
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
