336 related articles for article (PubMed ID: 11114254)
1. Folding pathway mediated by an intramolecular chaperone: the structural and functional characterization of the aqualysin I propeptide.
Marie-Claire C; Yabuta Y; Suefuji K; Matsuzawa H; Shinde U
J Mol Biol; 2001 Jan; 305(1):151-65. PubMed ID: 11114254
[TBL] [Abstract][Full Text] [Related]
2. Folding pathway mediated by an intramolecular chaperone: characterization of the structural changes in pro-subtilisin E coincident with autoprocessing.
Shinde U; Inouye M
J Mol Biol; 1995 Sep; 252(1):25-30. PubMed ID: 7666430
[TBL] [Abstract][Full Text] [Related]
3. Folding of subtilisin BPN': role of the pro-sequence.
Eder J; Rheinnecker M; Fersht AR
J Mol Biol; 1993 Sep; 233(2):293-304. PubMed ID: 8377204
[TBL] [Abstract][Full Text] [Related]
4. Autotomic behavior of the propeptide in propeptide-mediated folding of prosubtilisin E.
Falzon L; Patel S; Chen YJ; Inouye M
J Mol Biol; 2007 Feb; 366(2):494-503. PubMed ID: 17169372
[TBL] [Abstract][Full Text] [Related]
5. Functional analysis of the propeptides of subtilisin E and aqualysin I as intramolecular chaperones.
Takagi H; Koga M; Katsurada S; Yabuta Y; Shinde U; Inouye M; Nakamori S
FEBS Lett; 2001 Nov; 508(2):210-4. PubMed ID: 11718717
[TBL] [Abstract][Full Text] [Related]
6. Structure of POIA1, a homologous protein to the propeptide of subtilisin: implication for protein foldability and the function as an intramolecular chaperone.
Sasakawa H; Yoshinaga S; Kojima S; Tamura A
J Mol Biol; 2002 Mar; 317(1):159-67. PubMed ID: 11916386
[TBL] [Abstract][Full Text] [Related]
7. Positive selection dictates the choice between kinetic and thermodynamic protein folding and stability in subtilases.
Subbian E; Yabuta Y; Shinde U
Biochemistry; 2004 Nov; 43(45):14348-60. PubMed ID: 15533039
[TBL] [Abstract][Full Text] [Related]
8. Folding pathway mediated by an intramolecular chaperone: intrinsically unstructured propeptide modulates stochastic activation of subtilisin.
Subbian E; Yabuta Y; Shinde UP
J Mol Biol; 2005 Mar; 347(2):367-83. PubMed ID: 15740747
[TBL] [Abstract][Full Text] [Related]
9. Functional analysis of propeptide as an intramolecular chaperone for in vivo folding of subtilisin nattokinase.
Jia Y; Liu H; Bao W; Weng M; Chen W; Cai Y; Zheng Z; Zou G
FEBS Lett; 2010 Dec; 584(23):4789-96. PubMed ID: 21074529
[TBL] [Abstract][Full Text] [Related]
10. Identification of the interactions critical for propeptide-catalyzed folding of Tk-subtilisin.
Tanaka S; Matsumura H; Koga Y; Takano K; Kanaya S
J Mol Biol; 2009 Nov; 394(2):306-19. PubMed ID: 19766655
[TBL] [Abstract][Full Text] [Related]
11. Accelerated refolding of subtilisin BPN' by tertiary-structure-forming mutants of its propeptide.
Kojima S; Yanai H; Miura K
J Biochem; 2001 Oct; 130(4):471-4. PubMed ID: 11574065
[TBL] [Abstract][Full Text] [Related]
12. Substrate-induced activation of a trapped IMC-mediated protein folding intermediate.
Inouye M; Fu X; Shinde U
Nat Struct Biol; 2001 Apr; 8(4):321-5. PubMed ID: 11276251
[TBL] [Abstract][Full Text] [Related]
13. A pathway for conformational diversity in proteins mediated by intramolecular chaperones.
Shinde U; Fu X; Inouye M
J Biol Chem; 1999 May; 274(22):15615-21. PubMed ID: 10336458
[TBL] [Abstract][Full Text] [Related]
14. Mimicking cotranslational folding of prosubtilisin E in vitro.
Kim SG; Chen YJ; Falzon L; Baum J; Inouye M
J Biochem; 2020 May; 167(5):473-482. PubMed ID: 31943045
[TBL] [Abstract][Full Text] [Related]
15. Folding mediated by an intramolecular chaperone: autoprocessing pathway of the precursor resolved via a substrate assisted catalysis mechanism.
Shinde U; Inouye M
J Mol Biol; 1995 Mar; 247(3):390-5. PubMed ID: 7714895
[TBL] [Abstract][Full Text] [Related]
16. Protein memory through altered folding mediated by intramolecular chaperones.
Shinde UP; Liu JJ; Inouye M
Nature; 1997 Oct; 389(6650):520-2. PubMed ID: 9333245
[TBL] [Abstract][Full Text] [Related]
17. Inhibitor-assisted refolding of protease: a protease inhibitor as an intramolecular chaperone.
Kojima S; Iwahara A; Yanai H
FEBS Lett; 2005 Aug; 579(20):4430-6. PubMed ID: 16061231
[TBL] [Abstract][Full Text] [Related]
18. A new approach for alteration of protease functions: pro-sequence engineering.
Takagi H; Takahashi M
Appl Microbiol Biotechnol; 2003 Nov; 63(1):1-9. PubMed ID: 12879301
[TBL] [Abstract][Full Text] [Related]
19. Engineering the independent folding of the subtilisin BPN' pro-domain: correlation of pro-domain stability with the rate of subtilisin folding.
Wang L; Ruan B; Ruvinov S; Bryan PN
Biochemistry; 1998 Mar; 37(9):3165-71. PubMed ID: 9485470
[TBL] [Abstract][Full Text] [Related]
20. Roles of the propeptide and metal ions in the folding and stability of the catalytic domain of stromelysin (matrix metalloproteinase 3).
Wetmore DR; Hardman KD
Biochemistry; 1996 May; 35(21):6549-58. PubMed ID: 8639603
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
