244 related articles for article (PubMed ID: 15157092)
1. Key elements for protein foldability revealed by a combinatorial approach among similarly folded but distantly related proteins.
Morimoto S; Tamura A
Biochemistry; 2004 Jun; 43(21):6596-605. PubMed ID: 15157092
[TBL] [Abstract][Full Text] [Related]
2. 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]
3. Alteration of inhibitory properties of Pleurotus ostreatus proteinase A inhibitor 1 by mutation of its C-terminal region.
Kojima S; Hisano Y; Miura K
Biochem Biophys Res Commun; 2001 Mar; 281(5):1271-6. PubMed ID: 11243873
[TBL] [Abstract][Full Text] [Related]
4. Effects of hydrophobic amino acid substitution in Pleurotus ostreatus proteinase A inhibitor 1 on its structure and functions as protease inhibitor and intramolecular chaperone.
Kojima S; Iwahara A; Hisano Y; Yanai H
Protein Eng Des Sel; 2007 May; 20(5):211-7. PubMed ID: 17437962
[TBL] [Abstract][Full Text] [Related]
5. 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]
6. 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]
7. Engineering the independent folding of the subtilisin BPN' prodomain: analysis of two-state folding versus protein stability.
Ruvinov S; Wang L; Ruan B; Almog O; Gilliland GL; Eisenstein E; Bryan PN
Biochemistry; 1997 Aug; 36(34):10414-21. PubMed ID: 9265621
[TBL] [Abstract][Full Text] [Related]
8. Novel protease inhibitors via computational redesign of subtilisin BPN' propeptide.
Daugherty AB; Muthu P; Lutz S
Biochemistry; 2012 Oct; 51(41):8247-55. PubMed ID: 23009354
[TBL] [Abstract][Full Text] [Related]
9. Requirement for hydrophobic Phe residues in Pleurotus ostreatus proteinase A inhibitor 1 for stable inhibition.
Kojima S; Hisano Y
Protein Eng; 2002 Apr; 15(4):325-9. PubMed ID: 11983933
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. 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]
12. The crystal structure of an autoprocessed Ser221Cys-subtilisin E-propeptide complex at 2.0 A resolution.
Jain SC; Shinde U; Li Y; Inouye M; Berman HM
J Mol Biol; 1998 Nov; 284(1):137-44. PubMed ID: 9811547
[TBL] [Abstract][Full Text] [Related]
13. Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53--a structural and combinatorial approach.
Mora P; Carbajo RJ; Pineda-Lucena A; Sánchez del Pino MM; Pérez-Payá E
Proteins; 2008 Jun; 71(4):1670-85. PubMed ID: 18076077
[TBL] [Abstract][Full Text] [Related]
14. Stabilizing the subtilisin BPN' pro-domain by phage display selection: how restrictive is the amino acid code for maximum protein stability?
Ruan B; Hoskins J; Wang L; Bryan PN
Protein Sci; 1998 Nov; 7(11):2345-53. PubMed ID: 9828000
[TBL] [Abstract][Full Text] [Related]
15. Tertiary structure formation in the propeptide of subtilisin BPN' by successive amino acid replacements and its close relation to function.
Kojima S; Minagawa T; Miura K
J Mol Biol; 1998 Apr; 277(5):1007-13. PubMed ID: 9571018
[TBL] [Abstract][Full Text] [Related]
16. Folding of proteins with WD-repeats: comparison of six members of the WD-repeat superfamily to the G protein beta subunit.
Garcia-Higuera I; Fenoglio J; Li Y; Lewis C; Panchenko MP; Reiner O; Smith TF; Neer EJ
Biochemistry; 1996 Nov; 35(44):13985-94. PubMed ID: 8909296
[TBL] [Abstract][Full Text] [Related]
17. Protein design through systematic catalytic loop exchange in the (beta/alpha)8 fold.
Ochoa-Leyva A; Soberón X; Sánchez F; Argüello M; Montero-Morán G; Saab-Rincón G
J Mol Biol; 2009 Apr; 387(4):949-64. PubMed ID: 19233201
[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. The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.
Li M; Phylip LH; Lees WE; Winther JR; Dunn BM; Wlodawer A; Kay J; Gustchina A
Nat Struct Biol; 2000 Feb; 7(2):113-7. PubMed ID: 10655612
[TBL] [Abstract][Full Text] [Related]
20. 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]
[Next] [New Search]
