These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
137 related articles for article (PubMed ID: 7714895)
21. 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]
22. Synthesis of the pro-peptide of subtilisin BPN'. Cash PW; Zhu X; Ohta Y; Tsao J; Lackland H; Mateos-Nevado MD; Inouye M; Stein S; Jordan F; Tous GI Pept Res; 1989; 2(4):292-6. PubMed ID: 2520768 [TBL] [Abstract][Full Text] [Related]
23. 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]
24. 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]
25. 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]
26. Total chemical synthesis and oxidative folding of delta-conotoxin PVIA containing an N-terminal propeptide. Buczek P; Buczek O; Bulaj G Biopolymers; 2005; 80(1):50-7. PubMed ID: 15641120 [TBL] [Abstract][Full Text] [Related]
27. Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process. Zhu XL; Ohta Y; Jordan F; Inouye M Nature; 1989 Jun; 339(6224):483-4. PubMed ID: 2657436 [TBL] [Abstract][Full Text] [Related]
28. Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment. Strausberg S; Alexander P; Wang L; Schwarz F; Bryan P Biochemistry; 1993 Aug; 32(32):8112-9. PubMed ID: 8347611 [TBL] [Abstract][Full Text] [Related]
29. Mutated intramolecular chaperones generate high-activity isomers of mature enzymes. Nagayama M; Maeda H; Kuroda K; Ueda M Biochemistry; 2012 May; 51(17):3547-53. PubMed ID: 22482366 [TBL] [Abstract][Full Text] [Related]
30. Rapid folding of calcium-free subtilisin by a stabilized pro-domain mutant. Ruan B; Hoskins J; Bryan PN Biochemistry; 1999 Jun; 38(26):8562-71. PubMed ID: 10387104 [TBL] [Abstract][Full Text] [Related]
31. Proregion of Bombyx mori cysteine proteinase functions as an intramolecular chaperone to promote proper folding of the mature enzyme. Yamamoto Y; Watabe S; Kageyama T; Takahashi SY Arch Insect Biochem Physiol; 1999 Nov; 42(3):167-78. PubMed ID: 10536045 [TBL] [Abstract][Full Text] [Related]
32. 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]
33. Further evidence for the structure of the subtilisin propeptide and for its interactions with mature subtilisin. Hu Z; Haghjoo K; Jordan F J Biol Chem; 1996 Feb; 271(7):3375-84. PubMed ID: 8631936 [TBL] [Abstract][Full Text] [Related]
34. Ca2+-dependent maturation of subtilisin from a hyperthermophilic archaeon, Thermococcus kodakaraensis: the propeptide is a potent inhibitor of the mature domain but is not required for its folding. Pulido M; Saito K; Tanaka S; Koga Y; Morikawa M; Takano K; Kanaya S Appl Environ Microbiol; 2006 Jun; 72(6):4154-62. PubMed ID: 16751527 [TBL] [Abstract][Full Text] [Related]
35. Folding pathway mediated by an intramolecular chaperone: propeptide release modulates activation precision of pro-subtilisin. Yabuta Y; Takagi H; Inouye M; Shinde U J Biol Chem; 2001 Nov; 276(48):44427-34. PubMed ID: 11577106 [TBL] [Abstract][Full Text] [Related]
36. Functional analysis of the propeptide of subtilisin E as an intramolecular chaperone for protein folding. Refolding and inhibitory abilities of propeptide mutants. Li Y; Hu Z; Jordan F; Inouye M J Biol Chem; 1995 Oct; 270(42):25127-32. PubMed ID: 7559646 [TBL] [Abstract][Full Text] [Related]
37. Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide [corrected]. Ohta Y; Hojo H; Aimoto S; Kobayashi T; Zhu X; Jordan F; Inouye M Mol Microbiol; 1991 Jun; 5(6):1507-10. PubMed ID: 1686294 [TBL] [Abstract][Full Text] [Related]
38. The role of tryptophan residues in the autoprocessing of prosubtilisin E. Sone M; Falzon L; Inouye M Biochim Biophys Acta; 2005 May; 1749(1):15-22. PubMed ID: 15848132 [TBL] [Abstract][Full Text] [Related]
39. 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]
40. Increase in activation rate of Pro-Tk-subtilisin by a single nonpolar-to-polar amino acid substitution at the hydrophobic core of the propeptide domain. Yuzaki K; Sanda Y; You DJ; Uehara R; Koga Y; Kanaya S Protein Sci; 2013 Dec; 22(12):1711-21. PubMed ID: 24115021 [TBL] [Abstract][Full Text] [Related] [Previous] [Next] [New Search]