136 related articles for article (PubMed ID: 23106363)
1. Slow unfolding pathway of hyperthermophilic Tk-RNase H2 examined by pulse proteolysis using the stable protease Tk-subtilisin.
Okada J; Koga Y; Takano K; Kanaya S
Biochemistry; 2012 Nov; 51(45):9178-91. PubMed ID: 23106363
[TBL] [Abstract][Full Text] [Related]
2. Kinetically robust monomeric protein from a hyperthermophile.
Mukaiyama A; Takano K; Haruki M; Morikawa M; Kanaya S
Biochemistry; 2004 Nov; 43(43):13859-66. PubMed ID: 15504048
[TBL] [Abstract][Full Text] [Related]
3. Folding and Unfolding Kinetics of Unpurified Proteins by Pulse Proteolysis.
Shima K; Okada J; Sano S; Takano K
Protein Pept Lett; 2016; 23(11):976-987. PubMed ID: 27653628
[TBL] [Abstract][Full Text] [Related]
4. Subtilisin-like serine protease from hyperthermophilic archaeon Thermococcus kodakaraensis with N- and C-terminal propeptides.
Foophow T; Tanaka S; Koga Y; Takano K; Kanaya S
Protein Eng Des Sel; 2010 May; 23(5):347-55. PubMed ID: 20100702
[TBL] [Abstract][Full Text] [Related]
5. Proline effect on the thermostability and slow unfolding of a hyperthermophilic protein.
Takano K; Higashi R; Okada J; Mukaiyama A; Tadokoro T; Koga Y; Kanaya S
J Biochem; 2009 Jan; 145(1):79-85. PubMed ID: 18977771
[TBL] [Abstract][Full Text] [Related]
6. Accelerated maturation of Tk-subtilisin by a Leu→Pro mutation at the C-terminus of the propeptide, which reduces the binding of the propeptide to Tk-subtilisin.
Uehara R; Ueda Y; You DJ; Koga Y; Kanaya S
FEBS J; 2013 Feb; 280(4):994-1006. PubMed ID: 23237738
[TBL] [Abstract][Full Text] [Related]
7. Hydrophobic effect on the stability and folding of a hyperthermophilic protein.
Dong H; Mukaiyama A; Tadokoro T; Koga Y; Takano K; Kanaya S
J Mol Biol; 2008 Apr; 378(1):264-72. PubMed ID: 18353366
[TBL] [Abstract][Full Text] [Related]
8. Osmolyte effect on the stability and folding of a hyperthermophilic protein.
Mukaiyama A; Koga Y; Takano K; Kanaya S
Proteins; 2008 Apr; 71(1):110-8. PubMed ID: 17932924
[TBL] [Abstract][Full Text] [Related]
9. Folding of horse cytochrome c in the reduced state.
Bhuyan AK; Udgaonkar JB
J Mol Biol; 2001 Oct; 312(5):1135-60. PubMed ID: 11580255
[TBL] [Abstract][Full Text] [Related]
10. 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]
11. Kinetic and thermodynamic thermal stabilities of ribonuclease A and ribonuclease B.
Arnold U; Ulbrich-Hofmann R
Biochemistry; 1997 Feb; 36(8):2166-72. PubMed ID: 9047316
[TBL] [Abstract][Full Text] [Related]
12. Equilibrium and kinetic stability of a hyperthermophilic protein, O6-methylguanine-DNA methyltransferase under various extreme conditions.
Nishikori S; Shiraki K; Okanojo M; Imanaka T; Takagi M
J Biochem; 2004 Oct; 136(4):503-8. PubMed ID: 15625320
[TBL] [Abstract][Full Text] [Related]
13. Requirement of left-handed glycine residue for high stability of the Tk-subtilisin propeptide as revealed by mutational and crystallographic analyses.
Pulido MA; Tanaka S; Sringiew C; You DJ; Matsumura H; Koga Y; Takano K; Kanaya S
J Mol Biol; 2007 Dec; 374(5):1359-73. PubMed ID: 17988685
[TBL] [Abstract][Full Text] [Related]
14. Characterization of the folding and unfolding reactions of single-chain monellin: evidence for multiple intermediates and competing pathways.
Patra AK; Udgaonkar JB
Biochemistry; 2007 Oct; 46(42):11727-43. PubMed ID: 17902706
[TBL] [Abstract][Full Text] [Related]
15. An alternative mature form of subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis identified in the presence of Ca2+.
Sinsereekul N; Foophow T; Yamanouchi M; Koga Y; Takano K; Kanaya S
FEBS J; 2011 Jun; 278(11):1901-11. PubMed ID: 21443525
[TBL] [Abstract][Full Text] [Related]
16. Requirement of a unique Ca(2+)-binding loop for folding of Tk-subtilisin from a hyperthermophilic archaeon.
Takeuchi Y; Tanaka S; Matsumura H; Koga Y; Takano K; Kanaya S
Biochemistry; 2009 Nov; 48(44):10637-43. PubMed ID: 19813760
[TBL] [Abstract][Full Text] [Related]
17. Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins.
Okada J; Okamoto T; Mukaiyama A; Tadokoro T; You DJ; Chon H; Koga Y; Takano K; Kanaya S
BMC Evol Biol; 2010 Jul; 10():207. PubMed ID: 20615256
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Crystal structure of a subtilisin homologue, Tk-SP, from Thermococcus kodakaraensis: requirement of a C-terminal beta-jelly roll domain for hyperstability.
Foophow T; Tanaka S; Angkawidjaja C; Koga Y; Takano K; Kanaya S
J Mol Biol; 2010 Jul; 400(4):865-77. PubMed ID: 20595040
[TBL] [Abstract][Full Text] [Related]
20. 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]
[Next] [New Search]