207 related articles for article (PubMed ID: 11266600)
1. Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase from E. coli: fragment complementation and circular permutation reveal stable, alternatively folded forms.
Smith VF; Matthews CR
Protein Sci; 2001 Jan; 10(1):116-28. PubMed ID: 11266600
[TBL] [Abstract][Full Text] [Related]
2. Systematic circular permutation of an entire protein reveals essential folding elements.
Iwakura M; Nakamura T; Yamane C; Maki K
Nat Struct Biol; 2000 Jul; 7(7):580-5. PubMed ID: 10876245
[TBL] [Abstract][Full Text] [Related]
3. Multistate equilibrium unfolding of Escherichia coli dihydrofolate reductase: thermodynamic and spectroscopic description of the native, intermediate, and unfolded ensembles.
Ionescu RM; Smith VF; O'Neill JC; Matthews CR
Biochemistry; 2000 Aug; 39(31):9540-50. PubMed ID: 10924151
[TBL] [Abstract][Full Text] [Related]
4. Pivotal role of Gly 121 in dihydrofolate reductase from Escherichia coli: the altered structure of a mutant enzyme may form the basis of its diminished catalytic performance.
Swanwick RS; Shrimpton PJ; Allemann RK
Biochemistry; 2004 Apr; 43(14):4119-27. PubMed ID: 15065854
[TBL] [Abstract][Full Text] [Related]
5. The coordination of the isomerization of a conserved non-prolyl cis peptide bond with the rate-limiting steps in the folding of dihydrofolate reductase.
Svensson AK; O'Neill JC; Matthews CR
J Mol Biol; 2003 Feb; 326(2):569-83. PubMed ID: 12559923
[TBL] [Abstract][Full Text] [Related]
6. Probing minimal independent folding units in dihydrofolate reductase by molecular dissection.
Gegg CV; Bowers KE; Matthews CR
Protein Sci; 1997 Sep; 6(9):1885-92. PubMed ID: 9300488
[TBL] [Abstract][Full Text] [Related]
7. Refolding of [6-19F]tryptophan-labeled Escherichia coli dihydrofolate reductase in the presence of ligand: a stopped-flow NMR spectroscopy study.
Hoeltzli SD; Frieden C
Biochemistry; 1998 Jan; 37(1):387-98. PubMed ID: 9425060
[TBL] [Abstract][Full Text] [Related]
8. Molecular dissection of the folding mechanism of the alpha subunit of tryptophan synthase: an amino-terminal autonomous folding unit controls several rate-limiting steps in the folding of a single domain protein.
Zitzewitz JA; Matthews CR
Biochemistry; 1999 Aug; 38(31):10205-14. PubMed ID: 10433729
[TBL] [Abstract][Full Text] [Related]
9. Real-time refolding studies of 6-19F-tryptophan labeled Escherichia coli dihydrofolate reductase using stopped-flow NMR spectroscopy.
Hoeltzli SD; Frieden C
Biochemistry; 1996 Dec; 35(51):16843-51. PubMed ID: 8988023
[TBL] [Abstract][Full Text] [Related]
10. Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structure.
Protasova NYu ; Kireeva ML; Murzina NV; Murzin AG; Uversky VN; Gryaznova OI; Gudkov AT
Protein Eng; 1994 Nov; 7(11):1373-7. PubMed ID: 7700869
[TBL] [Abstract][Full Text] [Related]
11. GroEL-mediated folding of structurally homologous dihydrofolate reductases.
Clark AC; Frieden C
J Mol Biol; 1997 May; 268(2):512-25. PubMed ID: 9159487
[TBL] [Abstract][Full Text] [Related]
12. Crystal structures of Escherichia coli dihydrofolate reductase complexed with 5-formyltetrahydrofolate (folinic acid) in two space groups: evidence for enolization of pteridine O4.
Lee H; Reyes VM; Kraut J
Biochemistry; 1996 Jun; 35(22):7012-20. PubMed ID: 8679526
[TBL] [Abstract][Full Text] [Related]
13. Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands.
Uversky VN; Kutyshenko VP; Protasova NYu ; Rogov VV; Vassilenko KS; Gudkov AT
Protein Sci; 1996 Sep; 5(9):1844-51. PubMed ID: 8880908
[TBL] [Abstract][Full Text] [Related]
14. Native Escherichia coli and murine dihydrofolate reductases contain late-folding non-native structures.
Clark AC; Frieden C
J Mol Biol; 1999 Jan; 285(4):1765-76. PubMed ID: 9917410
[TBL] [Abstract][Full Text] [Related]
15. Cyclophilin-promoted folding of mouse dihydrofolate reductase does not include the slow conversion of the late-folding intermediate to the active enzyme.
von Ahsen O; Lim JH; Caspers P; Martin F; Schönfeld HJ; Rassow J; Pfanner N
J Mol Biol; 2000 Mar; 297(3):809-18. PubMed ID: 10731431
[TBL] [Abstract][Full Text] [Related]
16. Effects of mutation at methionine-42 of Escherichia coli dihydrofolate reductase on stability and function: implication of hydrophobic interactions.
Ohmae E; Fukumizu Y; Iwakura M; Gekko K
J Biochem; 2005 May; 137(5):643-52. PubMed ID: 15944418
[TBL] [Abstract][Full Text] [Related]
17. Effects of five-tryptophan mutations on structure, stability and function of Escherichia coli dihydrofolate reductase.
Ohmae E; Sasaki Y; Gekko K
J Biochem; 2001 Sep; 130(3):439-47. PubMed ID: 11530021
[TBL] [Abstract][Full Text] [Related]
18. The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli.
Svensson AK; Zitzewitz JA; Matthews CR; Smith VF
Protein Eng Des Sel; 2006 Apr; 19(4):175-85. PubMed ID: 16452118
[TBL] [Abstract][Full Text] [Related]
19. Effects of the difference in the unfolded-state ensemble on the folding of Escherichia coli dihydrofolate reductase.
Arai M; Kataoka M; Kuwajima K; Matthews CR; Iwakura M
J Mol Biol; 2003 Jun; 329(4):779-91. PubMed ID: 12787677
[TBL] [Abstract][Full Text] [Related]
20. Acid and thermal unfolding of Escherichia coli dihydrofolate reductase.
Ohmae E; Kurumiya T; Makino S; Gekko K
J Biochem; 1996 Nov; 120(5):946-53. PubMed ID: 8982861
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]