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Journal Abstract Search

202 related items for PubMed ID: 10978155

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  • 3. Interaction of Escherichia coli cobalamin-dependent methionine synthase and its physiological partner flavodoxin: binding of flavodoxin leads to axial ligand dissociation from the cobalamin cofactor.
    Hoover DM, Jarrett JT, Sands RH, Dunham WR, Ludwig ML, Matthews RG.
    Biochemistry; 1997 Jan 07; 36(1):127-38. PubMed ID: 8993326
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  • 4. The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12.
    Dixon MM, Huang S, Matthews RG, Ludwig M.
    Structure; 1996 Nov 15; 4(11):1263-75. PubMed ID: 8939751
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  • 6. Nitrous oxide inactivation of cobalamin-dependent methionine synthase from Escherichia coli: characterization of the damage to the enzyme and prosthetic group.
    Drummond JT, Matthews RG.
    Biochemistry; 1994 Mar 29; 33(12):3742-50. PubMed ID: 8142374
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  • 7. Changes in protonation associated with substrate binding and Cob(I)alamin formation in cobalamin-dependent methionine synthase.
    Jarrett JT, Choi CY, Matthews RG.
    Biochemistry; 1997 Dec 16; 36(50):15739-48. PubMed ID: 9398303
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  • 9. Mapping the interactions between flavodoxin and its physiological partners flavodoxin reductase and cobalamin-dependent methionine synthase.
    Hall DA, Vander Kooi CW, Stasik CN, Stevens SY, Zuiderweg ER, Matthews RG.
    Proc Natl Acad Sci U S A; 2001 Aug 14; 98(17):9521-6. PubMed ID: 11493691
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  • 10. Assignment of enzymatic function to specific protein regions of cobalamin-dependent methionine synthase from Escherichia coli.
    Drummond JT, Huang S, Blumenthal RM, Matthews RG.
    Biochemistry; 1993 Sep 14; 32(36):9290-5. PubMed ID: 8369297
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  • 12. Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine.
    Goulding CW, Postigo D, Matthews RG.
    Biochemistry; 1997 Jul 01; 36(26):8082-91. PubMed ID: 9201956
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  • 16. Protonation state of methyltetrahydrofolate in a binary complex with cobalamin-dependent methionine synthase.
    Smith AE, Matthews RG.
    Biochemistry; 2000 Nov 14; 39(45):13880-90. PubMed ID: 11076529
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  • 17. A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor.
    Datta S, Koutmos M, Pattridge KA, Ludwig ML, Matthews RG.
    Proc Natl Acad Sci U S A; 2008 Mar 18; 105(11):4115-20. PubMed ID: 18332423
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  • 18. Ligand trans influence governs conformation in cobalamin-dependent methionine synthase.
    Fleischhacker AS, Matthews RG.
    Biochemistry; 2007 Oct 30; 46(43):12382-92. PubMed ID: 17924667
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  • 19. Domain alternation switches B(12)-dependent methionine synthase to the activation conformation.
    Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML.
    Nat Struct Biol; 2002 Jan 30; 9(1):53-6. PubMed ID: 11731805
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  • 20. Participation of cob(I) alamin in the reaction catalyzed by methionine synthase from Escherichia coli: a steady-state and rapid reaction kinetic analysis.
    Banerjee RV, Frasca V, Ballou DP, Matthews RG.
    Biochemistry; 1990 Dec 18; 29(50):11101-9. PubMed ID: 2271698
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