| Year |
Citation |
Score |
| 2009 |
Matthews RG. Cobalamin- and corrinoid-dependent enzymes. Metal Ions in Life Sciences. 6: 53-114. PMID 20877792 DOI: 10.1039/Bk9781847559159-00053 |
0.424 |
|
| 2009 |
Koutmos M, Datta S, Pattridge KA, Smith JL, Matthews RG. Insights into the reactivation of cobalamin-dependent methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 106: 18527-32. PMID 19846791 DOI: 10.1073/Pnas.0906132106 |
0.377 |
|
| 2009 |
Liptak MD, Fleischhacker AS, Matthews RG, Telser J, Brunold TC. Spectroscopic and computational characterization of the base-off forms of cob(II)alamin. The Journal of Physical Chemistry. B. 113: 5245-54. PMID 19298066 DOI: 10.1021/Jp810136D |
0.73 |
|
| 2009 |
Hondorp ER, Matthews RG. Oxidation of cysteine 645 of cobalamin-independent methionine synthase causes a methionine limitation in Escherichia coli. Journal of Bacteriology. 191: 3407-10. PMID 19286805 DOI: 10.1128/Jb.01722-08 |
0.778 |
|
| 2008 |
Matthews RG, Koutmos M, Datta S. Cobalamin-dependent and cobamide-dependent methyltransferases. Current Opinion in Structural Biology. 18: 658-66. PMID 19059104 DOI: 10.1016/J.Sbi.2008.11.005 |
0.365 |
|
| 2008 |
Liptak MD, Datta S, Matthews RG, Brunold TC. Spectroscopic study of the cobalamin-dependent methionine synthase in the activation conformation: effects of the Y1139 residue and S-adenosylmethionine on the B12 cofactor. Journal of the American Chemical Society. 130: 16374-81. PMID 19006389 DOI: 10.1021/Ja8038129 |
0.442 |
|
| 2008 |
Datta S, Koutmos M, Pattridge KA, Ludwig ML, Matthews RG. A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor. Proceedings of the National Academy of Sciences of the United States of America. 105: 4115-20. PMID 18332423 DOI: 10.1073/Pnas.0800329105 |
0.45 |
|
| 2008 |
Koutmos M, Pejchal R, Bomer TM, Matthews RG, Smith JL, Ludwig ML. Metal active site elasticity linked to activation of homocysteine in methionine synthases. Proceedings of the National Academy of Sciences of the United States of America. 105: 3286-91. PMID 18296644 DOI: 10.1073/Pnas.0709960105 |
0.433 |
|
| 2007 |
Matthews RG, Elmore CL. Defects in homocysteine metabolism: diversity among hyperhomocyst(e)inemias. Clinical Chemistry and Laboratory Medicine : Cclm / Fescc. 45: 1700-3. PMID 17937607 DOI: 10.1515/Cclm.2007.324 |
0.347 |
|
| 2007 |
Fleischhacker AS, Matthews RG. Ligand trans influence governs conformation in cobalamin-dependent methionine synthase. Biochemistry. 46: 12382-92. PMID 17924667 DOI: 10.1021/Bi701367C |
0.775 |
|
| 2007 |
Huang S, Romanchuk G, Pattridge K, Lesley SA, Wilson IA, Matthews RG, Ludwig M. Reactivation of methionine synthase from Thermotoga maritima (TM0268) requires the downstream gene product TM0269. Protein Science : a Publication of the Protein Society. 16: 1588-95. PMID 17656578 DOI: 10.1110/Ps.072936307 |
0.368 |
|
| 2007 |
Liptak MD, Fleischhacker AS, Matthews RG, Brunold TC. Probing the role of the histidine 759 ligand in cobalamin-dependent methionine synthase. Biochemistry. 46: 8024-35. PMID 17567043 DOI: 10.1021/Bi700341Y |
0.758 |
|
| 2007 |
Elmore CL, Wu X, Leclerc D, Watson ED, Bottiglieri T, Krupenko NI, Krupenko SA, Cross JC, Rozen R, Gravel RA, Matthews RG. Metabolic derangement of methionine and folate metabolism in mice deficient in methionine synthase reductase. Molecular Genetics and Metabolism. 91: 85-97. PMID 17369066 DOI: 10.1016/J.Ymgme.2007.02.001 |
0.338 |
|
| 2007 |
Paul L, Mishra PK, Blumenthal RM, Matthews RG. Integration of regulatory signals through involvement of multiple global regulators: control of the Escherichia coli gltBDF operon by Lrp, IHF, Crp, and ArgR. Bmc Microbiology. 7: 2. PMID 17233899 DOI: 10.1186/1471-2180-7-2 |
0.338 |
|
| 2006 |
Hondorp ER, Matthews RG. Methionine. Ecosal Plus. 2. PMID 26443567 DOI: 10.1128/ecosalplus.3.6.1.7 |
0.788 |
|
| 2006 |
Chapman E, Farr GW, Usaite R, Furtak K, Fenton WA, Chaudhuri TK, Hondorp ER, Matthews RG, Wolf SG, Yates JR, Pypaert M, Horwich AL. Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL. Proceedings of the National Academy of Sciences of the United States of America. 103: 15800-5. PMID 17043235 DOI: 10.1073/Pnas.0607534103 |
0.762 |
|
| 2006 |
Taurog RE, Matthews RG. Activation of methyltetrahydrofolate by cobalamin-independent methionine synthase. Biochemistry. 45: 5092-102. PMID 16618098 DOI: 10.1021/Bi060052M |
0.762 |
|
| 2006 |
Taurog RE, Jakubowski H, Matthews RG. Synergistic, random sequential binding of substrates in cobalamin-independent methionine synthase. Biochemistry. 45: 5083-91. PMID 16618097 DOI: 10.1021/Bi060051U |
0.791 |
|
| 2006 |
Pejchal R, Campbell E, Guenther BD, Lennon BW, Matthews RG, Ludwig ML. Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation. Biochemistry. 45: 4808-18. PMID 16605249 DOI: 10.1021/Bi052294C |
0.402 |
|
| 2005 |
Yamada K, Strahler JR, Andrews PC, Matthews RG. Regulation of human methylenetetrahydrofolate reductase by phosphorylation. Proceedings of the National Academy of Sciences of the United States of America. 102: 10454-9. PMID 16024724 DOI: 10.1073/Pnas.0504786102 |
0.412 |
|
| 2004 |
Hondorp ER, Matthews RG. Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli. Plos Biology. 2: e336. PMID 15502870 DOI: 10.1371/Journal.Pbio.0020336 |
0.787 |
|
| 2004 |
Bandarian V, Matthews RG. Measurement of energetics of conformational change in cobalamin-dependent methionine synthase. Methods in Enzymology. 380: 152-69. PMID 15051336 DOI: 10.1016/S0076-6879(04)80007-7 |
0.599 |
|
| 2004 |
Evans JC, Huddler DP, Hilgers MT, Romanchuk G, Matthews RG, Ludwig ML. Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 101: 3729-36. PMID 14752199 DOI: 10.1073/Pnas.0308082100 |
0.364 |
|
| 2003 |
Dorweiler JS, Finke RG, Matthews RG. Cobalamin-dependent methionine synthase: probing the role of the axial base in catalysis of methyl transfer between methyltetrahydrofolate and exogenous cob(I)alamin or cob(I)inamide. Biochemistry. 42: 14653-62. PMID 14661978 DOI: 10.1021/Bi035525T |
0.417 |
|
| 2003 |
Bandarian V, Ludwig ML, Matthews RG. Factors modulating conformational equilibria in large modular proteins: a case study with cobalamin-dependent methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 100: 8156-63. PMID 12832615 DOI: 10.1073/Pnas.1133218100 |
0.684 |
|
| 2003 |
Penner-Hahn JE, Tobin D, Matthews RG, Fierke CA, Peariso K, Grahame DA, Garrow TA. Zinc catalyzed alkyl-transfer enzymes Journal of Inorganic Biochemistry. 96: 58. DOI: 10.1016/S0162-0134(03)80504-4 |
0.401 |
|
| 2003 |
Matthews RG, Smith AE, Zhou ZS, Taurog RE, Bandarian V, Evans JC, Ludwig M. Cobalamin-Dependent and Cobalamin-Independent Methionine Synthases: Are There Two Solutions to the Same Chemical Problem? Helvetica Chimica Acta. 86: 3939-3954. DOI: 10.1002/Hlca.200390329 |
0.763 |
|
| 2002 |
Tani TH, Khodursky A, Blumenthal RM, Brown PO, Matthews RG. Adaptation to famine: a family of stationary-phase genes revealed by microarray analysis. Proceedings of the National Academy of Sciences of the United States of America. 99: 13471-6. PMID 12374860 DOI: 10.1073/Pnas.212510999 |
0.744 |
|
| 2002 |
Matthews RG. Methylenetetrahydrofolate reductase: a common human polymorphism and its biochemical implications. Chemical Record (New York, N.Y.). 2: 4-12. PMID 11933257 DOI: 10.1002/Tcr.10006 |
0.302 |
|
| 2002 |
Ludwig ML, Matthews RG. Effector regulation in a monomeric enzyme. Nature Structural Biology. 9: 236-8. PMID 11914727 DOI: 10.1038/Nsb0402-236 |
0.349 |
|
| 2002 |
Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML. Domain alternation switches B(12)-dependent methionine synthase to the activation conformation. Nature Structural Biology. 9: 53-6. PMID 11731805 DOI: 10.1038/Nsb738 |
0.651 |
|
| 2001 |
Yamada K, Chen Z, Rozen R, Matthews RG. Effects of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase. Proceedings of the National Academy of Sciences of the United States of America. 98: 14853-8. PMID 11742092 DOI: 10.1073/Pnas.261469998 |
0.379 |
|
| 2001 |
Matthews RG. Cobalamin-dependent methyltransferases. Accounts of Chemical Research. 34: 681-9. PMID 11513576 DOI: 10.1021/Ar0000051 |
0.352 |
|
| 2001 |
Hall DA, Vander Kooi CW, Stasik CN, Stevens SY, Zuiderweg ER, Matthews RG. Mapping the interactions between flavodoxin and its physiological partners flavodoxin reductase and cobalamin-dependent methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 98: 9521-6. PMID 11493691 DOI: 10.1073/Pnas.171168898 |
0.398 |
|
| 2001 |
Paul L, Blumenthal RM, Matthews RG. Activation from a distance: roles of Lrp and integration host factor in transcriptional activation of gltBDF. Journal of Bacteriology. 183: 3910-8. PMID 11395454 DOI: 10.1128/Jb.183.13.3910-3918.2001 |
0.323 |
|
| 2001 |
Trimmer EE, Ballou DP, Ludwig ML, Matthews RG. Folate activation and catalysis in methylenetetrahydrofolate reductase from Escherichia coli: roles for aspartate 120 and glutamate 28. Biochemistry. 40: 6216-26. PMID 11371182 DOI: 10.1021/Bi002790V |
0.417 |
|
| 2001 |
Trimmer EE, Ballou DP, Matthews RG. Methylenetetrahydrofolate reductase from Escherichia coli: elucidation of the kinetic mechanism by steady-state and rapid-reaction studies. Biochemistry. 40: 6205-15. PMID 11371181 DOI: 10.1021/Bi002789W |
0.378 |
|
| 2001 |
Bandarian V, Matthews RG. Quantitation of rate enhancements attained by the binding of cobalamin to methionine synthase. Biochemistry. 40: 5056-64. PMID 11305922 DOI: 10.1021/Bi002801K |
0.665 |
|
| 2001 |
Peariso K, Zhou ZS, Smith AE, Matthews RG, Penner-Hahn JE. Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy. Biochemistry. 40: 987-93. PMID 11170420 DOI: 10.1021/Bi001711C |
0.363 |
|
| 2000 |
Smith AE, Matthews RG. Protonation state of methyltetrahydrofolate in a binary complex with cobalamin-dependent methionine synthase. Biochemistry. 39: 13880-90. PMID 11076529 DOI: 10.1021/Bi001431X |
0.369 |
|
| 2000 |
Hall DA, Jordan-Starck TC, Loo RO, Ludwig ML, Matthews RG. Interaction of flavodoxin with cobalamin-dependent methionine synthase. Biochemistry. 39: 10711-9. PMID 10978155 DOI: 10.1021/Bi001096C |
0.45 |
|
| 2000 |
Zhou ZS, Smith AE, Peariso K, Penner-Hahn JE, Matthews RG. METHYL TRANSFERS TO THIOLS: THE ROLE OF ZINC Biochemical Society Transactions. 28: A123-A123. DOI: 10.1042/Bst028A123A |
0.312 |
|
| 1999 |
Zhou ZS, Peariso K, Penner-Hahn JE, Matthews RG. Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli. Biochemistry. 38: 15915-26. PMID 10625458 DOI: 10.1021/Bi992062B |
0.408 |
|
| 1999 |
Matthews RG. Response from Matthews. Trends in Microbiology. 7: 399. PMID 10498947 DOI: 10.1016/S0966-842X(99)01585-1 |
0.303 |
|
| 1999 |
VanBogelen RA, Greis KD, Blumenthal RM, Tani TH, Matthews RG. Mapping regulatory networks in microbial cells. Trends in Microbiology. 7: 320-8. PMID 10431205 DOI: 10.1016/S0966-842X(99)01540-1 |
0.74 |
|
| 1999 |
Guenther BD, Sheppard CA, Tran P, Rozen R, Matthews RG, Ludwig ML. The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nature Structural Biology. 6: 359-65. PMID 10201405 DOI: 10.1038/7594 |
0.332 |
|
| 1999 |
Sheppard CA, Trimmer EE, Matthews RG. Purification and properties of NADH-dependent 5, 10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli. Journal of Bacteriology. 181: 718-25. PMID 9922232 DOI: 10.1128/Jb.181.3.718-725.1999 |
0.467 |
|
| 1998 |
Matthews RG, Drummond JT, Webb HK. Cobalamin-dependent methionine synthase and serine hydroxymethyltransferase: targets for chemotherapeutic intervention? Advances in Enzyme Regulation. 38: 377-92. PMID 9762364 DOI: 10.1016/S0065-2571(97)00006-X |
0.313 |
|
| 1998 |
Jarrett JT, Hoover DM, Ludwig ML, Matthews RG. The mechanism of adenosylmethionine-dependent activation of methionine synthase: a rapid kinetic analysis of intermediates in reductive methylation of Cob(II)alamin enzyme. Biochemistry. 37: 12649-58. PMID 9730838 DOI: 10.1021/Bi9808565 |
0.46 |
|
| 1998 |
Matthews RG, Sheppard C, Goulding C. Methylenetetrahydrofolate reductase and methionine synthase: biochemistry and molecular biology. European Journal of Pediatrics. 157: S54-9. PMID 9587027 DOI: 10.1007/Pl00014305 |
0.669 |
|
| 1998 |
Jarrett JT, Huang S, Matthews RG. Methionine synthase exists in two distinct conformations that differ in reactivity toward methyltetrahydrofolate, adenosylmethionine, and flavodoxin. Biochemistry. 37: 5372-82. PMID 9548919 DOI: 10.1021/Bi9730893 |
0.484 |
|
| 1998 |
Peariso K, Goulding CW, Huang S, Matthews RG, Penner-Hahn JE. Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: The role of zinc in the methylation of homocysteine Journal of the American Chemical Society. 120: 8410-8416. DOI: 10.1021/Ja980581G |
0.67 |
|
| 1997 |
Matthews RG, Goulding CW. Enzyme-catalyzed methyl transfers to thiols: the role of zinc. Current Opinion in Chemical Biology. 1: 332-9. PMID 9667865 DOI: 10.1016/S1367-5931(97)80070-1 |
0.672 |
|
| 1997 |
Goulding CW, Matthews RG. Cobalamin-dependent methionine synthase from Escherichia coli: involvement of zinc in homocysteine activation. Biochemistry. 36: 15749-57. PMID 9398304 DOI: 10.1021/Bi971988L |
0.681 |
|
| 1997 |
Jarrett JT, Choi CY, Matthews RG. Changes in protonation associated with substrate binding and Cob(I)alamin formation in cobalamin-dependent methionine synthase. Biochemistry. 36: 15739-48. PMID 9398303 DOI: 10.1021/Bi971987T |
0.459 |
|
| 1997 |
Jarrett JT, Goulding CW, Fluhr K, Huang S, Matthews RG. Purification and assay of cobalamin-dependent methionine synthase from Escherichia coli. Methods in Enzymology. 281: 196-213. PMID 9250984 DOI: 10.1016/S0076-6879(97)81026-9 |
0.802 |
|
| 1997 |
Ludwig ML, Matthews RG. Structure-based perspectives on B12-dependent enzymes. Annual Review of Biochemistry. 66: 269-313. PMID 9242908 DOI: 10.1146/Annurev.Biochem.66.1.269 |
0.432 |
|
| 1997 |
Wiese DE, Ernsting BR, Blumenthal RM, Matthews RG. A nucleoprotein activation complex between the leucine-responsive regulatory protein and DNA upstream of the gltBDF operon in Escherichia coli. Journal of Molecular Biology. 270: 152-68. PMID 9236118 DOI: 10.1006/Jmbi.1997.1057 |
0.349 |
|
| 1997 |
Goulding CW, Postigo D, Matthews RG. Cobalamin-dependent methionine synthase is a modular protein with distinct regions for binding homocysteine, methyltetrahydrofolate, cobalamin, and adenosylmethionine. Biochemistry. 36: 8082-91. PMID 9201956 DOI: 10.1021/Bi9705164 |
0.678 |
|
| 1997 |
Hoover DM, Jarrett JT, Sands RH, Dunham WR, Ludwig ML, Matthews RG. 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. Biochemistry. 36: 127-38. PMID 8993326 DOI: 10.1021/Bi961693S |
0.455 |
|
| 1997 |
Fluhr K, Huang S, Matthews RG. Activation and deactivation of cob alamin-dependent methionine synthase Faseb Journal. 11: A896. |
0.771 |
|
| 1997 |
González JC, Goulding CW, Jarrett JT, Peariso K, Penner-Hahn JE, Matthews RG. Methionine synthase: Two unrelated enzymes with the same function Protein Engineering. 10: 57. |
0.627 |
|
| 1996 |
Dixon MM, Huang S, Matthews RG, Ludwig M. The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12. Structure (London, England : 1993). 4: 1263-75. PMID 8939751 DOI: 10.1016/S0969-2126(96)00135-9 |
0.449 |
|
| 1996 |
Jarrett JT, Drennan CL, Amaratunga M, Scholten JD, Ludwig ML, Matthews RG. A protein radical cage slows photolysis of methylcobalamin in methionine synthase from Escherichia coli. Bioorganic & Medicinal Chemistry. 4: 1237-46. PMID 8879545 DOI: 10.1016/0968-0896(96)00119-8 |
0.468 |
|
| 1996 |
González JC, Peariso K, Penner-Hahn JE, Matthews RG. Cobalamin-independent methionine synthase from Escherichia coli: a zinc metalloenzyme. Biochemistry. 35: 12228-34. PMID 8823155 DOI: 10.1021/Bi9615452 |
0.421 |
|
| 1996 |
Ludwig ML, Drennan CL, Matthews RG. The reactivity of B12 cofactors: the proteins make a difference. Structure (London, England : 1993). 4: 505-12. PMID 8736549 DOI: 10.1016/S0969-2126(96)00056-1 |
0.379 |
|
| 1996 |
Jarrett JT, Amaratunga M, Drennan CL, Scholten JD, Sands RH, Ludwig ML, Matthews RG. Mutations in the B12-binding region of methionine synthase: how the protein controls methylcobalamin reactivity. Biochemistry. 35: 2464-75. PMID 8652590 DOI: 10.1021/Bi952389M |
0.435 |
|
| 1996 |
Amaratunga M, Fluhr K, Jarrett JT, Drennan CL, Ludwig ML, Matthews RG, Scholten JD. A synthetic module for the metH gene permits facile mutagenesis of the cobalamin-binding region of Escherichia coli methionine synthase: initial characterization of seven mutant proteins. Biochemistry. 35: 2453-63. PMID 8652589 DOI: 10.1021/Bi952388U |
0.787 |
|
| 1996 |
Drennan CL, Matthews RG, Rosenblatt DS, Ledley FD, Fenton WA, Ludwig ML. Molecular basis for dysfunction of some mutant forms of methylmalonyl-CoA mutase: deductions from the structure of methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 93: 5550-5. PMID 8643613 DOI: 10.1073/Pnas.93.11.5550 |
0.374 |
|
| 1996 |
Fluhr K, Sholten JD, Matthews RG. Use of a synthetic dna module to generate mutations in the adomet-binding region of cobalamin-dependent methionine synthase Faseb Journal. 10: A969. |
0.759 |
|
| 1995 |
Drummond JT, Jarrett J, González JC, Huang S, Matthews RG. Characterization of nonradioactive assays for cobalamin-dependent and cobalamin-independent methionine synthase enzymes. Analytical Biochemistry. 228: 323-9. PMID 8572314 DOI: 10.1006/Abio.1995.1358 |
0.421 |
|
| 1995 |
Lipman RS, Bailey SW, Jarrett JT, Matthews RG, Jorns MS. Stereospecificity of folate binding to DNA photolyase from Escherichia coli. Biochemistry. 34: 11217-20. PMID 7669779 DOI: 10.1021/Bi00035A030 |
0.374 |
|
| 1995 |
Frosst P, Blom HJ, Milos R, Goyette P, Sheppard CA, Matthews RG, Boers GJ, den Heijer M, Kluijtmans LA, van den Heuvel LP. A candidate genetic risk factor for vascular disease: a common mutation in methylenetetrahydrofolate reductase. Nature Genetics. 10: 111-3. PMID 7647779 DOI: 10.1038/Ng0595-111 |
0.31 |
|
| 1995 |
Webb HK, Matthews RG. 4-Chlorothreonine is substrate, mechanistic probe, and mechanism-based inactivator of serine hydroxymethyltransferase. The Journal of Biological Chemistry. 270: 17204-9. PMID 7615518 DOI: 10.1074/Jbc.270.29.17204 |
0.377 |
|
| 1995 |
Eichel J, González JC, Hotze M, Matthews RG, Schröder J. Vitamin-B12-independent methionine synthase from a higher plant (Catharanthus roseus). Molecular characterization, regulation, heterologous expression, and enzyme properties. European Journal of Biochemistry / Febs. 230: 1053-8. PMID 7601135 DOI: 10.1111/J.1432-1033.1995.Tb20655.X |
0.405 |
|
| 1995 |
Eichel J, González JC, Hotze M, Matthews RG, Schröder J. Vitamin‐B12‐Independent Methionine Synthase from a Higher Plant (Catharanthus Roseus) Febs Journal. 230: 1053-1058. DOI: 10.1111/J.1432-1033.1995.1053G.X |
0.392 |
|
| 1994 |
Drummond JT, Matthews RG. Nitrous oxide inactivation of cobalamin-dependent methionine synthase from Escherichia coli: characterization of the damage to the enzyme and prosthetic group. Biochemistry. 33: 3742-50. PMID 8142374 DOI: 10.1021/Bi00178A034 |
0.452 |
|
| 1994 |
Drummond JT, Matthews RG. Nitrous oxide degradation by cobalamin-dependent methionine synthase: characterization of the reactants and products in the inactivation reaction. Biochemistry. 33: 3732-41. PMID 8142373 DOI: 10.1021/Bi00178A033 |
0.443 |
|
| 1994 |
Drennan CL, Huang S, Drummond JT, Matthews RG, Lidwig ML. How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase. Science (New York, N.Y.). 266: 1669-74. PMID 7992050 DOI: 10.1126/Science.7992050 |
0.359 |
|
| 1994 |
Goyette P, Sumner JS, Milos R, Duncan AM, Rosenblatt DS, Matthews RG, Rozen R. Human methylenetetrahydrofolate reductase: isolation of cDNA, mapping and mutation identification. Nature Genetics. 7: 195-200. PMID 7920641 DOI: 10.1038/Ng0694-195 |
0.313 |
|
| 1994 |
Drennan CL, Matthews RG, Ludwig ML. Cobalamin-dependent methionine synthase: the structure of a methylcobalamin-binding fragment and implications for other B12-dependent enzymes. Current Opinion in Structural Biology. 4: 919-29. PMID 7712296 DOI: 10.1016/0959-440X(94)90275-5 |
0.423 |
|
| 1993 |
Drummond JT, Huang S, Blumenthal RM, Matthews RG. Assignment of enzymatic function to specific protein regions of cobalamin-dependent methionine synthase from Escherichia coli. Biochemistry. 32: 9290-5. PMID 8369297 DOI: 10.1021/Bi00087A005 |
0.487 |
|
| 1993 |
Drummond JT, Loo RR, Matthews RG. Electrospray mass spectrometric analysis of the domains of a large enzyme: observation of the occupied cobalamin-binding domain and redefinition of the carboxyl terminus of methionine synthase. Biochemistry. 32: 9282-9. PMID 8369296 DOI: 10.1021/Bi00087A004 |
0.342 |
|
| 1993 |
Drummond JT, Matthews RG. Cobalamin-dependent and cobalamin-independent methionine synthases in Escherichia coli: two solutions to the same chemical problem. Advances in Experimental Medicine and Biology. 338: 687-92. PMID 8304207 DOI: 10.1007/978-1-4615-2960-6_142 |
0.439 |
|
| 1993 |
Bianchi V, Eliasson R, Fontecave M, Mulliez E, Hoover DM, Matthews RG, Reichard P. Flavodoxin is required for the activation of the anaerobic ribonucleotide reductase. Biochemical and Biophysical Research Communications. 197: 792-7. PMID 8267617 DOI: 10.1006/Bbrc.1993.2548 |
0.369 |
|
| 1993 |
Ernsting BR, Denninger JW, Blumenthal RM, Matthews RG. Regulation of the gltBDF operon of Escherichia coli: how is a leucine-insensitive operon regulated by the leucine-responsive regulatory protein? Journal of Bacteriology. 175: 7160-9. PMID 7901196 DOI: 10.1128/Jb.175.22.7160-7169.1993 |
0.323 |
|
| 1992 |
Ernsting BR, Atkinson MR, Ninfa AJ, Matthews RG. Characterization of the regulon controlled by the leucine-responsive regulatory protein in Escherichia coli. Journal of Bacteriology. 174: 1109-18. PMID 1346534 DOI: 10.1128/Jb.174.4.1109-1118.1992 |
0.373 |
|
| 1992 |
González JC, Banerjee RV, Huang S, Sumner JS, Matthews RG. Comparison of cobalamin-independent and cobalamin-dependent methionine synthases from Escherichia coli: two solutions to the same chemical problem. Biochemistry. 31: 6045-56. PMID 1339288 DOI: 10.1021/Bi00141A013 |
0.46 |
|
| 1992 |
Sumner JS, Matthews RG. Stereochemistry and mechanism of hydrogen transfer between NADPH and methylenetetrahydrofolate in the reaction catalyzed by methylenetetrahydrofolate reductase from pig liver Journal of the American Chemical Society. 114: 6949-6956. DOI: 10.1021/Ja00044A001 |
0.328 |
|
| 1991 |
Osborne C, Chen LM, Matthews RG. Isolation, cloning, mapping, and nucleotide sequencing of the gene encoding flavodoxin in Escherichia coli. Journal of Bacteriology. 173: 1729-37. PMID 1999390 DOI: 10.1128/Jb.173.5.1729-1737.1991 |
0.328 |
|
| 1990 |
Banerjee RV, Matthews RG. Cobalamin-dependent methionine synthase. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 4: 1450-9. PMID 2407589 DOI: 10.1096/Fasebj.4.5.2407589 |
0.414 |
|
| 1990 |
Banerjee RV, Frasca V, Ballou DP, Matthews RG. Participation of cob(I) alamin in the reaction catalyzed by methionine synthase from Escherichia coli: a steady-state and rapid reaction kinetic analysis. Biochemistry. 29: 11101-9. PMID 2271698 DOI: 10.1021/Bi00502A013 |
0.405 |
|
| 1990 |
Rohlman CE, Matthews RG. Role of purine biosynthetic intermediates in response to folate stress in Escherichia coli. Journal of Bacteriology. 172: 7200-10. PMID 2254281 DOI: 10.1128/Jb.172.12.7200-7210.1990 |
0.319 |
|
| 1990 |
Banerjee RV, Harder SR, Ragsdale SW, Matthews RG. Mechanism of reductive activation of cobalamin-dependent methionine synthase: an electron paramagnetic resonance spectroelectrochemical study. Biochemistry. 29: 1129-35. PMID 2157485 DOI: 10.1021/Bi00457A005 |
0.41 |
|
| 1990 |
Vanoni MA, Lee S, Floss HG, Matthews RG. Stereochemistry of reduction of methylenetetrahydrofolate to methyltetrahydrofolate catalyzed by pig liver methylenetetrahydrofolate reductase Journal of the American Chemical Society. 112: 3987-3992. DOI: 10.1021/Ja00166A040 |
0.341 |
|
| 1990 |
Matthews RG, Drummond JT. Providing one-carbon units for biological methylations: Mechanistic studies on serine hydroxymethyltransferase, methylenetetrahydrofolate reductase, and methyltetrahydrofolate-homocysteine methyltransferase Chemical Reviews. 90: 1275-1290. DOI: 10.1021/Cr00105A010 |
0.416 |
|
| 1989 |
Matthews RG. Enzyme chemistry: mechanistic principles of enzyme activity. Science (New York, N.Y.). 246: 1064-5. PMID 17806400 DOI: 10.1126/Science.246.4933.1064 |
0.399 |
|
| 1988 |
Green JM, Ballou DP, Matthews RG. Examination of the role of methylenetetrahydrofolate reductase in incorporation of methyltetrahydrofolate into cellular metabolism Faseb Journal. 2: 42-47. PMID 3335280 DOI: 10.1096/Fasebj.2.1.3335280 |
0.372 |
|
| 1988 |
Green JM, MacKenzie RE, Matthews RG. Substrate flux through methylenetetrahydrofolate dehydrogenase: Predicted effects of the concentration of methylenetetrahydrofolate on its partitioning into pathways leading to nucleotide biosynthesis or methionine regeneration Biochemistry. 27: 8014-8022. PMID 3266075 DOI: 10.1021/Bi00421A007 |
0.374 |
|
| 1988 |
Frasca V, Banerjee RV, Dunham WR, Sands RH, Matthews RG. Cobalamin-dependent methionine synthase from Escherichia coli B: Electron paramagnetic resonance spectra of the inactive form and the active methylated form of the enzyme Biochemistry. 27: 8458-8465. PMID 2853966 DOI: 10.1021/Bi00422A025 |
0.446 |
|
| 1987 |
Matthews RG, Ghose C, Green JM, Matthews KD, Dunlap RB. Folylpolyglutamates as substrates and inhibitors of folate-dependent enzymes. Advances in Enzyme Regulation. 26: 157-71. PMID 2445177 DOI: 10.1016/0065-2571(87)90012-4 |
0.417 |
|
| 1986 |
Sumner J, Jencks DA, Khani S, Matthews RG. Photoaffinity labeling of methylenetetrahydrofolate reductase with 8-azido-S-adenosylmethionine Journal of Biological Chemistry. 261: 7697-7700. PMID 3754872 |
0.313 |
|
| 1986 |
Matthews RG. Methylenetetrahydrofolate reductase from pig liver Methods in Enzymology. 372-381. PMID 3702701 DOI: 10.1016/0076-6879(86)22196-5 |
0.405 |
|
| 1986 |
Frasca V, Stephenson Riazzi B, Matthews RG. In vitro inactivation of methionine synthase by nitrous oxide Journal of Biological Chemistry. 261: 15823-15826. PMID 3536916 |
0.351 |
|
| 1986 |
Zydowsky TM, Courtney LF, Frasca V, Kobayashi K, Shimizu H, Yuen LD, Matthews RG, Benkovic SJ, Floss HG. Stereochemical analysis of the methyl transfer catalyzed by cobalamin-dependent methionine synthase from Escherichia coli B Journal of the American Chemical Society. 108: 3152-3153. DOI: 10.1021/ja00271a081 |
0.448 |
|
| 1985 |
Klinman JP, Matthews RG. Calculation of substrate dissociation constants from steady-state isotope effects in enzyme-catalyzed reactions Journal of the American Chemical Society. 107: 1058-1060. DOI: 10.1002/Chin.198527085 |
0.368 |
|
| 1984 |
Ross J, Green J, Baugh CM, MacKenzie RE, Matthews RG. Studies on the polyglutamate specificity of methylenetetrahydrofolate dehydrogenase from pig liver Biochemistry. 23: 1796-1801. PMID 6609718 DOI: 10.1021/Bi00303A033 |
0.431 |
|
| 1984 |
Vanoni MA, Matthews RG. Kinetic isotope effects on the oxidation of reduced nicotinamide adenine dinucleotide phosphate by the flavoprotein methylenetetrahydrofolate reductase Biochemistry. 23: 5272-5279. PMID 6391540 DOI: 10.1021/Bi00317A027 |
0.367 |
|
| 1984 |
Lu YZ, Aiello PD, Matthews RG. Studies on the polyglutamate specificity of thymidylate synthase from fetal pig liver Biochemistry. 23: 6870-6876. PMID 6085013 DOI: 10.1021/Bi00321A091 |
0.361 |
|
| 1983 |
Matthews RG, Ross J, Baugh CM, Cook JD, Davis L. The role of folylpolyglutamates in the regulation of folate metabolism Advances in Experimental Medicine and Biology. 163: 35-44. PMID 6604398 DOI: 10.1007/978-1-4757-5241-0_3 |
0.376 |
|
| 1982 |
Matthews RG, Daubner SC. Modulation of methylenetetrahydrofolate reductase activity by S-adenosylmethionine and by dihydrofolate and its polyglutamate analogues Advances in Enzyme Regulation. 20: 123-131. PMID 7051769 DOI: 10.1016/0065-2571(82)90012-7 |
0.734 |
|
| 1982 |
Daubner SC, Matthews RG. Purification and properties of methylenetetrahydrofolate reductase from pig liver Journal of Biological Chemistry. 257: 140-145. PMID 6975779 |
0.719 |
|
| 1982 |
Matthews RG. Studies on the methylene/methyl interconversion catalyzed by methylenetetrahydrofolate reductase from pig liver Biochemistry. 21: 4165-4171. PMID 6289874 DOI: 10.1021/Bi00260A038 |
0.322 |
|
| 1980 |
Matthews RG, Baugh CM. Interactions of pig liver methylenetetrahydrofolate reductase with methylenetetrahydropteroylpolyglutamate substrates and with dihydropteroylpolyglutamate inhibitors Biochemistry. 19: 2040-2045. PMID 6990970 DOI: 10.1021/Bi00551A005 |
0.367 |
|
| 1979 |
Thorpe C, Matthews RG, Williams CH. Acyl-coenzyme A dehydrogenase from pig kidney. Purification and properties. Biochemistry. 18: 331-7. PMID 570409 DOI: 10.1021/Bi00569A016 |
0.667 |
|
| 1979 |
Williams CH, Arscott LD, Matthews RG, Thorpe C, Wilkinson KD. Methodology employed for anaerobic spectrophotometric titrations and for computer-assisted data analysis. Methods in Enzymology. 62: 185-98. PMID 374972 DOI: 10.1016/0076-6879(79)62217-6 |
0.625 |
|
| 1979 |
Matthews RG, Ballou DP, Williams CH. Reactions of pig heart lipoamide dehydrogenase with pyridine nucleotides. Evidence for an effector role for bound oxidized pyridine nucleotide. The Journal of Biological Chemistry. 254: 4974-81. PMID 36378 |
0.586 |
|
| 1977 |
Matthews RG, Ballou DP, Thorpe C, Williams CH. Ion pair formation in pig heart lipoamide dehydrogenase: rationalization of pH profiles for reactivity of oxidized enzyme with dihydrolipoamide and 2-electron-reduced enzyme with lipoamide and iodoacetamide. The Journal of Biological Chemistry. 252: 3199-207. PMID 16887 |
0.627 |
|
| 1976 |
Matthews RG, Williams CH. Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart. The Journal of Biological Chemistry. 251: 3956-64. PMID 6467 |
0.628 |
|
| 1975 |
Matthews RG, Massey V, Sweeley CC. Identification of p-hydroxybenzaldehyde as the ligand in the green form of old yellow enzyme. The Journal of Biological Chemistry. 250: 9294-8. PMID 1194284 |
0.648 |
|
| 1974 |
Matthews RG, Arscott LD, Williams CH. Isolation, characterization and partial sequencing of cystine and thiol peptides of pig heart lipoamide dehydrogenase. Biochimica Et Biophysica Acta. 370: 26-38. PMID 4609485 DOI: 10.1016/0005-2744(74)90028-X |
0.622 |
|
| 1974 |
Matthews RG, Williams CH. Identification of the thiol residues involved in modifications of pig heart lipoamide dehydrogenase by cupric ion and by iodoacetamide. Biochimica Et Biophysica Acta. 370: 39-48. PMID 4371848 DOI: 10.1016/0005-2744(74)90029-1 |
0.666 |
|
| 1969 |
Massey V, Strickland S, Mayhew SG, Howell LG, Engel PC, Matthews RG, Schuman M, Sullivan PA. The production of superoxide anion radicals in the reaction of reduced flavins and flavoproteins with molecular oxygen. Biochemical and Biophysical Research Communications. 36: 891-7. PMID 5388670 DOI: 10.1016/0006-291X(69)90287-3 |
0.738 |
|
| 1969 |
Massey V, Müller F, Feldberg R, Schuman M, Sullivan PA, Howell LG, Mayhew SG, Matthews RG, Foust GP. The reactivity of flavoproteins with sulfite. Possible relevance to the problem of oxygen reactivity. The Journal of Biological Chemistry. 244: 3999-4006. PMID 4389773 |
0.555 |
|
| 1969 |
Matthews RG, Massey V. Isolation of old yellow enzyme in free and complexed forms. The Journal of Biological Chemistry. 244: 1779-86. PMID 4388613 |
0.636 |
|
| 1963 |
MATTHEWS RG, HUBBARD R, BROWN PK, WALD G. TAUTOMERIC FORMS OF METARHODOPSIN. The Journal of General Physiology. 47: 215-40. PMID 14080814 DOI: 10.1085/Jgp.47.2.215 |
0.509 |
|
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