93 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
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  1
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  1
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  1
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  1
2005 Pejchal R, Sargeant R, Ludwig ML. Structures of NADH and CH3-H4folate complexes of Escherichia coli methylenetetrahydrofolate reductase reveal a spartan strategy for a ping-pong reaction. Biochemistry. 44: 11447-57. PMID 16114881 DOI: 10.1021/bi050533q  1
2005 Pejchal R, Ludwig ML. Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication. Plos Biology. 3: e31. PMID 15630480 DOI: 10.1371/journal.pbio.0030031  1
2004 Castro C, Gratson AA, Evans JC, Jiracek J, Collinsová M, Ludwig ML, Garrow TA. Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis. Biochemistry. 43: 5341-51. PMID 15122900 DOI: 10.1021/bi049821x  1
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  1
2003 Pattridge KA, Weber CH, Friesen JA, Sanker S, Kent C, Ludwig ML. Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis. The Journal of Biological Chemistry. 278: 51863-71. PMID 14506262 DOI: 10.1074/jbc.M306174200  1
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  1
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  1
2002 Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML. Betaine-homocysteine methyltransferase: zinc in a distorted barrel. Structure (London, England : 1993). 10: 1159-71. PMID 12220488 DOI: 10.1016/S0969-2126(02)00796-7  1
2002 Ludwig ML, Matthews RG. Effector regulation in a monomeric enzyme. Nature Structural Biology. 9: 236-8. PMID 11914727 DOI: 10.1038/nsb0402-236  1
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  1
2002 Ludwig ML, Matthews RG. B12-Dependent Methionine Synthase: A Structure That Adapts to Catalyze Multiple Methyl Transfer Reactions Acs Symposium Series. 827: 186-201.  1
2001 Hilgers MT, Ludwig ML. Crystal structure of the quorum-sensing protein LuxS reveals a catalytic metal site. Proceedings of the National Academy of Sciences of the United States of America. 98: 11169-74. PMID 11553770 DOI: 10.1073/pnas.191223098  1
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  1
2000 Williams CH, Arscott LD, Müller S, Lennon BW, Ludwig ML, Wang PF, Veine DM, Becker K, Schirmer RH. Thioredoxin reductase two modes of catalysis have evolved. European Journal of Biochemistry / Febs. 267: 6110-7. PMID 11012662 DOI: 10.1046/j.1432-1327.2000.01702.x  1
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  1
2000 Lennon BW, Williams CH, Ludwig ML. Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. Science (New York, N.Y.). 289: 1190-4. PMID 10947986 DOI: 10.1126/science.289.5482.1190  1
1999 Hoover DM, Drennan CL, Metzger AL, Osborne C, Weber CH, Pattridge KA, Ludwig ML. Comparisons of wild-type and mutant flavodoxins from Anacystis nidulans. Structural determinants of the redox potentials. Journal of Molecular Biology. 294: 725-43. PMID 10610792 DOI: 10.1006/jmbi.1999.3152  1
1999 Drennan CL, Pattridge KA, Weber CH, Metzger AL, Hoover DM, Ludwig ML. Refined structures of oxidized flavodoxin from Anacystis nidulans. Journal of Molecular Biology. 294: 711-24. PMID 10610791 DOI: 10.1006/jmbi.1999.3151  1
1999 Lennon BW, Williams CH, Ludwig ML. Crystal structure of reduced thioredoxin reductase from Escherichia coli: structural flexibility in the isoalloxazine ring of the flavin adenine dinucleotide cofactor. Protein Science : a Publication of the Protein Society. 8: 2366-79. PMID 10595539 DOI: 10.1110/ps.8.11.2366  1
1999 Weber CH, Park YS, Sanker S, Kent C, Ludwig ML. A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from bacillus subtilis. Structure (London, England : 1993). 7: 1113-24. PMID 10508782 DOI: 10.1016/S0969-2126(99)80178-6  1
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  1
1999 Ludwig ML, Marletta MA. A new decoration for nitric oxide synthase - a Zn(Cys)4 site. Structure (London, England : 1993). 7: R73-9. PMID 10198293 DOI: 10.1016/S0969-2126(99)80047-1  1
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  1
1998 Weber CH, Hark Y, Sankar S, Kent C, Ludwig M. The x-ray structure of CTP: Glycerol-3-phosphate cytidylyltransferase from bacillus subtilis Faseb Journal. 12: A1287.  1
1997 Hoover DM, Ludwig ML. A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution. Protein Science : a Publication of the Protein Society. 6: 2525-37. PMID 9416602 DOI: 10.1002/pro.5560061205  1
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  1
1997 Ludwig ML, Pattridge KA, Metzger AL, Dixon MM, Eren M, Feng Y, Swenson RP. Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes. Biochemistry. 36: 1259-80. PMID 9063874 DOI: 10.1021/bi962180o  1
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  1
1997 Hall PA, Hoover DM, Ludwig ML, Matthews RG. Interactions between escherichia coli flavodoxin and methionine synthase: The search for determinants of specificity Faseb Journal. 11: A1016.  1
1997 Sheppard CA, Jovette P, Frossr P, Rozen R, Guenlher B, Ludwig M, Matthews RG. Studies of a mutation in methylenetetrahydrofolate reductase. A risk factor for cardiovascular disease and neural tube defects Faseb Journal. 11: A1016.  1
1997 Guenther BD, Sheppard CA, Matthews RG, Ludwig M. The structure of methylenetetrahydrofolate reductase: A bacterial model for an enzyme involved in cardiac disease Faseb Journal. 11: A1021.  1
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  1
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  1
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  1
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  1
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  1
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  1
1996 Gatti DL, Entsch B, Ballou DP, Ludwig ML. pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis. Biochemistry. 35: 567-78. PMID 8555229 DOI: 10.1021/bi951344i  1
1996 Jarrett JT, Hoover DM, Drennan CL, Ludwig ML, Matthews BG. Protein residues control methylcobalamin reactivity in methionine synthase Faseb Journal. 10: A968.  1
1995 Tierney DL, Fee JA, Ludwig ML, Penner-Hahn JE. X-ray absorption spectroscopy of the iron site in Escherichia coli Fe(III) superoxide dismutase. Biochemistry. 34: 1661-8. PMID 7849025  1
1995 Lah MS, Dixon MM, Pattridge KA, Stallings WC, Fee JA, Ludwig ML. Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry. 34: 1646-60. PMID 7849024  1
1995 Gassner GT, Ludwig ML, Gatti DL, Correll CC, Ballou DP. Structure and mechanism of the iron-sulfur flavoprotein phthalate dioxygenase reductase. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 9: 1411-8. PMID 7589982  1
1994 Lah MS, Palfey BA, Schreuder HA, Ludwig ML. Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants. Biochemistry. 33: 1555-64. PMID 8312276  1
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  1
1994 Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML. The mobile flavin of 4-OH benzoate hydroxylase. Science (New York, N.Y.). 266: 110-4. PMID 7939628  1
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  1
1993 Wagner UG, Pattridge KA, Ludwig ML, Stallings WC, Werber MM, Oefner C, Frolow F, Sussman JL. Comparison of the crystal structures of genetically engineered human manganese superoxide dismutase and manganese superoxide dismutase from Thermus thermophilus: differences in dimer-dimer interaction. Protein Science : a Publication of the Protein Society. 2: 814-25. PMID 8495200 DOI: 10.1002/pro.5560020511  1
1993 Correll CC, Ludwig ML, Bruns CM, Karplus PA. Structural prototypes for an extended family of flavoprotein reductases: comparison of phthalate dioxygenase reductase with ferredoxin reductase and ferredoxin. Protein Science : a Publication of the Protein Society. 2: 2112-33. PMID 8298460 DOI: 10.1002/pro.5560021212  1
1992 Luschinsky CL, Drummond JT, Matthews RG, Ludwig ML. Crystallization and preliminary X-ray diffraction studies of the cobalamin-binding domain of methionine synthase from Escherichia coli. Journal of Molecular Biology. 225: 557-60. PMID 1593636 DOI: 10.1016/0022-2836(92)90940-L  1
1992 Correll CC, Batie CJ, Ballou DP, Ludwig ML. Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Science (New York, N.Y.). 258: 1604-10. PMID 1280857  1
1991 Stallings WC, Metzger AL, Pattridge KA, Fee JA, Ludwig ML. Structure-function relationships in iron and manganese superoxide dismutases. Free Radical Research Communications. 12: 259-68. PMID 2071033 DOI: 10.3109/10715769109145794  1
1991 Ludwig ML, Metzger AL, Pattridge KA, Stallings WC. Manganese superoxide dismutase from Thermus thermophilus. A structural model refined at 1.8 A resolution. Journal of Molecular Biology. 219: 335-58. PMID 2038060 DOI: 10.1016/0022-2836(91)90569-R  1
1990 Ludwig ML, Schopfer LM, Metzger AL, Pattridge KA, Massey V. Structure and oxidation-reduction behavior of 1-deaza-FMN flavodoxins: modulation of redox potentials in flavodoxins. Biochemistry. 29: 10364-75. PMID 2261478  1
1988 Carlioz A, Ludwig ML, Stallings WC, Fee JA, Steinman HM, Touati D. Iron superoxide dismutase. Nucleotide sequence of the gene from Escherichia coli K12 and correlations with crystal structures. The Journal of Biological Chemistry. 263: 1555-62. PMID 2447093  1
1985 Stallings WC, Pattridge KA, Strong RK, Ludwig ML. The structure of manganese superoxide dismutase from Thermus thermophilus HB8 at 2.4-A resolution. The Journal of Biological Chemistry. 260: 16424-32. PMID 4066716  1
1985 Correll CC, Batie CJ, Ballou DP, Ludwig ML. Crystallographic characterization of phthalate oxygenase reductase, an iron-sulfur flavoprotein from Pseudomonas cepacia. The Journal of Biological Chemistry. 260: 14633-5. PMID 2997216  1
1984 Ludwig ML, Weber LD, Ballou DP. Characterization of crystals of protocatechuate 3,4-dioxygenase from Pseudomonas cepacia. The Journal of Biological Chemistry. 259: 14840-2. PMID 6548751  1
1984 Stallings WC, Pattridge KA, Strong RK, Ludwig ML. Manganese and iron superoxide dismutases are structural homologs. The Journal of Biological Chemistry. 259: 10695-9. PMID 6381489  1
1983 Smith WW, Pattridge KA, Ludwig ML, Petsko GA, Tsernoglou D, Tanaka M, Yasunobu KT. Structure of oxidized flavodoxin from Anacystis nidulans. Journal of Molecular Biology. 165: 737-53. PMID 6406674 DOI: 10.1016/S0022-2836(83)80277-0  1
1983 Stallings WC, Powers TB, Pattridge KA, Fee JA, Ludwig ML. Iron superoxide dismutase from Escherichia coli at 3.1-A resolution: a structure unlike that of copper/zinc protein at both monomer and dimer levels. Proceedings of the National Academy of Sciences of the United States of America. 80: 3884-8. PMID 6346322  1
1983 Hille R, Yoshida T, Tarr GE, Williams CH, Ludwig ML, Fee JA, Kent TA, Huynh BH, Münck E. Studies of the ferredoxin from Thermus thermophilus. The Journal of Biological Chemistry. 258: 13008-13. PMID 6313685  1
1981 Shieh HS, Ghisla S, Hanson LK, Ludwig ML, Nordman CE. Molecular complex of lumiflavin and 2-aminobenzoic acid: crystal structure, crystal spectra, and solution properties. Biochemistry. 20: 4766-74. PMID 7295648  1
1981 Stallings WC, Pattridge KA, Powers TB, Fee JA, Ludwig ML. Characterization of crystals of tetrameric manganese superoxide dismutase from Thermus thermophilus HB8. The Journal of Biological Chemistry. 256: 5857-9. PMID 7240177  1
1979 Eriksson B, Ersson B, Kierkegaard P, Larsson LO, Skoglund U, Ludwig M, Yonetani T. A method for the preparation of heavy-atom derivatives of yeast cytochrome c peroxidase Journal of Molecular Biology. 127: 225-227. PMID 219200 DOI: 10.1016/0022-2836(79)90243-2  1
1978 Powers TB, Slykhouse TO, Fee JA, Ludwig ML. Characterization of an orthorhombic crystal form of iron-containing superoxide dismutase from Escherichia coli B. Journal of Molecular Biology. 123: 689-90. PMID 357744 DOI: 10.1016/0022-2836(78)90212-7  1
1977 Smith WW, Burnett RM, Darling GD, Ludwig ML. Structure of the semiquinone form of flavodoxin from Clostridum MP. Extension of 1.8 A resolution and some comparisons with the oxidized state. Journal of Molecular Biology. 117: 195-225. PMID 599565 DOI: 10.1016/0022-2836(77)90031-6  1
1975 Eaton WA, Hofrichter J, Makinen MW, Andersen RD, Ludwig ML. Optical spectra and electronic structure of flavine mononucleotide in flavodoxin crystals. Biochemistry. 14: 2146-51. PMID 1148163  1
1975 Smith WW, Entsch H, Ludwig ML, Nordman CE, Crespi HL. Crystallographic characterization of flavodoxin from Anacystis nidulans. Journal of Molecular Biology. 94: 123-6. PMID 806695 DOI: 10.1016/0022-2836(75)90409-X  1
1975 Mayhew SG, Ludwig ML. 2 Flavodoxins and Electron-Transferring Flavoproteins Enzymes. 12: 57-118. DOI: 10.1016/S1874-6047(08)60225-5  1
1974 Burnett RM, Darling GD, Kendall DS, LeQuesne ME, Mayhew SG, Smith WW, Ludwig ML. The structure of the oxidized form of clostridial flavodoxin at 1.9-A resolution. The Journal of Biological Chemistry. 249: 4383-92. PMID 4843141  1
1973 James TL, Ludwig ML, Cohn M. Dependence of the proton magnetic resonance spectra on the oxidation state of flavodoxin from Clostridium MP and from Peptostreptococcus elsdenii. Proceedings of the National Academy of Sciences of the United States of America. 70: 3292-5. PMID 4519623  1
1972 Hunter MJ, Ludwig ML. [54] amidination. Methods in Enzymology. 25: 585-96. PMID 23014443 DOI: 10.1016/S0076-6879(72)25058-3  1
1972 Andersen RD, Apgar PA, Burnett RM, Darling GD, Lequesne ME, Mayhew SG, Ludwig ML. Structure of the radical form of clostridial flavodoxin: a new molecular model. Proceedings of the National Academy of Sciences of the United States of America. 69: 3189-91. PMID 4508314  1
1972 Ludwig ML, Andersen RD, Apgar PA, Burnett RM, LeQuesne ME, Mayhew SG. The structure of a clostridial flavodoxin, an electron-transferring flavoprotein. 3. An interpretation of an electron-density map at a nominal resolution of 3.25 Angstrom. Cold Spring Harbor Symposia On Quantitative Biology. 36: 369-80. PMID 4508151  1
1972 Apgar PA, Ludwig ML. Crystal structure and absolute configuration of the hydrobromide salt of (-)-2-exo-aminonorbornane-2-carboxylic acid Journal of the American Chemical Society. 94: 964-967.  1
1969 Ludwig ML, Andersen RD, Mayhew SG, Massey V. The structure of a clostridial flavodoxin. I. Crystallographic characterization of the oxidized and semiquinone forms. The Journal of Biological Chemistry. 244: 6047-8. PMID 5350955  1
1968 Lipscomb WN, Hartsuck JA, Reeke GN, Quiocho FA, Bethge PH, Ludwig ML, Steitz TA, Muirhead H, Coppola JC. The structure of carboxypeptidase A. VII. The 2.0-angstrom resolution studies of the enzyme and of its complex with glycyltyrosine, and mechanistic deductions. Brookhaven Symposia in Biology. 21: 24-90. PMID 5719196  1
1967 Reeke GN, Hartsuck JA, Ludwig ML, Quiocho FA, Steitz TA, Lipscomb WN. The structure of carboxypeptidase a, vi. Some results at 2.0-a resolution, and the complex with glycyl-tyrosine at 2.8-a resolution. Proceedings of the National Academy of Sciences of the United States of America. 58: 2220-6. PMID 16591584 DOI: 10.1073/pnas.58.6.2220  1
1967 Steitz TA, Ludwig ML, Quiocho FA, Lipscomb WN. The structure of carboxypepidase A. V. Studies of enzyme-substrate and enzyme-inhibitor complexes at 6 A resolution. The Journal of Biological Chemistry. 242: 4662-8. PMID 6061411  1
1967 Ludwig ML, Hunter MJ. [73] Amidination Methods in Enzymology. 11: 595-604. DOI: 10.1016/S0076-6879(67)11076-8  1
1966 Lipscomb W, Coppola J, Hartsuck J, Ludwig M, Muirhead H, Searl J, Steitz T. The structure of carboxypeptidase A Journal of Molecular Biology. 19: 423-IN3. DOI: 10.1016/S0022-2836(66)80014-1  0.4
1965 Hartsuck JA, Ludwig ML, Muirhead H, Steitz TA, Lipscomb WN. CARBOXYPEPTIDASE A, II. THE THREE-DIMENSIONAL ELECTRON DENSITY MAP AT 6 A RESOLUTION. Proceedings of the National Academy of Sciences of the United States of America. 53: 396-403. PMID 16591261 DOI: 10.1073/pnas.53.2.396  1
1963 LUDWIG ML, PAUL IC, PAWLEY GS, LIPSCOMB WN. THE STRUCTURE OF CARBOXYPEPTIDASE A, I. A TWO-DIMENSIONAL SUPERPOSITION FUNCTION. Proceedings of the National Academy of Sciences of the United States of America. 50: 282-5. PMID 14060645  1
1963 Waugh DF, Ludwig ML, Gillespie JM, Melton B, Foley M, Kleiner ES. The αs-caseins of bovine milk Journal of the American Chemical Society. 84: 4929-4938.  1
1962 Ludwig ML, Byrne R. Reversible blocking of protein amino groups by the acetimidyl group [10] Journal of the American Chemical Society. 84: 4160-4162.  1
1962 Hunter MJ, Ludwig ML. The reaction of imidoesters with proteins and related small molecules Journal of the American Chemical Society. 84: 3491-3504.  1
1959 MELVILLE DB, LUDWIG ML, INAMINE E, RACHELE JR. Transmethylation in the biosynthesis of ergothionelne. The Journal of Biological Chemistry. 234: 1195-8. PMID 13654346  1
1957 MELVILLE DB, EICH S, LUDWIG ML. The biosynthesis of ergothioneine. The Journal of Biological Chemistry. 224: 871-7. PMID 13405916  1
1955 MELVILLE DB, HORNER WH, OTKEN CC, LUDWIG ML. Studies on the origin of ergothioneine in animals. The Journal of Biological Chemistry. 213: 61-8. PMID 14353906  1
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