Martha L. Ludwig

University of Michigan, Ann Arbor, Ann Arbor, MI 
structural biology
"Martha L. Ludwig"

(1931 - 2006)

Mean distance: 7.28
Cross-listing: MichiganTree

BETA: Related publications


You can help our author matching system! If you notice any publications incorrectly attributed to this author, please sign in and mark matches as correct or incorrect.

Birkeland AC, Ludwig ML, Meraj TS, et al. (2015) The Tip of the Iceberg: Clinical Implications of Genomic Sequencing Projects in Head and Neck Cancer. Cancers. 7: 2094-109
Beutlich J, Hammerl JA, Appel B, et al. (2015) Characterization of illegal food items and identification of foodborne pathogens brought into the European Union via two major German airports. International Journal of Food Microbiology. 209: 13-9
Datta S, Koutmos M, Pattridge KA, et al. (2008) 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
Koutmos M, Pejchal R, Bomer TM, et al. (2008) 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
Huang S, Romanchuk G, Pattridge K, et al. (2007) 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
Pejchal R, Campbell E, Guenther BD, et al. (2006) Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation. Biochemistry. 45: 4808-18
Pejchal R, Sargeant R, Ludwig ML. (2005) 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
Pejchal R, Ludwig ML. (2005) Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication. Plos Biology. 3: e31
Castro C, Gratson AA, Evans JC, et al. (2004) Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis. Biochemistry. 43: 5341-51
Evans JC, Huddler DP, Hilgers MT, et al. (2004) 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
See more...