Audrey L. Lamb, PhD - Publications

Affiliations: 
Molecular Biosciences University of Kansas, Lawrence, KS, United States 
Area:
Iron uptake
Website:
http://www.molecularbiosciences.ku.edu/audrey-lamb

50 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
2020 Forbes D, Meneely KM, Chilton A, Lamb AL, Ellis HR. 3-His Metal Coordination Site Promotes the Coupling of Oxygen Activation to Cysteine Oxidation in Cysteine Dioxygenase. Biochemistry. PMID 32368901 DOI: 10.1021/acs.biochem.9b01085  1
2019 McFarlane JS, Zhang J, Wang S, Lei X, Moran GR, Lamb AL. Staphylopine and pseudopaline dehydrogenase from bacterial pathogens catalyze reversible reactions and produce stereospecific metallophores. The Journal of Biological Chemistry. PMID 31615895 DOI: 10.1074/jbc.RA119.011059  1
2019 McFarlane JS, Ronnebaum TA, Meneely KM, Chilton A, Fenton AW, Lamb AL. Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-π bond. Acta Crystallographica. Section F, Structural Biology Communications. 75: 461-469. PMID 31204694 DOI: 10.1107/S2053230X19007209  1
2019 Kenjić N, Hoag MR, Moraski GC, Caperelli CA, Moran GR, Lamb AL. PvdF of pyoverdin biosynthesis is a structurally unique N-formyltetrahydrofolate-dependent formyltransferase. Archives of Biochemistry and Biophysics. 664: 40-50. PMID 30689984 DOI: 10.1016/j.abb.2019.01.028  0.36
2018 Ronnebaum TA, McFarlane JS, Prisinzano TE, Booker SJ, Lamb AL. Stuffed Methyltransferase Catalyzes Penultimate Step of Pyochelin Biosynthesis. Biochemistry. PMID 30525512 DOI: 10.1021/acs.biochem.8b00716  1
2018 McFarlane JS, Hagen R, Chilton AS, Forbes D, Lamb A, Ellis HR. Not as easy as π: an insertional residue does not explain the π-helix gain-of-function in two component FMN reductases. Protein Science : a Publication of the Protein Society. PMID 30171650 DOI: 10.1002/pro.3504  1
2018 McFarlane JS, Davis CL, Lamb AL. Staphylopine, pseudopaline and yersinopine dehydrogenases: a structural and kinetic analysis of a new functional class of opine dehydrogenase. The Journal of Biological Chemistry. PMID 29618515 DOI: 10.1074/jbc.RA118.002007  1
2018 Ronnebaum TA, Lamb AL. Nonribosomal peptides for iron acquisition: pyochelin biosynthesis as a case study. Current Opinion in Structural Biology. 53: 1-11. PMID 29455106 DOI: 10.1016/j.sbi.2018.01.015  1
2017 McFarlane JS, Lamb AL. Biosynthesis of an Opine Metallophore by Pseudomonas aeruginosa. Biochemistry. PMID 29091735 DOI: 10.1021/acs.biochem.7b00804  1
2016 Beaupre BA, Roman JV, Hoag MR, Meneely KM, Silvaggi NR, Lamb AL, Moran GR. Ligand binding phenomena that pertain to the metabolic function of renalase. Archives of Biochemistry and Biophysics. PMID 27769837 DOI: 10.1016/j.abb.2016.10.011  1
2016 Meneely KM, Ronnebaum TA, Riley AP, Prisinzano TE, Lamb AL. Holo-structure and steady state kinetics of the thiazolinyl imine reductases for siderophore biosynthesis. Biochemistry. PMID 27601130 DOI: 10.1021/acs.biochem.6b00735  1
2016 Meneely KM, Sundlov JA, Gulick AM, Moran GR, Lamb AL. An Open and Shut Case: The Interaction of Magnesium with MST Enzymes. Journal of the American Chemical Society. PMID 27373320 DOI: 10.1021/jacs.6b05134  1
2015 Lamb AL, Kappock TJ, Silvaggi NR. You are lost without a map: Navigating the sea of protein structures. Biochimica Et Biophysica Acta. 1854: 258-68. PMID 25554228 DOI: 10.1016/j.bbapap.2014.12.021  0.36
2015 Lamb AL. Breaking a pathogen's iron will: Inhibiting siderophore production as an antimicrobial strategy Biochimica Et Biophysica Acta - Proteins and Proteomics. 1854: 1054-1070. DOI: 10.1016/j.bbapap.2015.05.001  1
2015 Lamb AL, Kappock TJ, Silvaggi NR. You are lost without a map: Navigating the sea of protein structures Biochimica Et Biophysica Acta - Proteins and Proteomics. 1854: 258-268. DOI: 10.1016/j.bbapap.2014.12.021  1
2014 Chilton AS, Ellis AL, Lamb AL. Structure of an Aspergillus fumigatus old yellow enzyme (EasA) involved in ergot alkaloid biosynthesis. Acta Crystallographica. Section F, Structural Biology Communications. 70: 1328-32. PMID 25286934 DOI: 10.1107/S2053230X14018962  1
2014 Meneely KM, Luo Q, Riley AP, Taylor B, Roy A, Stein RL, Prisinzano TE, Lamb AL. Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism. Bioorganic & Medicinal Chemistry. 22: 5961-9. PMID 25282647 DOI: 10.1016/j.bmc.2014.09.010  1
2014 Lothrop AP, Snider GW, Flemer S, Ruggles EL, Davidson RS, Lamb AL, Hondal RJ. Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis. Biochemistry. 53: 664-74. PMID 24490974 DOI: 10.1021/bi4007258  1
2014 Frederick RE, Ojha S, Lamb A, Dubois JL. How pH modulates the reactivity and selectivity of a siderophore-associated flavin monooxygenase. Biochemistry. 53: 2007-16. PMID 24490904 DOI: 10.1021/bi401256b  1
2013 Meneely KM, Luo Q, Lamb AL. Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities Archives of Biochemistry and Biophysics. 539: 70-80. PMID 24055536 DOI: 10.1016/j.abb.2013.09.007  1
2013 Meneely KM, Luo Q, Dhar P, Lamb AL. Lysine221 is the general base residue of the isochorismate synthase from Pseudomonas aeruginosa (PchA) in a reaction that is diffusion limited Archives of Biochemistry and Biophysics. 538: 49-56. PMID 23942051 DOI: 10.1016/j.abb.2013.07.026  1
2012 Meneely KM, Lamb AL. Two structures of a thiazolinyl imine reductase from yersinia enterocolitica provide insight into catalysis and binding to the nonribosomal peptide synthetase module of HMWP1 Biochemistry. 51: 9002-9013. PMID 23066849 DOI: 10.1021/bi3011016  1
2012 Olucha J, Meneely KM, Lamb AL. Modification of residue 42 of the active site loop with a lysine-mimetic side chain rescues isochorismate-pyruvate lyase activity in Pseudomonas aeruginosa PchB Biochemistry. 51: 7525-7532. PMID 22970849 DOI: 10.1021/bi300472n  1
2011 Olucha J, Lamb AL. Mechanistic and structural studies of the N-hydroxylating flavoprotein monooxygenases Bioorganic Chemistry. 39: 171-177. PMID 21871647 DOI: 10.1016/j.bioorg.2011.07.006  1
2011 Lamb AL. Pericyclic reactions catalyzed by chorismate-utilizing enzymes Biochemistry. 50: 7476-7483. PMID 21823653 DOI: 10.1021/bi2009739  1
2011 Olucha J, Meneely KM, Chilton AS, Lamb AL. Two structures of an N-hydroxylating flavoprotein monooxygenase: Ornithine hydroxylase from Pseudomonas aeruginosa Journal of Biological Chemistry. 286: 31789-31798. PMID 21757711 DOI: 10.1074/jbc.M111.265876  1
2011 Olucha J, Ouellette AN, Luo Q, Lamb AL. PH dependence of catalysis by pseudomonas aeruginosa isochorismate - Pyruvate lyase: Implications for transition state stabilization and the role of lysine 42 Biochemistry. 50: 7198-7207. PMID 21751784 DOI: 10.1021/bi200599j  1
2011 Luo Q, Meneely KM, Lamb AL. Entropic and enthalpic components of catalysis in the mutase and lyase activities of pseudomonas aeruginosa PchB Journal of the American Chemical Society. 133: 7229-7233. PMID 21504201 DOI: 10.1021/ja202091a  1
2009 Zaitseva J, Meneely KM, Lamb AL. Structure of escherichia coli malate dehydrogenase at 1.45 Å resolution Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65: 866-869. PMID 19724119 DOI: 10.1107/S1744309109032217  1
2009 Hickey JM, Hefty PS, Lamb AL. Expression, purification, crystallization and preliminary X-ray analysis of the DNA-binding domain of a Chlamydia trachomatis OmpR/PhoB-subfamily response regulator homolog, ChxR Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 65: 791-794. PMID 19652341 DOI: 10.1107/S1744309109025184  1
2009 Luo Q, Olucha J, Lamb AL. Structure-function analyses of isochorismate-pyruvate lyase from Pseudomonas aeruginosa suggest differing catalytic mechanisms for the two pericyclic reactions of this bifunctional enzyme Biochemistry. 48: 5239-5245. PMID 19432488 DOI: 10.1021/bi900456e  1
2009 Meneely KM, Barr EW, Bollinger JM, Lamb AL. Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. Biochemistry. 48: 4371-6. PMID 19368334 DOI: 10.1021/bi900442z  1
2009 Meneely KM, Barr EW, Bollinger JM, Lamb AL. Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. Biochemistry. 48: 4371-6. PMID 19368334 DOI: 10.1021/bi900442z  1
2007 Meneely KM, Lamb AL. Biochemical characterization of a flavin adenine dinculeotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism Biochemistry. 46: 11930-11937. PMID 17900176 DOI: 10.1021/bi700932q  1
2006 Zaitseva J, Lu J, Olechoski KL, Lamb AL. Two crystal structures of the isochorismate pyruvate lyase from Pseudomonas aeruginosa Journal of Biological Chemistry. 281: 33441-33449. PMID 16914555 DOI: 10.1074/jbc.M605470200  1
2001 Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nature Structural Biology. 8: 751-5. PMID 11524675 DOI: 10.1038/nsb0901-751  1
2001 Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC. Heterodimeric structure of superoxide dismutase in complex with its metallochaperone. Nature Structural Biology. 8: 751-5. PMID 11524675 DOI: 10.1038/nsb0901-751  1
2000 Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC. Heterodimer formation between superoxide dismutase and its copper chaperone. Biochemistry. 39: 14720-7. PMID 11101286 DOI: 10.1021/bi002207a  1
2000 Lamb AL, Torres AS, O'Halloran TV, Rosenzweig AC. Heterodimer formation between superoxide dismutase and its copper chaperone. Biochemistry. 39: 14720-7. PMID 11101286 DOI: 10.1021/bi002207a  1
2000 Wernimont AK, Huffman DL, Lamb AL, O'Halloran TV, Rosenzweig AC. Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nature Structural Biology. 7: 766-71. PMID 10966647 DOI: 10.1038/78999  1
2000 Wernimont AK, Huffman DL, Lamb AL, O'Halloran TV, Rosenzweig AC. Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nature Structural Biology. 7: 766-71. PMID 10966647 DOI: 10.1038/78999  1
2000 Lamb AL, Wernimont AK, Pufahl RA, O'Halloran TV, Rosenzweig AC. Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry. 39: 1589-95. PMID 10677207 DOI: 10.1021/bi992822i  1
2000 Lamb AL, Wernimont AK, Pufahl RA, O'Halloran TV, Rosenzweig AC. Crystal structure of the second domain of the human copper chaperone for superoxide dismutase. Biochemistry. 39: 1589-95. PMID 10677207 DOI: 10.1021/bi992822i  1
1999 Lamb AL, Wernimont AK, Pufahl RA, Culotta VC, O'Halloran TV, Rosenzweig AC. Crystal structure of the copper chaperone for superoxide dismutase. Nature Structural Biology. 6: 724-9. PMID 10426947 DOI: 10.1038/11489  1
1999 Lamb AL, Wernimont AK, Pufahl RA, Culotta VC, O'Halloran TV, Rosenzweig AC. Crystal structure of the copper chaperone for superoxide dismutase. Nature Structural Biology. 6: 724-9. PMID 10426947 DOI: 10.1038/11489  1
1999 Lamb AL, Newcomer ME. The structure of retinal dehydrogenase type II at 2.7 Å resolution: Implications for retinal specificity Biochemistry. 38: 6003-6011. PMID 10320326 DOI: 10.1021/bi9900471  1
1999 Lamb AL, Newcomer ME. The structure of retinal dehydrogenase type II at 2.7 Å resolution: Implications for retinal specificity Biochemistry. 38: 6003-6011. PMID 10320326 DOI: 10.1021/bi9900471  0.32
1998 Lamb AL, Wang X, Napoli JL, Newcomer ME. Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II. Acta Crystallographica. Section D, Biological Crystallography. 54: 639-42. PMID 9761861 DOI: 10.1107/S0907444997014121  1
1998 Lamb AL, Wang X, Napoli JL, Newcomer ME. Purification, crystallization and preliminary X-ray diffraction studies of retinal dehydrogenase type II. Acta Crystallographica. Section D, Biological Crystallography. 54: 639-42. PMID 9761861 DOI: 10.1107/S0907444997014121  1
1991 Lamb A, Tibbetts M, Hammond CI. The product of the KIN1 locus in Saccharomyces cerevisiae is a serine/threonine-specific protein kinase Yeast. 7: 219-228. PMID 1652871  1
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