Kurt L. Krause, MD, PhD - Publications

Affiliations: 
University of Otago, Dunedin, Otago, New Zealand 
Area:
Structural Biology
Website:
http://biochem.otago.ac.nz/our-people/professor-kurt-krause/

43 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
2021 Campbell AC, Tanner JJ, Krause KL. Optimisation of Neuraminidase Expression for Use in Drug Discovery by Using HEK293-6E Cells. Viruses. 13. PMID 34696326 DOI: 10.3390/v13101893  0.489
2019 Kvach MV, Barzak FM, Harjes S, Schares HAM, Kurup HM, Jones KF, Sutton L, Donahue J, D'Aquila RT, Jameson GB, Harki DA, Krause KL, Harjes E, Filichev V. Differential inhibition of APOBEC3 DNA-mutator isozymes by fluoro- versus non-fluoro-substituted 2'-deoxyzebularine embedded in single-stranded DNA. Chembiochem : a European Journal of Chemical Biology. PMID 31633265 DOI: 10.1002/Cbic.201900505  0.307
2018 Watkins OC, Sharpe ML, Perry NB, Krause KL. New Zealand glowworm (Arachnocampa luminosa) bioluminescence is produced by a firefly-like luciferase but an entirely new luciferin. Scientific Reports. 8: 3278. PMID 29459729 DOI: 10.1038/S41598-018-21298-W  0.362
2017 Christensen EM, Patel SM, Korasick DA, Campbell AC, Krause KL, Becker DF, Tanner JJ. Resolving the Cofactor Binding Site in the Proline Biosynthetic Enzyme Human Pyrroline-5-Carboxylate Reductase 1. The Journal of Biological Chemistry. PMID 28258219 DOI: 10.1074/Jbc.M117.780288  0.621
2017 Krause KL, Christensen EM, Patel SM, Korasick DA, Campbell AC, Becker DF, Tanner JJ. Correcting the record – cofactor binding of human pyrroline-5-carboxylate reductase Acta Crystallographica Section a Foundations and Advances. 73: C49-C49. DOI: 10.1107/S2053273317095213  0.516
2016 Poen S, Nakatani Y, Opel-Reading HK, Lassé M, Dobson RC, Krause KL. Exploring the Structure of Glutamate Racemase from Mycobacterium tuberculosis as a Template for Anti-mycobacterial Drug Discovery. The Biochemical Journal. PMID 26964898 DOI: 10.1042/Bcj20160186  0.364
2015 Couñago RM, Knapp KM, Nakatani Y, Fleming SB, Corbett M, Wise LM, Mercer AA, Krause KL. Structures of Orf Virus Chemokine Binding Protein in Complex with Host Chemokines Reveal Clues to Broad Binding Specificity. Structure (London, England : 1993). PMID 26095031 DOI: 10.1016/J.Str.2015.04.023  0.319
2014 Davis E, Scaletti-Hutchinson E, Opel-Reading H, Nakatani Y, Krause KL. The structure of alanine racemase from Acinetobacter baumannii. Acta Crystallographica. Section F, Structural Biology Communications. 70: 1199-205. PMID 25195891 DOI: 10.1107/S2053230X14017725  0.385
2014 Opel-Reading H, Luckner S, Schaller R, Kurtz D, Krause K. Rubrerythrin from Trichomonas vaginalis- structural insights into its mechanism of action Acta Crystallographica Section a Foundations and Advances. 70: C821-C821. DOI: 10.1107/S2053273314091785  0.383
2014 Krause K. William Nunn Lipscomb, Jr – A Kentucky Colonel's Contribution to Boranes, Proteins and Atomic Structure Acta Crystallographica Section a Foundations and Advances. 70: C1305-C1305. DOI: 10.1107/S205327331408694X  0.315
2012 Scaletti ER, Luckner SR, Krause KL. Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50) Acta Crystallographica Section D: Biological Crystallography. 68: 82-92. PMID 22194336 DOI: 10.1107/S0907444911050682  0.408
2011 Anthony KG, Strych U, Yeung KR, Shoen CS, Perez O, Krause KL, Cynamon MH, Aristoff PA, Koski RA. New classes of alanine racemase inhibitors identified by high-throughput screening show antimicrobial activity against mycobacterium tuberculosis Plos One. 6. PMID 21637807 DOI: 10.1371/Journal.Pone.0020374  0.306
2011 Im H, Sharpe ML, Strych U, Davlieva M, Krause KL. The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design Bmc Microbiology. 11. PMID 21612658 DOI: 10.1186/1471-2180-11-116  0.352
2010 Couñago RM, Fleming SB, Mercer AA, Krause KL. Crystallization and preliminary X-ray analysis of the chemokine-binding protein from orf virus (Poxviridae). Acta Crystallographica. Section F, Structural Biology and Crystallization Communications. 66: 819-23. PMID 20606282 DOI: 10.1107/S1744309110018166  0.342
2009 Couñago RM, Davlieva M, Strych U, Hill RE, Krause KL. Biochemical and structural characterization of alanine racemase from Bacillus anthracis (Ames). Bmc Structural Biology. 9: 53. PMID 19695097 DOI: 10.1186/1472-6807-9-53  0.367
2009 Chen C, Krause K, Pettitt BM. Advantage of being a dimer for Serratia marcescens endonuclease. The Journal of Physical Chemistry. B. 113: 511-21. PMID 19053714 DOI: 10.1021/Jp8057838  0.322
2007 Strych U, Davlieva M, Longtin JP, Murphy EL, Im H, Benedik MJ, Krause KL. Purification and preliminary crystallization of alanine racemase from Streptococcus pneumoniae Bmc Microbiology. 7. PMID 17509154 DOI: 10.1186/1471-2180-7-40  0.326
2007 Chen C, Beck BW, Krause K, Weksberg TE, Pettitt BM. Effects of dimerization of Serratia marcescens endonuclease on water dynamics. Biopolymers. 85: 241-52. PMID 17133507 DOI: 10.1002/Bip.20641  0.31
2006 Chen C, Beck BW, Krause K, Pettitt BM. Solvent participation in Serratia marcescens endonuclease complexes. Proteins. 62: 982-95. PMID 16355414 DOI: 10.1002/Prot.20694  0.318
2005 LeMagueres P, Im H, Ebalunode J, Strych U, Benedik MJ, Briggs JM, Kohn H, Krause KL. The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site. Biochemistry. 44: 1471-81. PMID 15683232 DOI: 10.1021/Bi0486583  0.437
2003 LeMagueres P, Im H, Dvorak A, Strych U, Benedik M, Krause KL. Crystal Structure at 1.45 Å Resolution of Alanine Racemase from a Pathogenic Bacterium, Pseudomonas aeruginosa, Contains Both Internal and External Aldimine Forms Biochemistry. 42: 14752-14761. PMID 14674749 DOI: 10.1021/Bi030165V  0.418
2003 Liu L, Im H, Cegielski M, LeMagueres P, Schultz LW, Krause KL, Hastings JW. Characterization and crystallization of active domains of a novel luciferase from a marine dinoflagellate. Acta Crystallographica. Section D, Biological Crystallography. 59: 761-4. PMID 12657805 DOI: 10.1107/S0907444903002920  0.32
2002 Crossnoe CR, Germanas JP, LeMagueres P, Mustata G, Krause KL. The crystal structure of Trichomonas vaginalis ferredoxin provides insight into metronidazole activation Journal of Molecular Biology. 318: 503-518. PMID 12051855 DOI: 10.1016/S0022-2836(02)00051-7  0.324
2001 Strych U, Penland RL, Jimenez M, Krause KL, Benedik MJ. Characterization of the alanine racemases from two Mycobacteria Fems Microbiology Letters. 196: 93-98. PMID 11267762 DOI: 10.1111/J.1574-6968.2001.Tb10547.X  0.356
2000 Strych U, Huang HC, Krause KL, Benedik MJ. Characterization of the alanine racemases from Pseudomonas aeruginosa PAO1 Current Microbiology. 41: 290-294. PMID 10977898 DOI: 10.1007/S002840010136  0.389
1999 Miller MD, Cai J, Krause KL. The active site of Serratia endonuclease contains a conserved magnesium-water cluster Journal of Molecular Biology. 288: 975-987. PMID 10329193 DOI: 10.1006/Jmbi.1999.2729  0.321
1999 Friedhoff P, Franke I, Krause KL, Pingoud A. Cleavage experiments with deoxythymidine 3',5'-bis-(p-nitrophenyl phosphate) suggest that the homing endonuclease I-PpoI follows the same mechanism of phosphodiester bond hydrolysis as the non-specific Serratia nuclease Febs Letters. 443: 209-214. PMID 9989607 DOI: 10.1016/S0014-5793(98)01660-3  0.417
1997 Antosiewicz J, Miller MD, Krause KL, McCammon JA. Simulation of electrostatic and hydrodynamic properties of Serratia endonuclease Biopolymers. 41: 443-450. PMID 9080779 DOI: 10.1002/(Sici)1097-0282(19970405)41:4<443::Aid-Bip8>3.0.Co;2-M  0.487
1997 Tanner JJ, Miller MD, Wilson KS, Tu SC, Krause KL. Structure of bacterial luciferase beta 2 homodimer: implications for flavin binding. Biochemistry. 36: 665-72. PMID 9020763 DOI: 10.1021/Bi962511X  0.554
1996 Tanner JJ, Lei B, Tu SC, Krause KL. Flavin reductase P: structure of a dimeric enzyme that reduces flavin. Biochemistry. 35: 13531-9. PMID 8885832 DOI: 10.1021/Bi961400V  0.613
1996 Miller MD, Krause KL. Identification of the Serratia endonuclease dimer: Structural basis and implications for catalysis Protein Science. 5: 24-33. PMID 8771193 DOI: 10.1002/Pro.5560050104  0.403
1996 Friedhoff P, Kolmes B, Gimadutdinow O, Wende W, Krause KL, Pingoud A. Analysis of the mechanism of the Serratia nuclease using site-directed mutagenesis Nucleic Acids Research. 24: 2632-2639. PMID 8758988 DOI: 10.1093/Nar/24.14.2632  0.377
1996 Tanner JJ, Hecht RM, Krause KL. Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms Resolution. Biochemistry. 35: 2597-609. PMID 8611563 DOI: 10.1021/Bi951988Q  0.557
1994 Tanner J, Hecht RM, Pisegna M, Seth DM, Krause KL. Preliminary crystallographic analysis of glyceraldehyde 3-phosphate dehydrogenase from the extreme thermophile Thermus aquaticus. Acta Crystallographica. Section D, Biological Crystallography. 50: 744-8. PMID 15299371 DOI: 10.1107/S0907444994001915  0.578
1994 Tanner J, Lei B, Liu M, Tu SC, Krause KL. Crystallization and preliminary crystallographic analysis of NADPH:FMN oxidoreductase from Vibrio harveyi Journal of Molecular Biology. 241: 283-287. PMID 8057370 DOI: 10.1006/Jmbi.1994.1501  0.559
1994 Miller MD, Tanner J, Alpaugh M, Benedik MJ, Krause KL. 2.1 Å structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA Nature Structural Biology. 1: 461-468. PMID 7664065 DOI: 10.1038/Nsb0794-461  0.599
1994 Tanner J, Hecht RM, Pisegna M, Seth DM, Krause KL. Preliminary crystallographic analysis of glyceraldehyde 3-phosphate dehydrogenase from the extreme thermophile Thermus aquaticus Acta Crystallographica Section D: Biological Crystallography. 50: 744-748. DOI: 10.1107/S0907444994001915  0.507
1993 Tanner JJ, Smith PE, Krause KL. Molecular dynamics simulations and rigid body (TLS) analysis of aspartate carbamoyltransferase: evidence for an uncoupled R state. Protein Science : a Publication of the Protein Society. 2: 927-35. PMID 8318897 DOI: 10.1002/Pro.5560020606  0.545
1991 Miller MD, Benedik MJ, Sullivan MC, Shipley NS, Krause KL. Crystallization and preliminary crystallographic analysis of a novel nuclease from Serratia marcescens Journal of Molecular Biology. 222: 27-30. PMID 1658338 DOI: 10.1016/0022-2836(91)90734-N  0.396
1987 Krause KL, Volz KW, Lipscomb WN. 2.5 A structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate. Journal of Molecular Biology. 193: 527-53. PMID 3586030 DOI: 10.1016/0022-2836(87)90265-8  0.543
1987 Gouaux JE, Krause KL, Lipscomb WN. The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study. Biochemical and Biophysical Research Communications. 142: 893-7. PMID 3548720 DOI: 10.1016/0006-291X(87)91497-5  0.689
1986 Vol? KW, Krause KL, Lipscomb WN. The binding of N-(phosphonacetyl)-L-aspartate to aspartate carbamoyltransferase of Escherichia coli. Biochemical and Biophysical Research Communications. 136: 822-6. PMID 3518720 DOI: 10.1016/0006-291X(86)90514-0  0.513
1985 Krause KL, Volz KW, Lipscomb WN. Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate. Proceedings of the National Academy of Sciences of the United States of America. 82: 1643-7. PMID 3856843 DOI: 10.1073/Pnas.82.6.1643  0.532
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