Kurt L Krause
Kurt L Krause
Verified email at otago.ac.nz - Homepage
TitleCited byYear
Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 2.5 ┼ resolution
JJ Tanner, RM Hecht, KL Krause
Biochemistry 35 (8), 2597-2609, 1996
Emergence of macrolide resistance during treatment of pneumococcal pneumonia
DM Musher, ME Dowell, VD Shortridge, RK Flamm, JH Jorgensen, ...
New England Journal of Medicine 346 (8), 630-631, 2002
Severe diabetes associated with protease inhibitor therapy
F Visnegarwala, KL Krause, DM Musher
Annals of internal medicine 127 (10), 947-947, 1997
2.5 ┼ structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate
KL Krause, KW Volz, WN Lipscomb
Journal of molecular biology 193 (3), 527-553, 1987
2.1 ┼ structure of Serratia endonuclease suggests a mechanism for binding to double-stranded DNA
MD Miller, J Tanner, M Alpaugh, MJ Benedik, KL Krause
Nature structural biology 1 (7), 461, 1994
Flavin Reductase P:  Structure of a Dimeric Enzyme That Reduces Flavin,
JJ Tanner, B Lei, SC Tu, KL Krause
Biochemistry 35 (42), 13531-13539, 1996
Chemical Generation of C602-and Electron Transfer Mechanism for the Reactions with Alkyl Bromides
R Subramanian, KM Kadish, MN Vijayashree, X Gao, MT Jones, ...
The Journal of Physical Chemistry 100 (40), 16327-16335, 1996
Analysis of the mechanism of the Serratia nuclease using site-directed mutagenesis
P Friedhoff, B Kolmes, O Gimadutdinow, W Wende, KL Krause, A Pingoud
Nucleic acids research 24 (14), 2632-2639, 1996
Characterization of the alanine racemases from two mycobacteria
U Strych, RL Penland, M Jimenez, KL Krause, MJ Benedik
FEMS microbiology letters 196 (2), 93-98, 2001
The active site of Serratia endonuclease contains a conserved magnesium-water cluster
MD Miller, J Cai, KL Krause
Journal of molecular biology 288 (5), 975-987, 1999
Structure at 2.9-A resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate
KL Krause, KW Volz, WN Lipscomb
Proceedings of the National Academy of Sciences 82 (6), 1643-1647, 1985
The 1.9 ┼ Crystal Structure of Alanine Racemase from Mycobacterium tuberculosis Contains a Conserved Entryway into the Active Site,
P LeMagueres, H Im, J Ebalunode, U Strych, MJ Benedik, JM Briggs, ...
Biochemistry 44 (5), 1471-1481, 2005
A similar active site for non–specific and specific endonucleases
P Friedhoff, I Franke, G Meiss, W Wende, KL Krause, A Pingoud
Nature structural biology 6 (2), 112, 1999
Characterization of the alanine racemases from Pseudomonas aeruginosa PAO1
U Strych, HC Huang, KL Krause, MJ Benedik
Current microbiology 41 (4), 290-294, 2000
Identification of the Serratia endonuclease dimer: Structural basis and implications for catalysis
MD Miller, KL Krause
Protein science 5 (1), 24-33, 1996
Experience with commercial area detectors: abuyer's' perspective
KL Krause, GN Phillips
Journal of applied crystallography 25 (2), 146-154, 1992
The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study
JE Gouaux, KL Krause, WN Lipscomb
Biochemical and biophysical research communications 142 (3), 893-897, 1987
The alanine racemase of Mycobacterium smegmatis is essential for growth in the absence of D-alanine
DL Milligan, SL Tran, U Strych, GM Cook, KL Krause
Journal of bacteriology 189 (22), 8381-8386, 2007
Spacer capture and integration by a type IF Cas1–Cas2-3 CRISPR adaptation complex
RD Fagerlund, ME Wilkinson, O Klykov, A Barendregt, FG Pearce, ...
Proceedings of the National Academy of Sciences 114 (26), E5122-E5128, 2017
Crystal structure at 1.45 ┼ resolution of alanine racemase from a pathogenic bacterium, Pseudomonas aeruginosa, contains both internal and external aldimine forms
P LeMagueres, H Im, A Dvorak, U Strych, M Benedik, KL Krause
Biochemistry 42 (50), 14752-14761, 2003
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