Gerd N. La Mar, Prof.
Affiliations: | Chemistry | University of California, Davis, Davis, CA |
Website:
http://chemistry.ucdavis.edu/faculty/department_Faculty/gerd_laMar.htmlGoogle:
"Gerd La Mar"Bio:
https://www.gf.org/fellows/all-fellows/gerd-n-la-mar/
Mean distance: 7.57
Parents
Sign in to add mentorLeland C. Allen | grad student | 1964 | Princeton | |
(Interpretation of the proton magnetic resonance spectra of some triarylphosphine complexes of cobalt (II) and nickel (II)) | ||||
William DeW. Horrocks | grad student | 1964 | Princeton |
Children
Sign in to add traineeDungeng Peng | grad student | (Neurotree) | |
Nicki Lee Davis | grad student | 1978-1982 | UC Davis |
Thomas Jue | grad student | 1983 | UC Davis |
Robert D Johnson | grad student | 1979-1983 | UC Davis |
Anh-Tuyet T. Tran | grad student | 2002 | UC Davis |
Zhenming Du | grad student | 2001-2007 | UC Davis |
Harold M. Goff | post-doc | UC Davis | |
Lechosław Latos-Grażyński | post-doc | 1979-1981 | UC Davis |
Vadappuram Pilo Chacko | post-doc | 1980-1982 | UC Davis |
Kara L. Bren | post-doc | 1996-1997 | UC Davis |
Mateus Webba da Silva | post-doc | 1997-1999 | UC Davis |
Yangzhong Liu | post-doc | 2002-2005 | UC Davis |
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Publications
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Peng D, Ogura H, Ma LH, et al. (2013) Solution NMR characterization of magnetic/electronic properties of azide and cyanide-inhibited substrate complexes of human heme oxygenase: implications for steric ligand tilt. Journal of Inorganic Biochemistry. 121: 179-86 |
Peng D, Ma LH, Smith KM, et al. (2012) Role of propionates in substrate binding to heme oxygenase from Neisseria meningitidis: a nuclear magnetic resonance study. Biochemistry. 51: 7054-63 |
Peng D, Satterlee JD, Ma LH, et al. (2011) Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis. A 1H NMR study. Biochemistry. 50: 8823-33 |
Du Z, Unno M, Matsui T, et al. (2010) Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes. Journal of Inorganic Biochemistry. 104: 1063-70 |
Peng D, Ma LH, Ogura H, et al. (2010) 1H NMR study of the influence of mutation on the interaction of the C-terminus with the active site in heme oxygenase from Neisseria meningitidis: implications for product release. Biochemistry. 49: 5832-40 |
Peng D, Ogura H, Zhu W, et al. (2009) Coupling of the distal hydrogen bond network to the exogenous ligand in substrate-bound, resting state human heme oxygenase. Biochemistry. 48: 11231-42 |
Ogura H, Evans JP, Peng D, et al. (2009) The orbital ground state of the azide-substrate complex of human heme oxygenase is an indicator of distal H-bonding: implications for the enzyme mechanism. Biochemistry. 48: 3127-37 |
Ma LH, Liu Y, Zhang X, et al. (2009) 1H NMR study of the effect of variable ligand on heme oxygenase electronic and molecular structure. Journal of Inorganic Biochemistry. 103: 10-9 |
Ogura H, Evans JP, de Montellano PR, et al. (2008) Implication for using heme methyl hyperfine shifts as indicators of heme seating as related to stereoselectivity in the catabolism of heme by heme oxygenase: in-plane heme versus axial his rotation. Biochemistry. 47: 421-30 |
La Mar GN. (2007) Application of the paramagnetic dipole field for solution NMR active site structure determination in low-spin, cyanide-inhibited ferric hemoproteins. Iubmb Life. 59: 513-27 |