Thomas C. Alber

Molecular and Cell Biology University of California, Berkeley, Berkeley, CA, United States 
host-pathogen interactions, motions in proteins
"Thomas Alber"

Mean distance: 8.55


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Gregory A. Petsko grad student 1981 MIT
 (Structural origins of the catalytic power of triose phosphate isomerase)
Brian W. Matthews post-doc University of Oregon, Eugene


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Sarah M. McWhirter grad student 2000 UC Berkeley
James M. Holton grad student 2001 UC Berkeley
Kristi E. Pullen grad student 2006 UC Berkeley
James S. Fraser grad student 2010 UC Berkeley
Robert B. Rose post-doc 1996-2001 UC Berkeley
Ho Leung Ng post-doc 2001-2007 UC Berkeley
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Hu S, Offenbacher AR, Thompson EM, et al. (2019) Biophysical Characterization of a Disabled Double Mutant of Soybean Lipoxygenase: The "Undoing" of Precise Substrate Positioning Relative to Metal Cofactor and an Identified Dynamical Network. Journal of the American Chemical Society
Heinkel F, Shen L, Richard-Greenblatt M, et al. (2018) Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacteriumtuberculosis ABC Transporter Rv1747. Structure (London, England : 1993)
Buchko GW, Echols N, Flynn EM, et al. (2017) Structural and biophysical characterization of the Mycobacterium tuberculosis protein Rv0577, a protein associated with neutral red staining of virulent tuberculosis strains and homolog of the Streptomyces coelicolor protein KbpA. Biochemistry
Offenbacher AR, Hu S, Poss EM, et al. (2017) Hydrogen-Deuterium Exchange of Lipoxygenase Uncovers a Relationship between Distal, Solvent Exposed Protein Motions and the Thermal Activation Barrier for Catalytic Proton-Coupled Electron Tunneling. Acs Central Science. 3: 570-579
Prigozhin DM, Papavinasasundaram KG, Baer CE, et al. (2016) Structural and genetic analyses of the Mycobacterium tuberculosis Protein Kinase B sensor domain identify a potential ligand binding site. The Journal of Biological Chemistry
Kerns SJ, Agafonov RV, Cho YJ, et al. (2015) The energy landscape of adenylate kinase during catalysis. Nature Structural & Molecular Biology. 22: 124-31
Prigozhin DM, Krieger IV, Huizar JP, et al. (2014) Subfamily-specific adaptations in the structures of two penicillin-binding proteins from Mycobacterium tuberculosis. Plos One. 9: e116249
Baer CE, Iavarone AT, Alber T, et al. (2014) Biochemical and spatial coincidence in the provisional Ser/Thr protein kinase interaction network of Mycobacterium tuberculosis. The Journal of Biological Chemistry. 289: 20422-33
Hu S, Sharma SC, Scouras AD, et al. (2014) Extremely elevated room-temperature kinetic isotope effects quantify the critical role of barrier width in enzymatic C-H activation. Journal of the American Chemical Society. 136: 8157-60
Mavrici D, Marakalala MJ, Holton JM, et al. (2014) Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC. Proceedings of the National Academy of Sciences of the United States of America. 111: 8037-42
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