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Tom Alber

Affiliations: 
Molecular & Cell Biology University of California, Berkeley, Berkeley, CA, United States 
Area:
Biochemistry, Molecular Biology, Cell Biology
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"Tom Alber"
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Parents

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Children

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Laurie M. Gay grad student 2007 UC Berkeley
Andrew E. Greenstein grad student 2007 UC Berkeley
Nathaniel Echols grad student 2008 UC Berkeley
Twyla N. Lombana grad student 2008 UC Berkeley
Elizabeth M. Flynn grad student 2009 UC Berkeley
Alison N. Killilea grad student 2009 UC Berkeley
Lisa M. Prach grad student 2009 UC Berkeley
Christina E. Baer grad student 2010 UC Berkeley
Alexandra Cavazos grad student 2012 UC Berkeley

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Publications

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Zhang Y, Prach LM, O'Brien TE, et al. (2020) Crystal Structure and Mechanistic Molecular Modeling Studies of Diterpene Cyclase Rv3377c. Biochemistry
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
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