Faculty Research Page
Professor of the Graduate School Division of Biochemistry, Biophysics and Structural Biology
My longstanding research interests are in protein chemistry and structure-function relationships, enzymology, and biophysical chemistry, and diverse issues in environmental science. My research encompassed studies of the assembly and structure-function relationships of macromolecular complexes, analysis of fundamental processes in light-harvesting in photosynthesis, development of fluorescent reagents for cell sorting and cell analyses, for detection of reactive oxygen species and physiologically important antioxidants, reagents and methods for high sensitivity DNA sequencing and detection.
From 1997-2005, I served as the University of California system representative on the California Biodiversity Council (http://biodiversity.ca.gov). From 1998 through the end of 2009, I was the director of the University of California Natural Reserve System (NRS; http://nrs.ucop.edu) at the UC Office of the President. The NRS manages 37 reserves that encompass about 135,000 acres across twelve ecological regions in California. The NRS supports research and teaching at all campuses of the University of California in a variety of disciplines that require fieldwork in natural areas (see http://nrs.ucop.edu). As a result of this administrative responsibility, my interests have expanded to include a broad spectrum of environmental sciences.
My current major (though not exclusive) focus is on the impact of anthropogenic fixed nitrogen on the Earth, the depletion and contamination of freshwater resources, forest die-off, and the environmental impacts of natural gas, coal, and oil production.
In other collaborative studies, we utilize the very large, rapidly expanding public protein sequence databases to explore the patterns of conservation and change of amino acid sequences within protein families over their evolutionary history in an attempt to exploit these patterns to gain insights into protein structure-function relationships and to attempt to identify some of the factors that drive the observed sequence changes.
Multiple Amino Acid Sequence Alignment Nitrogenase Component 1: Insights into Phylogenetics and Structure-Function Relationships. [J.B. Howard, K.J. Kechris, D.C. Rees, and A.N. Glazer (2013) PLos ONE 8(9): e72751. doi:10.1371//journal.pone.072751]
The Water Table: The Shifting Foundation of Life on Land. [A.N. Glazer and G.E. Likens (2012) AMBIO 41, 657-669 DOI 10.1007/s13280-012-0328]
Natural Reserves and Preserves. [A.N. Glazer (2013) in S.A. Lewin (ed.) Encyclopedia of Biodiversity, Second Edition, Vol. 5, pp.442-450. Waltham, M.A.: Academic Press]
The Evolution and Future of Earth's Nitrogen Cycle. [D.E. Canfield, A.N. Glazer, and P.G. Falkowski (2010) Science 330, 192-196]
Conserved Amino Acid Sequence Features in the Subunits of MoFe, VFe, and FeFe Nitrogenases. [A.N. Glazer and K.J. Kechris (2009) PLoS ONE 4(7): e6136.doi:10.1371/journal.pone.0006136]
Microbial Biotechnology. Fundamentals of Applied Microbiology. [A.N. Glazer and H. Nikaido (2007) 2nd Ed. Cambridge University Press, Cambridge, U.K.]
Quantitative exploration of the occurrence of lateral gene transfer by using nitrogen fixation genes as a case study. [K. Kechris, J.C. Lin, P.J. Bickel, and A.N. Glazer (2006) Proc. Natl. Acad. Sci. USA 103, 9584-9589]
Cryptic species within the cosmopolitan dessication-tolerant moss Grimmia laevigata. [C.C. Fernandez, J.R. Shevock, A.N. Glazer, and J.N. Thompson (2006) Proc. Natl. Acad. Sci. USA 103, 637-642]
Energy Transfer Fluorescent Labels for DNA Sequencing and Analysis. [J. Xie, S.-C. Hung, A. N., Glazer, and R. A. Mathies (2003) In Topics in Fluorescence Spectroscopy. DNA Technology, Vol. 7, pp. 105-127 ed. J. R. Lakowicz. Kluwer Academic/Plenum Publishers, NY]
Finding Important Sites in Protein Sequences. [P.J. Bickel, K.J. Kechris, P.C. Spector, G.J. Wedemayer, and A.N. Glazer (2002) Proc. Natl. Acad. Sci. USA 99, 14764-114771]
Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-alpha-subunit in a heterologous host. [A.J. Tooley, Y.A. Cai, and A.N. Glazer (2001) Proc. Natl. Acad. Sci. USA 98, 10560- 10565]).
Recombinant Phycobiliproteins. Recombinant C-Phycocyanins Equipped with Affinity Tags, Oligomerization, and Biospecific Recognition Domains. [Y.A. Cai, J.T. Murphy, G.J. Wedemayer, and A.N. Glazer (2001) Anal. Biochem. 290, 186-204]
Photo credit: Mark Joseph Hanson of Mark Joseph Studio.
Last Updated 2013-12-15