Read, Betsy 照片

Read, Betsy

Dr

所属大学: California State University, San Marcos

所属学院: Department of Biological Sciences

邮箱:
bread@csusm.edu

个人主页:
http://faculty.csusm.edu/read/

个人简介

Dr. Read's area of specialization is Molecular Cell Biology. She is the founder/initiator of the Biotechnology program at CSUSM and teaches core courses for the major. Currently, she is working on the molecular mechanisms of calcification and coccolithogenesis in the marine algae, Emiliania huxleyi, and her general research interests lie in the area of functional genomics. Prior to her arrival at CSUSM in 1993, she was a Postdoctoral Fellow in the Microbiology Department at The Ohio State University.

研究领域

Genomics and Functional Genomics of Algae

近期论文

Wahlund, T.M. , X. Zhang, and B.A. Read. 2004. EST Expression Profiles from Calcifying and Non-Calcifying Cultures of Emiliania huxleyi . Journal of Micropaleontology. Accepted April, 2004. Publication Date, Special Issue, Fall 2004. Wahlund, T.M., Hadaegh, A.R., Clark, R*., Nguyen, B*., Fanelli, M*., and B.A. Read. Analysis of Expressed Sequence Tags from Calcifying Cells of the Marine Coccolithophorid, Emiliania huxleyi. Journal of Marine Biotechnology, In Press, March 2004. Laguna, R*., J. Romo*, B.A. Read, and T.M. Wahlund. 2001. Induction of Phase Variation Events in the Life Cycle of the Marine Coccolithophore Emilania huxleyi. Appl. Environ. Microbiol. 67(9):3824-3831. Read, B.A. & F.R. Tabita. 1994. High substrate specificity factor ribulose bisphosphate carboxylase/oxygenase from eucaryotic marine algae and properties of recombinant cyanobacterial rubisco containing "algal" residue modifications. Arch. of Biochem. and Biophys., 312(l), 210-218. Read, B.A. & F.R. Tabita. 1992. A hybrid ribulose-bisphosphate carboxylase/oxygenase enzyme exhibiting a substantial increase in substrate specificity factor. Biochemistry, 31, 5553-5560. Read, B.A. & F.R. Tabita. 1992. Amino acid substitutions in the small subunit of ribulse- 1, 5 -bisphosphate carboxylase/oxygenase that influence the catalytic activity of the holoenzyme. Biochemistry, 30, 519525.