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Dr. Maria Linder

Professor Biochemistry

linder 1

Mammalian copper and iron metabolism, focusing on the structure, function and regulation of proteins associated with these elements; emphasis is on mechanisms of copper transport in pregnancy and lactation, and on the intestinal absorption and storage of iron; studies use a broad variety of approaches from cell culture models, transgenic mice and tracer radioisotopes, to isolation, sequencing and characterization of proteins, as well as manipulation of mRNA/protein expression.


Office: MH-582K
Phone: (657) 278-2472
Lab: DBH-176/177
Phone: (657) 278-2475/3912
Email: This email address is being protected from spambots. You need JavaScript enabled to view it.


Maria Linder, who earned her bachelor's degree in chemistry from Vassar College in New York and her doctorate in biochemistry from Harvard University, has been a mentor to hundreds of students in her laboratory. Students have collaborated with her on research that focuses on examining how copper and iron function in the body. Her work also has contributed to a greater understanding of cancer.

Over the years, Linder has garnered over $12 million in research grants, authored 137 scientific publications and two books, directed the  Howard Hughes Medical Institute Research Scholars Program, and has received numerous accolades for her research and teaching.

Those honors include CSUF's 1985 Outstanding Professor Award and the inaugural recipient of the L. Donald Shields Excellence in Scholarship and Creativity Award in 2013. She also received the California State University Wang Family Excellence Award in 2007, and last year, became a Fellow of the American Association for the Advancement of Science.

Maria Linder, professor of chemistry and biochemistry, was recognized on April 12 for her 40 years of service during the 2016-17 University Awards Program.  Linder wants to continue doing research and educating future scientists: "I'm proud of my own research accomplishments, as well as the work of my students. It's been rewarding to be a mentor and interact with the wonderful young people entering the sciences, and to help them achieve their goals.”

Courses Taught

  • CHEM 421 Biological Chemistry
  • CHEM 422 Biochemistry Laboratory
  • CHEM 445 Nutritional Biochemistry


Postdoctoral M.I.T. Cambridge, MA
Postdoctoral Harvard Medical School, Boston, MA
Ph.D. Harvard University, Cambridge, MA 
B.Sc. Vassar College, Poughkeepsie, NY

Research Interests

An expert on mammalian copper and iron metabolism, Dr. Linder is currently focusing her research on mechanisms of copper transport in the period before and after birth, and on the intestinal absorption and storage of iron, using a broad variety of approaches, from cell culture models, transgenic mice and tracer radioisotopes, to isolation, sequencing and characterization of proteins, as well as si/shRNA manipulation of mRNA/protein expression.

Selected Publications

Linder, M.C. (2010) Nutritional biochemistry of copper, with emphasis on the perinatal period. In: Biochemical Aspects of Human Nutrition (L. Avigliano and L. Rossi, eds.), ISBN 978-81-7895-478-3. Transworld Research Network, Trivandrum, Kerala, India, pp.143-179, in press

Moriya, M., Ho, Y-H., Grana, A., Nguyen, L., Alvarez, A., Jamil,, R., Ackland, M.L., Michalczyk, A., Hamer, P., Ramos,, D. Kim, S., Mercer, J.F.B., and Linder, M.C. (2008) Copper is taken up efficiently from albumin and alpha-2-macroglobulin by cultured human cells by more than one mechanism.  Am. J. Physiol. (Cell Physiology) 295: 708-721.

Liu, N.M., Lo, L.S.L., Askary, S.H., Jones, L.T., Nguyen, T.T.M., Kidane, T.Z., Goforth, J., Vivas, E., Tsai, M.T., Westbrook, T. and Linder, M.C.  (2007) Transcuprein is a macroglobulin regulated by copper availability. J. Nutritional Biochem. 18: 597-608.

Kidane,, T.Z., Sauble, E. and Linder, M.C. (2006) In three cell types, release of iron from ferritin requires lysosomal activity.  Am. J. Physiol. (Cell Biol.) 291: C445-C455. 

Donley, S.A., Ilagan, B.J., Rim, H. and Linder, M.C. (2002)  Copper transport to mammary gland and milk during lactation in rats.  Am. J. Physiol. (Endoc. Metab.), 283, E667-E675.