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Proceedings of the National Academy of Sciences of the United States of America|November 21, 1995
Structure determination of murine mitochondrial carbonic anhydrase V at 2.45-A resolution: implications for catalytic proton transfer and inhibitor designP A Boriack-Sjodin, R W Heck, P J Laipis, et al.Biochimica Et Biophysica Acta|November 11, 1999
Proton transfer to residues of basic pK(a) during catalysis by carbonic anhydraseM Qian, J N Earnhardt, N R Wadhwa, et al.The Journal of Biological Chemistry|October 7, 1994
Catalytic properties of mouse carbonic anhydrase VR W Heck, S M Tanhauser, R Manda, et al.Biochemistry|August 27, 1991
Catalytic enhancement of human carbonic anhydrase III by replacement of phenylalanine-198 with leucineP V LoGrasso, C K Tu, D A Jewell, et al.Biochemistry|October 12, 1993
Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase IIID N Silverman, C Tu, X Chen, et al.Molecular Genetics and Metabolism|September 13, 2005
Impaired glutamatergic synaptic transmission in the PKU brainA E Martynyuk, A V Glushakov, C Sumners, et al.Gene|January 1, 1980
Genetic mapping of bovine mitochondrial DNA from a single animalW W Hauswirth, P J Laipis, M E Gilman, et al.The Journal of Biological Chemistry|September 16, 1994
Interactions of active-site residues and catalytic activity of human carbonic anhydrase IIIC Tu, X Chen, X Ren, et al.Nature|October 5, 1986
Anatomical, cellular and molecular analysis of 8,000-yr-old human brain tissue from the Windover archaeological siteG H Doran, D N Dickel, W E Ballinger, et al.Endocrinology|December 1, 1993
Multiple copies of the bone-specific osteocalcin gene in mouse and ratS Rahman, A Oberdorf, M Montecino, et al.Pageof 5