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Showing results (291-300 of 316) with videos related to

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Biochemistry|April 9, 1999
The role of water in the catalytic efficiency of triosephosphate isomeraseZ Zhang, E A Komives, S Sugio, et al.
Biochemistry|January 24, 1989
Activity and spectroscopic properties of bacterial D-amino acid transaminase after multiple site-directed mutagenesis of a single tryptophan residueA Martínez del Pozo, M Merola, H Ueno, et al.
The Journal of Clinical Endocrinology and Metabolism|January 25, 2007
Effect of monitoring bone turnover markers on persistence with risedronate treatment of postmenopausal osteoporosisPierre D Delmas, Bernard Vrijens, Richard Eastell, et al.
Biochemistry|February 15, 1994
Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acidK N Allen, A Lavie, A Glasfeld, et al.
Biochemistry|January 13, 1987
Thermal expansion of a proteinH Frauenfelder, H Hartmann, M Karplus, et al.
The Journal of Biological Chemistry|December 25, 1990
Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial D-amino acid transaminase. Effects of exogenous amines on the slow formation of intermediatesS Futaki, H Ueno, A Martinez del Pozo, et al.
Osteoporosis International : a Journal Established As Result of Cooperation Between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA|April 15, 2015
The position of strontium ranelate in today's management of osteoporosisJ-Y Reginster, M-L Brandi, J Cannata-Andía, et al.
Science (New York, N.Y.)|February 24, 1995
A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acidsP C Babbitt, G T Mrachko, M S Hasson, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 2, 1998
Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolaseM S Hasson, I Schlichting, J Moulai, et al.
Medizinische Klinik (Munich, Germany : 1983)|August 10, 2000
[Osteoporosis in the male]B Allolio, M Dambacher, R Dreher, et al.
Pageof 32

Showing results (291-300 of 316) with videos related to

Sort By:
Pageof 32
Biochemistry|April 9, 1999
The role of water in the catalytic efficiency of triosephosphate isomeraseZ Zhang, E A Komives, S Sugio, et al.
Biochemistry|January 24, 1989
Activity and spectroscopic properties of bacterial D-amino acid transaminase after multiple site-directed mutagenesis of a single tryptophan residueA Martínez del Pozo, M Merola, H Ueno, et al.
The Journal of Clinical Endocrinology and Metabolism|January 25, 2007
Effect of monitoring bone turnover markers on persistence with risedronate treatment of postmenopausal osteoporosisPierre D Delmas, Bernard Vrijens, Richard Eastell, et al.
Biochemistry|February 15, 1994
Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acidK N Allen, A Lavie, A Glasfeld, et al.
Biochemistry|January 13, 1987
Thermal expansion of a proteinH Frauenfelder, H Hartmann, M Karplus, et al.
The Journal of Biological Chemistry|December 25, 1990
Substitution of glutamine for lysine at the pyridoxal phosphate binding site of bacterial D-amino acid transaminase. Effects of exogenous amines on the slow formation of intermediatesS Futaki, H Ueno, A Martinez del Pozo, et al.
Osteoporosis International : a Journal Established As Result of Cooperation Between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA|April 15, 2015
The position of strontium ranelate in today's management of osteoporosisJ-Y Reginster, M-L Brandi, J Cannata-Andía, et al.
Science (New York, N.Y.)|February 24, 1995
A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acidsP C Babbitt, G T Mrachko, M S Hasson, et al.
Proceedings of the National Academy of Sciences of the United States of America|September 2, 1998
Evolution of an enzyme active site: the structure of a new crystal form of muconate lactonizing enzyme compared with mandelate racemase and enolaseM S Hasson, I Schlichting, J Moulai, et al.
Medizinische Klinik (Munich, Germany : 1983)|August 10, 2000
[Osteoporosis in the male]B Allolio, M Dambacher, R Dreher, et al.
Pageof 32