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M Stroud

Showing results (341-350 of 475) with videos related to

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ACS Biomaterials Science & Engineering|January 12, 2021
Shell Structure and Growth in the Base Plate of the Barnacle <i>Amphibalanus amphitrite</i>Bradley T De Gregorio, Rhonda M Stroud, Daniel K Burden, et al.
Journal of Molecular Biology|November 25, 1998
Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transferC L Reyes, C R Sage, E E Rutenber, et al.
Circulation|June 5, 2014
Screening for acute IKr block is insufficient to detect torsades de pointes liability: role of late sodium currentTao Yang, Young Wook Chun, Dina M Stroud, et al.
Plos One|May 8, 2020
Diversity in kinetics correlated with structure in nano body-stabilized LacYHemant Kumar, Janet Finer-Moore, Irina Smirnova, et al.
Biochemistry|September 30, 1998
D221 in thymidylate synthase controls conformation change, and thereby opening of the imidazolidineC R Sage, M D Michelitsch, T J Stout, et al.
Science (New York, N.Y.)|January 23, 1987
Atomic structure of thymidylate synthase: target for rational drug designL W Hardy, J S Finer-Moore, W R Montfort, et al.
Journal of Molecular Biology|March 26, 1998
Contributions of orientation and hydrogen bonding to catalysis in Asn229 mutants of thymidylate synthaseJ S Finer-Moore, L Liu, D L Birdsall, et al.
The Journal of Biological Chemistry|July 25, 1991
Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor. A low resolution projection structure of the ligand-binding domainI Lax, A K Mitra, C Ravera, et al.
Journal of Medicinal Chemistry|November 27, 2014
Alanine mutants of the interface residues of human thymidylate synthase decode key features of the binding mode of allosteric anticancer peptidesAnna Tochowicz, Matteo Santucci, Puneet Saxena, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 29, 2011
EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts a unique dimeric structure among helix-turn-helix proteinsOren S Rosenberg, Cole Dovey, Michael Tempesta, et al.
Pageof 48

Showing results (341-350 of 475) with videos related to

Sort By:
Pageof 48
ACS Biomaterials Science & Engineering|January 12, 2021
Shell Structure and Growth in the Base Plate of the Barnacle <i>Amphibalanus amphitrite</i>Bradley T De Gregorio, Rhonda M Stroud, Daniel K Burden, et al.
Journal of Molecular Biology|November 25, 1998
Inactivity of N229A thymidylate synthase due to water-mediated effects: isolating a late stage in methyl transferC L Reyes, C R Sage, E E Rutenber, et al.
Circulation|June 5, 2014
Screening for acute IKr block is insufficient to detect torsades de pointes liability: role of late sodium currentTao Yang, Young Wook Chun, Dina M Stroud, et al.
Plos One|May 8, 2020
Diversity in kinetics correlated with structure in nano body-stabilized LacYHemant Kumar, Janet Finer-Moore, Irina Smirnova, et al.
Biochemistry|September 30, 1998
D221 in thymidylate synthase controls conformation change, and thereby opening of the imidazolidineC R Sage, M D Michelitsch, T J Stout, et al.
Science (New York, N.Y.)|January 23, 1987
Atomic structure of thymidylate synthase: target for rational drug designL W Hardy, J S Finer-Moore, W R Montfort, et al.
Journal of Molecular Biology|March 26, 1998
Contributions of orientation and hydrogen bonding to catalysis in Asn229 mutants of thymidylate synthaseJ S Finer-Moore, L Liu, D L Birdsall, et al.
The Journal of Biological Chemistry|July 25, 1991
Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor. A low resolution projection structure of the ligand-binding domainI Lax, A K Mitra, C Ravera, et al.
Journal of Medicinal Chemistry|November 27, 2014
Alanine mutants of the interface residues of human thymidylate synthase decode key features of the binding mode of allosteric anticancer peptidesAnna Tochowicz, Matteo Santucci, Puneet Saxena, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 29, 2011
EspR, a key regulator of Mycobacterium tuberculosis virulence, adopts a unique dimeric structure among helix-turn-helix proteinsOren S Rosenberg, Cole Dovey, Michael Tempesta, et al.
Pageof 48