Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

M J Glucksman

Showing results (1-10 of 32) with videos related to

Pageof 4
Sort By:
Journal of Molecular Biology|July 20, 1992
Three-dimensional structure of a cloning vector. X-ray diffraction studies of filamentous bacteriophage M13 at 7 A resolutionM J Glucksman, S Bhattacharjee, L Makowski
Journal of Molecular Biology|January 5, 1988
Conformation of the coat protein of filamentous bacteriophage Pf1 determined by neutron diffraction from magnetically oriented gels of specifically deuterated virionsW Stark, M J Glucksman, L Makowski
Biophysical Journal|March 1, 1992
Structural polymorphism correlated to surface charge in filamentous bacteriophagesS Bhattacharjee, M J Glucksman, L Makowski
Biophysical Journal|April 1, 1992
Structural and functional studies of the metalloendopeptidase (EC 3.4.24.15) involved in degrading gonadotropin releasing hormoneM J Glucksman, M Orlowski, J L Roberts
Science (New York, N.Y.)|March 14, 1986
X-ray diffraction from magnetically oriented solutions of macromolecular assembliesM J Glucksman, R D Hay, L Makowski
Acta Biologica Et Medica Germanica|January 1, 1981
ATP-dependent proteolysis in erythroid and muscle cellsJ D Etlinger, S Speiser, E Wajnberg, et al.
Biophysical Journal|August 1, 1987
Structural responsiveness of filamentous bacteriophage Pf1: comparison of virion structure in fibers and solution. The effect of temperature and ionic strengthL Specthrie, J Greenberg, M J Glucksman, et al.
The Journal of Biological Chemistry|May 29, 1999
Zinc coordination and substrate catalysis within the neuropeptide processing enzyme endopeptidase EC 3.4.24.15. Identification of active site histidine and glutamate residuesP M Cummins, A Pabon, E H Margulies, et al.
DNA and Cell Biology|October 29, 1999
Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)E S Ferro, J W Tullai, M J Glucksman, et al.
Journal of Cell Science|October 3, 1999
Distribution of thimet oligopeptidase (E.C. 3.4.24.15) in human and rat testesC Pineau, S McCool, M J Glucksman, et al.
Pageof 4

Showing results (1-10 of 32) with videos related to

Sort By:
Pageof 4
Journal of Molecular Biology|July 20, 1992
Three-dimensional structure of a cloning vector. X-ray diffraction studies of filamentous bacteriophage M13 at 7 A resolutionM J Glucksman, S Bhattacharjee, L Makowski
Journal of Molecular Biology|January 5, 1988
Conformation of the coat protein of filamentous bacteriophage Pf1 determined by neutron diffraction from magnetically oriented gels of specifically deuterated virionsW Stark, M J Glucksman, L Makowski
Biophysical Journal|March 1, 1992
Structural polymorphism correlated to surface charge in filamentous bacteriophagesS Bhattacharjee, M J Glucksman, L Makowski
Biophysical Journal|April 1, 1992
Structural and functional studies of the metalloendopeptidase (EC 3.4.24.15) involved in degrading gonadotropin releasing hormoneM J Glucksman, M Orlowski, J L Roberts
Science (New York, N.Y.)|March 14, 1986
X-ray diffraction from magnetically oriented solutions of macromolecular assembliesM J Glucksman, R D Hay, L Makowski
Acta Biologica Et Medica Germanica|January 1, 1981
ATP-dependent proteolysis in erythroid and muscle cellsJ D Etlinger, S Speiser, E Wajnberg, et al.
Biophysical Journal|August 1, 1987
Structural responsiveness of filamentous bacteriophage Pf1: comparison of virion structure in fibers and solution. The effect of temperature and ionic strengthL Specthrie, J Greenberg, M J Glucksman, et al.
The Journal of Biological Chemistry|May 29, 1999
Zinc coordination and substrate catalysis within the neuropeptide processing enzyme endopeptidase EC 3.4.24.15. Identification of active site histidine and glutamate residuesP M Cummins, A Pabon, E H Margulies, et al.
DNA and Cell Biology|October 29, 1999
Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)E S Ferro, J W Tullai, M J Glucksman, et al.
Journal of Cell Science|October 3, 1999
Distribution of thimet oligopeptidase (E.C. 3.4.24.15) in human and rat testesC Pineau, S McCool, M J Glucksman, et al.
Pageof 4