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

V Mainfroid

Showing results (1-10 of 15) with videos related to

Pageof 2
Sort By:
The Journal of Biological Chemistry|June 14, 1996
Characterization of lactogen receptor-binding site 1 of human prolactinS Kinet, V Goffin, V Mainfroid, et al.
The Journal of Biological Chemistry|December 23, 1994
Evidence for a second receptor binding site on human prolactinV Goffin, I Struman, V Mainfroid, et al.
Biochemistry|April 2, 1996
Stabilization of human triosephosphate isomerase by improvement of the stability of individual alpha-helices in dimeric as well as monomeric forms of the proteinV Mainfroid, S C Mande, W G Hol, et al.
Protein Science : a Publication of the Protein Society|May 1, 1994
Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzymeS C Mande, V Mainfroid, K H Kalk, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 17, 1999
Opposing actions of intact and N-terminal fragments of the human prolactin/growth hormone family members on angiogenesis: an efficient mechanism for the regulation of angiogenesisI Struman, F Bentzien, H Lee, et al.
The Journal of Biological Chemistry|June 26, 1999
Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperaturesM Alvarez, J Wouters, D Maes, et al.
Acta Crystallographica. Section D, Biological Crystallography|July 1, 1993
Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolutionM E Noble, J P Zeelen, R K Wierenga, et al.
The Journal of Biological Chemistry|January 27, 1998
Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural propertiesM Alvarez, J P Zeelen, V Mainfroid, et al.
Journal of Molecular Biology|March 29, 1996
Three hTIM mutants that provide new insights on why TIM is a dimerV Mainfroid, P Terpstra, M Beauregard, et al.
Protein Science : a Publication of the Protein Society|December 1, 1995
Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactionsL F Delboni, S C Mande, F Rentier-Delrue, et al.
Pageof 2

Showing results (1-10 of 15) with videos related to

Sort By:
Pageof 2
The Journal of Biological Chemistry|June 14, 1996
Characterization of lactogen receptor-binding site 1 of human prolactinS Kinet, V Goffin, V Mainfroid, et al.
The Journal of Biological Chemistry|December 23, 1994
Evidence for a second receptor binding site on human prolactinV Goffin, I Struman, V Mainfroid, et al.
Biochemistry|April 2, 1996
Stabilization of human triosephosphate isomerase by improvement of the stability of individual alpha-helices in dimeric as well as monomeric forms of the proteinV Mainfroid, S C Mande, W G Hol, et al.
Protein Science : a Publication of the Protein Society|May 1, 1994
Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzymeS C Mande, V Mainfroid, K H Kalk, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 17, 1999
Opposing actions of intact and N-terminal fragments of the human prolactin/growth hormone family members on angiogenesis: an efficient mechanism for the regulation of angiogenesisI Struman, F Bentzien, H Lee, et al.
The Journal of Biological Chemistry|June 26, 1999
Lys13 plays a crucial role in the functional adaptation of the thermophilic triose-phosphate isomerase from Bacillus stearothermophilus to high temperaturesM Alvarez, J Wouters, D Maes, et al.
Acta Crystallographica. Section D, Biological Crystallography|July 1, 1993
Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolutionM E Noble, J P Zeelen, R K Wierenga, et al.
The Journal of Biological Chemistry|January 27, 1998
Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural propertiesM Alvarez, J P Zeelen, V Mainfroid, et al.
Journal of Molecular Biology|March 29, 1996
Three hTIM mutants that provide new insights on why TIM is a dimerV Mainfroid, P Terpstra, M Beauregard, et al.
Protein Science : a Publication of the Protein Society|December 1, 1995
Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactionsL F Delboni, S C Mande, F Rentier-Delrue, et al.
Pageof 2