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

C Georgopoulos

Showing results (101-110 of 146) with videos related to

Pageof 15
Sort By:
Journal of Bacteriology|August 1, 1993
Identification and transcriptional analysis of the Escherichia coli htrE operon which is homologous to pap and related pilin operonsS Raina, D Missiakas, L Baird, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 22, 1994
NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domainT Szyperski, M Pellecchia, D Wall, et al.
The Journal of Biological Chemistry|July 25, 1988
Purification and properties of the NusB protein of Escherichia coliJ Swindle, M Zylicz, C Georgopoulos, et al.
Clinical and Experimental Immunology|November 1, 1994
Heat shock proteins as carrier molecules: in vivo helper effect mediated by Escherichia coli GroEL and DnaK proteins requires cross-linking with antigenC Barrios, C Georgopoulos, P H Lambert, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 1, 1991
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaKK Liberek, J Marszalek, D Ang, et al.
The Journal of Biological Chemistry|August 5, 1991
The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target proteinK Liberek, D Skowyra, M Zylicz, et al.
The Journal of Biological Chemistry|December 25, 1991
Biological role and regulation of the universally conserved heat shock proteinsD Ang, K Liberek, D Skowyra, et al.
The Journal of Biological Chemistry|March 30, 2001
Structure-function analysis of the zinc-binding region of the Clpx molecular chaperoneB Banecki, A Wawrzynow, J Puzewicz, et al.
Infection and Immunity|March 1, 1990
Synthesis of a select group of proteins by Neisseria gonorrhoeae in response to thermal stressM L Woods, R Bonfiglioli, Z A McGee, et al.
Nature|April 14, 1994
Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein foldingS M van der Vies, A A Gatenby, C Georgopoulos
Pageof 15

Showing results (101-110 of 146) with videos related to

Sort By:
Pageof 15
Journal of Bacteriology|August 1, 1993
Identification and transcriptional analysis of the Escherichia coli htrE operon which is homologous to pap and related pilin operonsS Raina, D Missiakas, L Baird, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 22, 1994
NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domainT Szyperski, M Pellecchia, D Wall, et al.
The Journal of Biological Chemistry|July 25, 1988
Purification and properties of the NusB protein of Escherichia coliJ Swindle, M Zylicz, C Georgopoulos, et al.
Clinical and Experimental Immunology|November 1, 1994
Heat shock proteins as carrier molecules: in vivo helper effect mediated by Escherichia coli GroEL and DnaK proteins requires cross-linking with antigenC Barrios, C Georgopoulos, P H Lambert, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 1, 1991
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaKK Liberek, J Marszalek, D Ang, et al.
The Journal of Biological Chemistry|August 5, 1991
The Escherichia coli DnaK chaperone, the 70-kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target proteinK Liberek, D Skowyra, M Zylicz, et al.
The Journal of Biological Chemistry|December 25, 1991
Biological role and regulation of the universally conserved heat shock proteinsD Ang, K Liberek, D Skowyra, et al.
The Journal of Biological Chemistry|March 30, 2001
Structure-function analysis of the zinc-binding region of the Clpx molecular chaperoneB Banecki, A Wawrzynow, J Puzewicz, et al.
Infection and Immunity|March 1, 1990
Synthesis of a select group of proteins by Neisseria gonorrhoeae in response to thermal stressM L Woods, R Bonfiglioli, Z A McGee, et al.
Nature|April 14, 1994
Bacteriophage T4 encodes a co-chaperonin that can substitute for Escherichia coli GroES in protein foldingS M van der Vies, A A Gatenby, C Georgopoulos
Pageof 15