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

A Jeltsch

Showing results (21-30 of 52) with videos related to

Pageof 6
Sort By:
Journal of Molecular Biology|October 8, 1998
Towards the design of rare cutting restriction endonucleases: using directed evolution to generate variants of EcoRV differing in their substrate specificity by two orders of magnitudeT Lanio, A Jeltsch, A Pingoud
Cellular and Molecular Life Sciences : CMLS|November 5, 2004
Biochemistry and biology of mammalian DNA methyltransferasesA Hermann, H Gowher, A Jeltsch
Protein Engineering|May 1, 1996
Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison with known structures of methyltransferases and isolation of catalytically inactive single mutantsA Jeltsch, T Sobotta, A Pingoud
Journal of Molecular Biology|January 27, 1999
Mutational analysis of target base flipping by the EcoRV adenine-N6 DNA methyltransferaseA Jeltsch, M Roth, T Friedrich
The EMBO Journal|December 16, 2000
DNA of Drosophila melanogaster contains 5-methylcytosineH Gowher, O Leismann, A Jeltsch
FEMS Microbiology Letters|December 1, 2001
DNA from Aspergillus flavus contains 5-methylcytosineH Gowher, K C Ehrlich, A Jeltsch
Journal of Molecular Biology|June 12, 2001
The activity of the murine DNA methyltransferase Dnmt1 is controlled by interaction of the catalytic domain with the N-terminal part of the enzyme leading to an allosteric activation of the enzyme after binding to methylated DNAM Fatemi, A Hermann, S Pradhan, et al.
Biological Chemistry|June 17, 1998
The mechanism of DNA cleavage by the type II restriction enzyme EcoRV: Asp36 is not directly involved in DNA cleavage but serves to couple indirect readout to catalysisF Stahl, W Wende, A Jeltsch, et al.
The EMBO Journal|September 16, 1996
Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzymeA Jeltsch, C Wenz, F Stahl, et al.
The Journal of Biological Chemistry|July 3, 1999
On the substrate specificity of DNA methyltransferases. adenine-N6 DNA methyltransferases also modify cytosine residues at position N4A Jeltsch, F Christ, M Fatemi, et al.
Pageof 6

Showing results (21-30 of 52) with videos related to

Sort By:
Pageof 6
Journal of Molecular Biology|October 8, 1998
Towards the design of rare cutting restriction endonucleases: using directed evolution to generate variants of EcoRV differing in their substrate specificity by two orders of magnitudeT Lanio, A Jeltsch, A Pingoud
Cellular and Molecular Life Sciences : CMLS|November 5, 2004
Biochemistry and biology of mammalian DNA methyltransferasesA Hermann, H Gowher, A Jeltsch
Protein Engineering|May 1, 1996
Structure prediction of the EcoRV DNA methyltransferase based on mutant profiling, secondary structure analysis, comparison with known structures of methyltransferases and isolation of catalytically inactive single mutantsA Jeltsch, T Sobotta, A Pingoud
Journal of Molecular Biology|January 27, 1999
Mutational analysis of target base flipping by the EcoRV adenine-N6 DNA methyltransferaseA Jeltsch, M Roth, T Friedrich
The EMBO Journal|December 16, 2000
DNA of Drosophila melanogaster contains 5-methylcytosineH Gowher, O Leismann, A Jeltsch
FEMS Microbiology Letters|December 1, 2001
DNA from Aspergillus flavus contains 5-methylcytosineH Gowher, K C Ehrlich, A Jeltsch
Journal of Molecular Biology|June 12, 2001
The activity of the murine DNA methyltransferase Dnmt1 is controlled by interaction of the catalytic domain with the N-terminal part of the enzyme leading to an allosteric activation of the enzyme after binding to methylated DNAM Fatemi, A Hermann, S Pradhan, et al.
Biological Chemistry|June 17, 1998
The mechanism of DNA cleavage by the type II restriction enzyme EcoRV: Asp36 is not directly involved in DNA cleavage but serves to couple indirect readout to catalysisF Stahl, W Wende, A Jeltsch, et al.
The EMBO Journal|September 16, 1996
Linear diffusion of the restriction endonuclease EcoRV on DNA is essential for the in vivo function of the enzymeA Jeltsch, C Wenz, F Stahl, et al.
The Journal of Biological Chemistry|July 3, 1999
On the substrate specificity of DNA methyltransferases. adenine-N6 DNA methyltransferases also modify cytosine residues at position N4A Jeltsch, F Christ, M Fatemi, et al.
Pageof 6