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

Li-Jun Bi

Showing results (51-60 of 53) with videos related to

Pageof 6
Sort By:
You have reached the last page of results.This site can display upto 53 results.
Antimicrobial Agents and Chemotherapy|December 25, 2013
Binding pocket alterations in dihydrofolate synthase confer resistance to para-aminosalicylic acid in clinical isolates of Mycobacterium tuberculosisFei Zhao, Xu-De Wang, Luke N Erber, et al.
Ebiomedicine|April 7, 2018
Identification of Serine 119 as an Effective Inhibitor Binding Site of M. tuberculosis Ubiquitin-like Protein Ligase PafA Using Purified Proteins and M. smegmatisHe-Wei Jiang, Daniel M Czajkowsky, Tao Wang, et al.
The FEBS Journal|March 5, 2013
Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferaseQun-Fang Zhang, Qunfang Zhang, Jing Gu, et al.
Pageof 6

Showing results (51-60 of 53) with videos related to

Sort By:
Pageof 6
You have reached the last page of results.This site can display upto 53 results.
Antimicrobial Agents and Chemotherapy|December 25, 2013
Binding pocket alterations in dihydrofolate synthase confer resistance to para-aminosalicylic acid in clinical isolates of Mycobacterium tuberculosisFei Zhao, Xu-De Wang, Luke N Erber, et al.
Ebiomedicine|April 7, 2018
Identification of Serine 119 as an Effective Inhibitor Binding Site of M. tuberculosis Ubiquitin-like Protein Ligase PafA Using Purified Proteins and M. smegmatisHe-Wei Jiang, Daniel M Czajkowsky, Tao Wang, et al.
The FEBS Journal|March 5, 2013
Reversibly acetylated lysine residues play important roles in the enzymatic activity of Escherichia coli N-hydroxyarylamine O-acetyltransferaseQun-Fang Zhang, Qunfang Zhang, Jing Gu, et al.
Pageof 6