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FEBS Letters|December 31, 2008
The FHA-containing protein GarA acts as a phosphorylation-dependent molecular switch in mycobacterial signalingPatrick England, Annemarie Wehenkel, Sonia Martins, et al.Life Science Alliance|January 9, 2023
Horizontal transfer of the rfb cluster in Leptospira is a genetic determinant of serovar identityCecilia Nieves, Antony T Vincent, Leticia Zarantonelli, et al.Acta Crystallographica. Section D, Biological Crystallography|March 23, 2013
Structure of a human IgA1 Fab fragment at 1.55 Å resolution: potential effect of the constant domains on antigen-affinity modulationAgustin Correa, Felipe Trajtenberg, Gonzalo Obal, et al.Journal of Bacteriology|September 19, 2006
The Ser/Thr protein kinase PknB is essential for sustaining mycobacterial growthPablo Fernandez, Brigitte Saint-Joanis, Nathalie Barilone, et al.Molecular Microbiology|September 3, 2003
PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosisBrigitte Boitel, Miguel Ortiz-Lombardía, Rosario Durán, et al.Proceedings of the National Academy of Sciences of the United States of America|November 7, 2007
Remodeling a DNA-binding protein as a specific in vivo inhibitor of bacterial secretin PulDBarbara Mouratou, Francis Schaeffer, Ingrid Guilvout, et al.FEBS Letters|May 6, 2006
The structure of PknB in complex with mitoxantrone, an ATP-competitive inhibitor, suggests a mode of protein kinase regulation in mycobacteriaAnnemarie Wehenkel, Pablo Fernandez, Marco Bellinzoni, et al.Molecular Microbiology|January 22, 2009
Genome-wide regulon and crystal structure of BlaI (Rv1846c) from Mycobacterium tuberculosisClaudia Sala, Ahmed Haouz, Frederick A Saul, et al.The Journal of Biological Chemistry|September 21, 2005
Identification of the critical residues involved in peptidoglycan detection by Nod1Stephen E Girardin, Muguette Jéhanno, Dominique Mengin-Lecreulx, et al.The FEBS Journal|July 27, 2019
Arabidopsis thaliana Hcc1 is a Sco-like metallochaperone for CuA assembly in Cytochrome c OxidaseMaría-Eugenia Llases, María-Natalia Lisa, Marcos N Morgada, et al.Pageof 18