Rv2969c, essential for optimal growth in Mycobacterium tuberculosis, is a DsbA-like enzyme that interacts with VKOR-derived peptides and has atypical features of DsbA-like disulfid...

Por Premkumar, Lakshmanane, Heras, Begoña, Duprez, Wilko, Walden, Patricia, Halili, Maria, Kurth, Fabian, Fairlie, David P., Martin, Jennifer L.
Publicado em 2013

Antifibrotic activity of an inhibitor of histone deacetylases in DOCA-salt hypertensive rats

Por Iyer, Abishek, Fenning, Andrew, Lim, Junxian, Le, Giang T, Reid, Robert C, Halili, Maria A, Fairlie, David P, Brown, Lindsay
Publicado em 2010

The α-Proteobacteria Wolbachia pipientis Protein Disulfide Machinery Has a Regulatory Mechanism Absent in γ-Proteobacteria

Por Walden, Patricia M., Halili, Maria A., Archbold, Julia K., Lindahl, Fredrik, Fairlie, David P., Inaba, Kenji, Martin, Jennifer L.
Publicado em 2013

Structure of the Acinetobacter baumannii Dithiol Oxidase DsbA Bound to Elongation Factor EF-Tu Reveals a Novel Protein Interaction Site

Por Premkumar, Lakshmanane, Kurth, Fabian, Duprez, Wilko, Grøftehauge, Morten K., King, Gordon J., Halili, Maria A., Heras, Begoña, Martin, Jennifer L.
Publicado em 2014

Disarming Burkholderia pseudomallei: Structural and Functional Characterization of a Disulfide Oxidoreductase (DsbA) Required for Virulence In Vivo

Por Ireland, Philip M., McMahon, Róisín M., Marshall, Laura E., Halili, Maria, Furlong, Emily, Tay, Stephanie, Martin, Jennifer L., Sarkar-Tyson, Mitali
Publicado em 2014

Comparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct Classes

Por Kurth, Fabian, Rimmer, Kieran, Premkumar, Lakshmanane, Mohanty, Biswaranjan, Duprez, Wilko, Halili, Maria A., Shouldice, Stephen R., Heras, Begoña, Fairlie, David P., Scanlon, Martin J., Martin, Jennifer L.
Publicado em 2013