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Trends in Microbiology|October 7, 2008
PhoP, a key player in Mycobacterium tuberculosis virulenceMichelle Ryndak, Shuishu Wang, Issar SmithBiochemistry|December 7, 2007
Structure of the DNA-binding domain of the response regulator PhoP from Mycobacterium tuberculosisShuishu Wang, Jean Engohang-Ndong, Issar SmithJournal of Bacteriology|December 2, 2009
The Mycobacterium tuberculosis high-affinity iron importer, IrtA, contains an FAD-binding domainMichelle B Ryndak, Shuishu Wang, Issar Smith, et al.ACS Omega|August 8, 2017
Asymmetric Structure of the Dimerization Domain of PhoR, a Sensor Kinase Important for the Virulence of Mycobacterium tuberculosisDaniel Xing, Michelle B Ryndak, Liqin Wang, et al.Clinical Microbiology Reviews|July 15, 2003
Mycobacterium tuberculosis pathogenesis and molecular determinants of virulenceIssar SmithMicrobes and Infection|June 6, 2003
Mycobacterium tuberculosis gene expression in macrophagesEugenie Dubnau, Issar SmithJournal of Bacteriology|December 31, 2005
Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosisG Marcela Rodriguez, Issar SmithMolecular Microbiology|March 8, 2003
Mechanisms of iron regulation in mycobacteria: role in physiology and virulenceG Marcela Rodriguez, Issar SmithBiochemistry|June 4, 2011
Structure of the response regulator PhoP from Mycobacterium tuberculosis reveals a dimer through the receiver domainSmita Menon, Shuishu WangBiochemistry|December 2, 2014
DNA consensus sequence motif for binding response regulator PhoP, a virulence regulator of Mycobacterium tuberculosisXiaoyuan He, Shuishu WangPageof 10