TitleAssociate Professor
InstitutionBaylor College of Medicine
DepartmentDepartment of Biochemistry & Molecular Biology
AddressOne Baylor Plaza
Houston, TX 77030
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    Collapse Biography 
    Collapse awards and honors
    2011 - 2012Junior Faculty Research Award , The Gillson-Longenbaugh Foundation
    2008 - 2010Beginning Grant-in-Aid Award, American Heart Association
    2001 - 2003Postdoctoral Fellowship, The Irvington Institute for Immunological Research
    1997 - 2000British Overseas Research Student (ORS) Awards, United Kingdom
    1997 - 2000Cambridge Overseas Trust Studentship, University of Cambridge

    Collapse Overview 
    Collapse overview
    The research interest in our laboratory is focused on the following topics:

    Epigenetic Regulation in Embryonic Stem Cells and Cancer Stem Cells
    Polycomb group proteins (PcGs) and Trithorax group proteins (TrxG) are evolutionarily conserved regulatory factors that regulate directly the expression of hundreds of genes involved in differentiation, development, cell fate decisions, stem cell self renewal, X-inactivation in females and genomic imprinting. Mutations of these proteins are implicated in defects in stem cell fates and their abnormal levels show good correlation with the severity and invasiveness of at least 11 cancer types including prostate cancer and breast cancer. Our laboratory is combining bioinformatics, biochemistry, biophysics and structural biology approaches to elucidate the molecular mechanisms of PcG and TrxG-mediated epigenetic regulation in embryonic stem cells and cancer stem cells. Ultimately, the insights gained from these structural and functional studies are expected to aid in the development of therapeutic agents for clinical intervention.

    Actin Cytoskeleton in Signal Transduction
    Actin is the most abundant protein in eukaryotic cells. It exists primarily as monomers (G-actin) bound by G-actin binding proteins that prevent spontaneous nucleation of new actin filaments, making nucleation the rate-limiting step in forming filamentous actin (F-actin). In response to cellular signals, specific actin nucleators initiate actin polymerization in a tight temporally and spatially controlled manner, which regulates many fundamental cellular processes including cellular motility, cell shape and polarity determination, and embryonic development. Understanding the de novo actin nucleation in response to stimuli lies in the core of modern biology. Our laboratory is combining bioinformatics, biochemistry and structural biology tools to investigate the molecular mechanisms of actin cytoskeleton in signal transduction.

    Mechanisms of Influenza Virus Infection
    Influenza virus is a negative-stranded RNA virus belonging to orthomyxoviridae family. Infections caused by influenza A and B viruses remain a major source of human morbidity and mortality worldwide, due to naturally evolving strains and to their potential use as man-made bio-weapons by terrorists. They both have a major surface glycoprotein HA that are responsible for binding to cell-surface receptors and for entering into host cells for replication. We are investigating the structures and functions of influenza A and B virus HAs. These include influenza A virus H1N1, H3N2, H5N1 and influenza B virus. Development of anti-influenza inhibitors is also underway.

    Collapse Research 
    Collapse research activities and funding
    R01AI067839     (WANG, QINGHUA)Feb 3, 2009 - Jan 31, 2015
    Structural and Functional Study of Influenza Virus Hemagglutinin
    Role: Principal Investigator

    R01GM116280     (WANG, QINGHUA)Jan 1, 2016 - Dec 31, 2020
    Molecular Mechanisms of Actin Cytoskeleton Dynamics
    Role: Principal Investigator

    R01GM127628     (MA, JIANPENG)Jun 1, 2018 - Feb 28, 2022
    New Methods for Large-scale Computer Simulation
    Role: Co-Principal Investigator

    Collapse Bibliographic 
    Collapse selected publications
    Publications listed below are automatically derived from MEDLINE/PubMed and other sources, which might result in incorrect or missing publications. Faculty can login to make corrections and additions.
    Newest   |   Oldest   |   Most Cited   |   Most Discussed   |   Timeline   |   Field Summary   |   Plain Text
    PMC Citations indicate the number of times the publication was cited by articles in PubMed Central, and the Altmetric score represents citations in news articles and social media. (Note that publications are often cited in additional ways that are not shown here.) Fields are based on how the National Library of Medicine (NLM) classifies the publication's journal and might not represent the specific topic of the publication. Translation tags are based on the publication type and the MeSH terms NLM assigns to the publication. Some publications (especially newer ones and publications not in PubMed) might not yet be assigned Field or Translation tags.) Click a Field or Translation tag to filter the publications.
    1. Du J, Kirk B, Zeng J, Ma J, Wang Q. Three classes of response elements for human PRC2 and MLL1/2-Trithorax complexes. Nucleic Acids Res. 2018 09 28; 46(17):8848-8864. PMID: 29992232.
      Citations: 3     Fields:    Translation:HumansCells
    2. Ni F, Kondrashkina E, Wang Q. Determinant of receptor-preference switch in influenza hemagglutinin. Virology. 2018 01 01; 513:98-107. PMID: 29055255.
      Citations: 3     Fields:    Translation:HumansCells
    3. Chen X, Ni F, Kondrashkina E, Ma J, Wang Q. Mechanisms of leiomodin 2-mediated regulation of actin filament in muscle cells. Proc Natl Acad Sci U S A. 2015 Oct 13; 112(41):12687-92. PMID: 26417072.
      Citations: 15     Fields:    Translation:HumansAnimalsCells
    4. Ni F, Kondrashkina E, Wang Q. Structural and Functional Studies of Influenza Virus A/H6 Hemagglutinin. PLoS One. 2015; 10(7):e0134576. PMID: 26226046.
      Citations: 10     Fields:    Translation:HumansAnimalsCells
    5. Ni F, Chen X, Shen J, Wang Q. Structural insights into the membrane fusion mechanism mediated by influenza virus hemagglutinin. Biochemistry. 2014 Feb 11; 53(5):846-54. PMID: 24433110.
      Citations: 7     Fields:    Translation:Cells
    6. Ni F, Mbawuike IN, Kondrashkina E, Wang Q. The roles of hemagglutinin Phe-95 in receptor binding and pathogenicity of influenza B virus. Virology. 2014 Feb; 450-451:71-83. PMID: 24503069.
      Citations: 7     Fields:    Translation:HumansAnimalsCells
    7. Ni F, Kondrashkina E, Wang Q. Structural basis for the divergent evolution of influenza B virus hemagglutinin. Virology. 2013 Nov; 446(1-2):112-22. PMID: 24074573.
      Citations: 25     Fields:    Translation:HumansCells
    8. Chen X, Ni F, Tian X, Kondrashkina E, Wang Q, Ma J. Structural basis of actin filament nucleation by tandem W domains. Cell Rep. 2013 Jun 27; 3(6):1910-20. PMID: 23727244.
      Citations: 11     Fields:    Translation:HumansAnimalsCells
    9. Zeng J, Kirk BD, Gou Y, Wang Q, Ma J. Genome-wide polycomb target gene prediction in Drosophila melanogaster. Nucleic Acids Res. 2012 Jul; 40(13):5848-63. PMID: 22416065.
      Citations: 10     Fields:    Translation:AnimalsCells
    10. Chen X, Wang Q, Ni F, Ma J. Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement. Proc Natl Acad Sci U S A. 2010 Jun 22; 107(25):11352-7. PMID: 20534430.
      Citations: 109     Fields:    Translation:AnimalsCells
    11. Shen J, Ma J, Wang Q. Evolutionary trends of A(H1N1) influenza virus hemagglutinin since 1918. PLoS One. 2009 Nov 17; 4(11):e7789. PMID: 19924230.
      Citations: 26     Fields:    Translation:HumansAnimalsCellsPHPublic Health
    12. Yu K, Luo C, Qin G, Xu Z, Li N, Liu H, Shen X, Ma J, Wang Q, Yang C, Zhu W, Jiang H. Why are oseltamivir and zanamivir effective against the newly emerged influenza A virus (A/H1N1)? Cell Res. 2009 Oct; 19(10):1221-4. PMID: 19770846.
      Citations: 9     Fields:    Translation:HumansCells
    13. Ni F, Poon BK, Wang Q, Ma J. Application of normal-mode refinement to X-ray crystal structures at the lower resolution limit. Acta Crystallogr D Biol Crystallogr. 2009 Jul; 65(Pt 7):633-43. PMID: 19564683.
      Citations: 6     Fields:    Translation:AnimalsCells
    14. Chen X, Lu M, Poon BK, Wang Q, Ma J. Structural improvement of unliganded simian immunodeficiency virus gp120 core by normal-mode-based X-ray crystallographic refinement. Acta Crystallogr D Biol Crystallogr. 2009 Apr; 65(Pt 4):339-47. PMID: 19307715.
      Citations: 12     Fields:    Translation:Cells
    15. Shen J, Kirk BD, Ma J, Wang Q. Diversifying selective pressure on influenza B virus hemagglutinin. J Med Virol. 2009 Jan; 81(1):114-24. PMID: 19031453.
      Citations: 17     Fields:    Translation:Cells
    16. Cheng F, Wang Q, Chen M, Quiocho FA, Ma J. Molecular docking study of the interactions between the thioesterase domain of human fatty acid synthase and its ligands. Proteins. 2008 Mar; 70(4):1228-34. PMID: 17847090.
      Citations: 10     Fields:    Translation:HumansCells
    17. Wang Q, Cheng F, Lu M, Tian X, Ma J. Crystal structure of unliganded influenza B virus hemagglutinin. J Virol. 2008 Mar; 82(6):3011-20. PMID: 18184701.
      Citations: 50     Fields:    Translation:Cells
    18. Wang Q, Tian X, Chen X, Ma J. Structural basis for receptor specificity of influenza B virus hemagglutinin. Proc Natl Acad Sci U S A. 2007 Oct 23; 104(43):16874-9. PMID: 17942670.
      Citations: 29     Fields:    Translation:HumansAnimalsCells
    19. Chen X, Poon BK, Dousis A, Wang Q, Ma J. Normal-mode refinement of anisotropic thermal parameters for potassium channel KcsA at 3.2 A crystallographic resolution. Structure. 2007 Aug; 15(8):955-62. PMID: 17698000.
      Citations: 22     Fields:    Translation:Cells
    20. Poon BK, Chen X, Lu M, Vyas NK, Quiocho FA, Wang Q, Ma J. Normal mode refinement of anisotropic thermal parameters for a supramolecular complex at 3.42-A crystallographic resolution. Proc Natl Acad Sci U S A. 2007 May 08; 104(19):7869-74. PMID: 17470791.
      Citations: 35     Fields:    Translation:Cells
    21. Wu Y, Tian X, Lu M, Chen M, Wang Q, Ma J. Folding of small helical proteins assisted by small-angle X-ray scattering profiles. Structure. 2005 Nov; 13(11):1587-97. PMID: 16271882.
      Citations: 13     Fields:    Translation:AnimalsCells
    22. Wu Y, Chen M, Lu M, Wang Q, Ma J. Determining protein topology from skeletons of secondary structures. J Mol Biol. 2005 Jul 15; 350(3):571-86. PMID: 15961102.
      Citations: 10     Fields:    Translation:Cells
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