V Pancholi

Summary

Affiliation: The Rockefeller University
Country: USA

Publications

  1. pmc Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptococcal surface dehydrogenase: signal transduction between streptococci and pharyngeal cells
    V Pancholi
    Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York 10021, USA
    J Exp Med 186:1633-43. 1997
  2. ncbi request reprint alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    V Pancholi
    Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York 10021, USA
    J Biol Chem 273:14503-15. 1998
  3. ncbi request reprint Multifunctional alpha-enolase: its role in diseases
    V Pancholi
    Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NewYork 10021, USA
    Cell Mol Life Sci 58:902-20. 2001
  4. pmc Group A streptococci bind to mucin and human pharyngeal cells through sialic acid-containing receptors
    P A Ryan
    Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York 10021, USA
    Infect Immun 69:7402-12. 2001
  5. pmc A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    V Pancholi
    Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, New York 10021
    J Exp Med 176:415-26. 1992
  6. pmc Induction of lysogenic bacteriophage and phage-associated toxin from group a streptococci during coculture with human pharyngeal cells
    T B Broudy
    Department of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, New York 10021, USA
    Infect Immun 69:1440-3. 2001
  7. pmc Characterization and biological properties of a new staphylococcal exotoxin
    K Ren
    Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York 10021
    J Exp Med 180:1675-83. 1994
  8. ncbi request reprint Differential expression of the enolase gene under in vivo versus in vitro growth conditions of Aeromonas hydrophila
    Jian Sha
    Department of Microbiology and Immunology, 301 University Blvd, Medical Research Building, The University of Texas Medical Branch, Galveston, TX 77555 1070, USA
    Microb Pathog 34:195-204. 2003

Collaborators

Detail Information

Publications8

  1. pmc Regulation of the phosphorylation of human pharyngeal cell proteins by group A streptococcal surface dehydrogenase: signal transduction between streptococci and pharyngeal cells
    V Pancholi
    Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York 10021, USA
    J Exp Med 186:1633-43. 1997
    ....
  2. ncbi request reprint alpha-enolase, a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    V Pancholi
    Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York 10021, USA
    J Biol Chem 273:14503-15. 1998
    ..Our findings, showing both the protected protease activity of SEN-bound plasmin and SEN-specific immune responses, provide evidence for an important role of SEN in the disease process and post-streptococcal autoimmune diseases...
  3. ncbi request reprint Multifunctional alpha-enolase: its role in diseases
    V Pancholi
    Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, NewYork 10021, USA
    Cell Mol Life Sci 58:902-20. 2001
    ..In addition to this property, its ability to function as a heat-shock protein and to bind cytoskeletal and chromatin structures indicate that enolase may play a crucial role in transcription and a variety of pathophysiological processes...
  4. pmc Group A streptococci bind to mucin and human pharyngeal cells through sialic acid-containing receptors
    P A Ryan
    Laboratory of Bacterial Pathogenesis and Immunology, The Rockefeller University, New York, New York 10021, USA
    Infect Immun 69:7402-12. 2001
    ..The results are the first to show that sialic acid not only is involved in the binding of the streptococci to mucin but also plays an important role in adherence of group A streptococci to the pharyngeal cell surface...
  5. pmc A major surface protein on group A streptococci is a glyceraldehyde-3-phosphate-dehydrogenase with multiple binding activity
    V Pancholi
    Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, New York 10021
    J Exp Med 176:415-26. 1992
    ..The multiple binding capacity of the SDH in conjunction with its GAPDH activity may play a role in the colonization, internalization, and the subsequent proliferation of group A streptococci...
  6. pmc Induction of lysogenic bacteriophage and phage-associated toxin from group a streptococci during coculture with human pharyngeal cells
    T B Broudy
    Department of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, New York 10021, USA
    Infect Immun 69:1440-3. 2001
    ..Furthermore, we show that the bacteriophage induction event is mediated by a pharyngeal cell soluble factor for which we provide an initial characterization...
  7. pmc Characterization and biological properties of a new staphylococcal exotoxin
    K Ren
    Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York 10021
    J Exp Med 180:1675-83. 1994
    ..We conclude therefore that this 25-kD protein belongs to the staphylococcal enterotoxin gene family that is capable of inducing a TSS-like illness in rabbits...
  8. ncbi request reprint Differential expression of the enolase gene under in vivo versus in vitro growth conditions of Aeromonas hydrophila
    Jian Sha
    Department of Microbiology and Immunology, 301 University Blvd, Medical Research Building, The University of Texas Medical Branch, Galveston, TX 77555 1070, USA
    Microb Pathog 34:195-204. 2003
    ..pyogenes enolase. This is a first report describing the increased expression of enolase gene in vivo that could potentially contribute to the pathogenesis of A. hydrophila infections...