P D Kwong

Summary

Affiliation: Columbia University
Country: USA

Publications

  1. pmc Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus
    P D Kwong
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
    J Virol 74:1961-72. 2000
  2. ncbi request reprint Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    P D Kwong
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
    Nature 393:648-59. 1998
  3. ncbi request reprint Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates
    P D Kwong
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
    Structure 8:1329-39. 2000
  4. ncbi request reprint Dimeric association and segmental variability in the structure of human CD4
    H Wu
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
    Nature 387:527-30. 1997
  5. ncbi request reprint Structural basis of cell-cell adhesion by cadherins
    L Shapiro
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032
    Nature 374:327-37. 1995
  6. ncbi request reprint Crystal structure of an HIV-binding recombinant fragment of human CD4
    S E Ryu
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032
    Nature 348:419-26. 1990

Collaborators

Detail Information

Publications6

  1. pmc Oligomeric modeling and electrostatic analysis of the gp120 envelope glycoprotein of human immunodeficiency virus
    P D Kwong
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
    J Virol 74:1961-72. 2000
    ..This dependence on charge and not structure may make electrostatic interactions between this basic region and the cell difficult to target therapeutically and may also provide a means of viral escape from immune system surveillance...
  2. ncbi request reprint Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    P D Kwong
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
    Nature 393:648-59. 1998
    ..Our results provide a framework for understanding the complex biology of HIV entry into cells and should guide efforts to intervene...
  3. ncbi request reprint Structures of HIV-1 gp120 envelope glycoproteins from laboratory-adapted and primary isolates
    P D Kwong
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
    Structure 8:1329-39. 2000
    ..This revealed atomic details of gp120-receptor interactions and suggested multiple mechanisms of immune evasion...
  4. ncbi request reprint Dimeric association and segmental variability in the structure of human CD4
    H Wu
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032, USA
    Nature 387:527-30. 1997
    ..Dynamic light scattering measurements and chemical crosslinking of sCD4 corroborate dimerization at high protein concentration. We suggest that such dimers mayhave relevance as mediators of signal transduction in T cells...
  5. ncbi request reprint Structural basis of cell-cell adhesion by cadherins
    L Shapiro
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032
    Nature 374:327-37. 1995
    ..This cell-adhesion zipper may provide a mechanism to marshal individual molecular adhesive interactions into strong bonds between cells...
  6. ncbi request reprint Crystal structure of an HIV-binding recombinant fragment of human CD4
    S E Ryu
    Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York 10032
    Nature 348:419-26. 1990
    ..Domain D2 is distinguished by a variation on the beta-strand topologies of antibody domains and by an intra-sheet disulphide bridge...