The intriguing Cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding

@inproceedings{Solbak2010TheIC,
  title={The intriguing Cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding},
  author={Sara M{\O} Solbak and Tove Ragna Reksten and Victor Wray and Ulrich Schubert and Ole Horvli and Arnt Johan Raae and Petra Henklein and Peter Henklein and Ren{\'e} R{\"o}der and David Mitzner and Ulrich S. Schubert and Torgils Fossen},
  booktitle={BMC Structural Biology},
  year={2010}
}
BackgroundCyclophilin A (CypA) represents a potential target for antiretroviral therapy since inhibition of CypA suppresses human immunodeficiency virus type 1 (HIV-1) replication, although the mechanism through which CypA modulates HIV-1 infectivity still remains unclear. The interaction of HIV-1 viral protein R (Vpr) with the human peptidyl prolyl isomerase CypA is known to occur in vitro and in vivo. However, the nature of the interaction of CypA with Pro-35 of N-terminal Vpr has remained… CONTINUE READING
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HIGHLY INFLUENCED

References

Publications referenced by this paper.
SHOWING 1-10 OF 52 REFERENCES

Catalysis of cis/trans isomerisation in native HIV-1 capsid by human CypA

DA Bosco, EZ Eisenmesser, S Pochapsky, WI Sundsquist, D Kern
  • PNAS
  • 2002
VIEW 16 EXCERPTS
HIGHLY INFLUENTIAL