메뉴 건너뛰기




Volumn 416, Issue 3-4, 2011, Pages 252-257

A structural model of the HIV-1 Rev-integrase complex: The molecular basis of integrase regulation by Rev

Author keywords

Docking; HIV 1; Integrase; Modeling; Peptides; Protein protein interaction; Rev

Indexed keywords

DIMER; DNA POLYMERASE REV1; INTEGRASE; LENS EPITHELIUM DERIVED GROWTH FACTOR; MONOMER; MULTIPROTEIN COMPLEX; TETRAMER; VIRUS DNA;

EID: 84855879701     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.10.116     Document Type: Article
Times cited : (3)

References (34)
  • 1
    • 73949140662 scopus 로고    scopus 로고
    • Integration of HIV-1 DNA is regulated by interplay between viral rev and cellular LEDGF/p75 proteins
    • Levin A., Rosenbluh J., Hayouka Z., Friedler A., Loyter A. Integration of HIV-1 DNA is regulated by interplay between viral rev and cellular LEDGF/p75 proteins. Mol. Med. 2010, 16:34-44.
    • (2010) Mol. Med. , vol.16 , pp. 34-44
    • Levin, A.1    Rosenbluh, J.2    Hayouka, Z.3    Friedler, A.4    Loyter, A.5
  • 2
    • 77955686538 scopus 로고    scopus 로고
    • Specific eradication of HIV-1 from infected cultured cells
    • Levin A., Hayouka Z., Friedler A., Loyter A. Specific eradication of HIV-1 from infected cultured cells. AIDS Res. Ther. 2010, 7:31.
    • (2010) AIDS Res. Ther. , vol.7 , pp. 31
    • Levin, A.1    Hayouka, Z.2    Friedler, A.3    Loyter, A.4
  • 4
    • 58349109557 scopus 로고    scopus 로고
    • Peptides derived from HIV-1 integrase that bind Rev stimulate viral genome integration
    • Levin A., Hayouka Z., Helfer M., Brack-Werner R., Friedler A., Loyter A. Peptides derived from HIV-1 integrase that bind Rev stimulate viral genome integration. PLoS One 2009, 4:e4155.
    • (2009) PLoS One , vol.4
    • Levin, A.1    Hayouka, Z.2    Helfer, M.3    Brack-Werner, R.4    Friedler, A.5    Loyter, A.6
  • 6
    • 0036062256 scopus 로고    scopus 로고
    • Charting HIV's remarkable voyage through the cell: Basic science as a passport to future therapy
    • Greene W.C., Peterlin B.M. Charting HIV's remarkable voyage through the cell: Basic science as a passport to future therapy. Nat. Med. 2002, 8:673-680.
    • (2002) Nat. Med. , vol.8 , pp. 673-680
    • Greene, W.C.1    Peterlin, B.M.2
  • 7
    • 18744371922 scopus 로고    scopus 로고
    • HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins
    • Van Maele B., Debyser Z. HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins. AIDS Rev 2005, 7:26-43.
    • (2005) AIDS Rev , vol.7 , pp. 26-43
    • Van Maele, B.1    Debyser, Z.2
  • 8
    • 77958010223 scopus 로고    scopus 로고
    • Reverse transcription and integration
    • Caister Academic Press, Norfolk, UK, R. Kurth, N. Bannert (Eds.)
    • Engelman A. Reverse transcription and integration. Retroviruses: Molecular Biology, Genomics and Pathogenesis 2010, 129-159. Caister Academic Press, Norfolk, UK. R. Kurth, N. Bannert (Eds.).
    • (2010) Retroviruses: Molecular Biology, Genomics and Pathogenesis , pp. 129-159
    • Engelman, A.1
  • 12
    • 63549089353 scopus 로고    scopus 로고
    • Raltegravir, elvitegravir, and metoogravir: the birth of "me-too" HIV-1 integrase inhibitors
    • Serrao E., Odde S., Ramkumar K., Neamati N. Raltegravir, elvitegravir, and metoogravir: the birth of "me-too" HIV-1 integrase inhibitors. Retrovirology 2009, 6:25.
    • (2009) Retrovirology , vol.6 , pp. 25
    • Serrao, E.1    Odde, S.2    Ramkumar, K.3    Neamati, N.4
  • 15
    • 29244450157 scopus 로고    scopus 로고
    • Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions
    • Li L., Li H.S., Pauza C.D., Bukrinsky M., Zhao R.Y. Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions. Cell Res. 2005, 15:923-934.
    • (2005) Cell Res. , vol.15 , pp. 923-934
    • Li, L.1    Li, H.S.2    Pauza, C.D.3    Bukrinsky, M.4    Zhao, R.Y.5
  • 16
    • 69249219158 scopus 로고    scopus 로고
    • Measurement of human immunodeficiency virus type 1 preintegration transcription by using Rev-dependent Rev-CEM cells reveals a sizable transcribing DNA population comparable to that from proviral templates
    • Iyer S.R., Yu D., Biancotto A., Margolis L.B., Wu Y. Measurement of human immunodeficiency virus type 1 preintegration transcription by using Rev-dependent Rev-CEM cells reveals a sizable transcribing DNA population comparable to that from proviral templates. J. Virol. 2009, 83:8662-8673.
    • (2009) J. Virol. , vol.83 , pp. 8662-8673
    • Iyer, S.R.1    Yu, D.2    Biancotto, A.3    Margolis, L.B.4    Wu, Y.5
  • 17
    • 77954654457 scopus 로고    scopus 로고
    • Stimulation of the HIV-1 integrase enzymatic activity and cDNA integration by a peptide derived from the integrase protein
    • Levin A., Hayouka Z., Helfer M., Brack-Werner R., Friedler A., Loyter A. Stimulation of the HIV-1 integrase enzymatic activity and cDNA integration by a peptide derived from the integrase protein. Biopolymers 2010, 93:740-751.
    • (2010) Biopolymers , vol.93 , pp. 740-751
    • Levin, A.1    Hayouka, Z.2    Helfer, M.3    Brack-Werner, R.4    Friedler, A.5    Loyter, A.6
  • 18
    • 52949106060 scopus 로고    scopus 로고
    • Peptides derived from HIV-1 Rev inhibit HIV-1 integrase in a shiftide mechanism
    • Hayouka Z., Rosenbluh J., Levin A., Maes M., Loyter A., Friedler A. Peptides derived from HIV-1 Rev inhibit HIV-1 integrase in a shiftide mechanism. Biopolymers 2008, 90:481-487.
    • (2008) Biopolymers , vol.90 , pp. 481-487
    • Hayouka, Z.1    Rosenbluh, J.2    Levin, A.3    Maes, M.4    Loyter, A.5    Friedler, A.6
  • 22
    • 77951232176 scopus 로고    scopus 로고
    • FiberDock: Flexible induced-fit backbone refinement in molecular docking
    • Mashiach E., Nussinov R., Wolfson H.J. FiberDock: Flexible induced-fit backbone refinement in molecular docking. Proteins 2010, 78:1503-1519.
    • (2010) Proteins , vol.78 , pp. 1503-1519
    • Mashiach, E.1    Nussinov, R.2    Wolfson, H.J.3
  • 23
    • 18844462557 scopus 로고    scopus 로고
    • FastContact: rapid estimate of contact and binding free energies
    • Camacho C.J., Zhang C. FastContact: rapid estimate of contact and binding free energies. Bioinformatics 2005, 21:2534-2536.
    • (2005) Bioinformatics , vol.21 , pp. 2534-2536
    • Camacho, C.J.1    Zhang, C.2
  • 24
    • 38849181672 scopus 로고    scopus 로고
    • Coil check: an interactive server for the analysis of interface regions in coiled coils
    • Alva V., Devi D.P., Sowdhamini R. Coil check: an interactive server for the analysis of interface regions in coiled coils. Protein Pept. Lett. 2008, 15:33-38.
    • (2008) Protein Pept. Lett. , vol.15 , pp. 33-38
    • Alva, V.1    Devi, D.P.2    Sowdhamini, R.3
  • 25
    • 28444445583 scopus 로고    scopus 로고
    • Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75
    • Cherepanov P., Ambrosio A.L., Rahman S., Ellenberger T., Engelman A. Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75. Proc. Natl. Acad. Sci. USA 2005, 102:17308-17313.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17308-17313
    • Cherepanov, P.1    Ambrosio, A.L.2    Rahman, S.3    Ellenberger, T.4    Engelman, A.5
  • 26
    • 0037126629 scopus 로고    scopus 로고
    • Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein
    • Wang J.Y., Ling H., Yang W., Craigie R. Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein. Embo J. 2001, 20:7333-7343.
    • (2001) Embo J. , vol.20 , pp. 7333-7343
    • Wang, J.Y.1    Ling, H.2    Yang, W.3    Craigie, R.4
  • 27
    • 77949365510 scopus 로고    scopus 로고
    • Retroviral intasome assembly and inhibition of DNA strand transfer
    • Hare S., Gupta S.S., Valkov E., Engelman A., Cherepanov P. Retroviral intasome assembly and inhibition of DNA strand transfer. Nature 2010, 464:232-236.
    • (2010) Nature , vol.464 , pp. 232-236
    • Hare, S.1    Gupta, S.S.2    Valkov, E.3    Engelman, A.4    Cherepanov, P.5
  • 28
    • 84956979675 scopus 로고    scopus 로고
    • Efficient unbound docking of rigid molecules
    • LNCS, Rome, Italy, R. Guigo, D. Gusfield (Eds.)
    • Duhovny D., Nussinov R., Wolfson H.J. Efficient unbound docking of rigid molecules. Workshop on Algorithms in Bioinformatics 2002, 185-200. LNCS, Rome, Italy. R. Guigo, D. Gusfield (Eds.).
    • (2002) Workshop on Algorithms in Bioinformatics , pp. 185-200
    • Duhovny, D.1    Nussinov, R.2    Wolfson, H.J.3
  • 30
  • 31
    • 0031552370 scopus 로고    scopus 로고
    • Determination of atomic desolvation energies from the structures of crystallized proteins
    • Zhang C., Vasmatzis G., Cornette J.L., DeLisi C. Determination of atomic desolvation energies from the structures of crystallized proteins. J. Mol. Biol. 1997, 267:707-726.
    • (1997) J. Mol. Biol. , vol.267 , pp. 707-726
    • Zhang, C.1    Vasmatzis, G.2    Cornette, J.L.3    DeLisi, C.4
  • 34
    • 77954267296 scopus 로고    scopus 로고
    • FiberDock: a web server for flexible induced-fit backbone refinement in molecular docking
    • Mashiach E., Nussinov R., Wolfson H.J. FiberDock: a web server for flexible induced-fit backbone refinement in molecular docking. Nucleic Acids Res. 2010, 38:W457-W461.
    • (2010) Nucleic Acids Res. , vol.38
    • Mashiach, E.1    Nussinov, R.2    Wolfson, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.