New targets for inhibitors of HIV-1 replication.
作者： John P. Moore , Mario Stevenson
DOI: 10.1038/35036060
关键词: Cell fusion 、 DNA 、 Virus 、 Lipid bilayer fusion 、 Virology 、 Viral life cycle 、 Viral entry 、 Biology 、 Protease 、 Reverse transcriptase
摘要: Despite the success of protease and reverse transcriptase inhibitors, new drugs to suppress HIV-1 replication are still needed. Several other early events in viral life cycle (stages before genome is inserted into host cell DNA) susceptible drugs, including virus attachment target cells, membrane fusion post-entry such as integration, accessory-gene function assembly particles. Among these, inhibitors virus?cell integration most promising candidates.
nature.com
elsevier.com
sci-hub.se 参考文章(105)
Cecilia Cabrera, Myriam Witvrouw, Arantxa Gutierrez, Bonaventura Clotet, Miriam E Kuipers, Pieter J Swart, Dirk KF Meijer, Jan Desmyter, Erik De Clercq, Jose A Este, None, Resistance of the human immunodeficiency virus to the inhibitory action of negatively charged albumins on virus binding to CD4. AIDS Research and Human Retroviruses. ,vol. 15, pp. 1535- 1543 ,(1999) , 10.1089/088922299309829
Olivier Delézay, Djilali Hammache, Jacques Fantini, Nouara Yahi, SPC3, a V3 loop-derived synthetic peptide inhibitor of HIV-1 infection, binds to cell surface glycosphingolipids. Biochemistry. ,vol. 35, pp. 15663- 15671 ,(1996) , 10.1021/BI961205G
David C. Chan, Deborah Fass, James M. Berger, Peter S. Kim, Core Structure of gp41 from the HIV Envelope Glycoprotein Cell. ,vol. 89, pp. 263- 273 ,(1997) , 10.1016/S0092-8674(00)80205-6
M. Pritsker, P. Jones, R. Blumenthal, Y. Shai, A synthetic all d-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion Proceedings of the National Academy of Sciences of the United States of America. ,vol. 95, pp. 7287- 7292 ,(1998) , 10.1073/PNAS.95.13.7287
Jason W. Rausch, B. K. Sathyanarayana, Marion K. Bona, Stuart F. J. Le Grice, Probing Contacts between the Ribonuclease H Domain of HIV-1 Reverse Transcriptase and Nucleic Acid by Site-specific Photocross-linking Journal of Biological Chemistry. ,vol. 275, pp. 16015- 16022 ,(2000) , 10.1074/JBC.M909808199
P. Gallay, T. Hope, D. Chin, D. Trono, HIV-1 infection of nondividing cells through the recognition of integrase by the importin/karyopherin pathway. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 94, pp. 9825- 9830 ,(1997) , 10.1073/PNAS.94.18.9825
F. Cocchi, A. L. DeVico, A. Garzino-Demo, S. K. Arya, R. C. Gallo, P. Lusso, Identification of RANTES, MIP-1α, and MIP-1β as the Major HIV-Suppressive Factors Produced by CD8+ T Cells Science. ,vol. 270, pp. 1811- 1815 ,(1995) , 10.1126/SCIENCE.270.5243.1811
Jim A. Turpin, Yongsheng Song, John K. Inman, Mingjun Huang, Anders Wallqvist, Andrew Maynard, David G. Covell, William G. Rice, Ettore Appella, Synthesis and Biological Properties of Novel Pyridinioalkanoyl Thiolesters (PATE) as Anti-HIV-1 Agents That Target the Viral Nucleocapsid Protein Zinc Fingers Journal of Medicinal Chemistry. ,vol. 42, pp. 67- 86 ,(1999) , 10.1021/JM9802517
Wim Pluymers, Peter Cherepanov, Dominique Schols, Erik De Clercq, Zeger Debyser, Nuclear localization of human immunodeficiency virus type 1 integrase expressed as a fusion protein with green fluorescent protein. Virology. ,vol. 258, pp. 327- 332 ,(1999) , 10.1006/VIRO.1999.9727
Nouri Neamati, Huixiao Hong, Joshua M. Owen, Sanjay Sunder, Heather E. Winslow, John L. Christensen, He Zhao, Terrence R. Burke,, George W. A. Milne, Yves Pommier, Salicylhydrazine-containing inhibitors of HIV-1 integrase: implication for a selective chelation in the integrase active site. Journal of Medicinal Chemistry. ,vol. 41, pp. 3202- 3209 ,(1998) , 10.1021/JM9801760