Clip download factor gag

Campbell, E. Forshey, B. Formation of a human immunodeficiency virus type 1 core of optimal stability is crucial for viral replication.

HIV-1 Gag: an emerging target for antiretroviral therapy. Ternois, F. The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor. Zhang, H. A cell-penetrating helical peptide as a potential HIV-1 inhibitor.

Kelly, B. Antiviral inhibition of the HIV-1 capsid protein. Lemke, C. Distinct effects of two HIV-1 capsid assembly inhibitor families that bind the same site within the N-terminal domain of the viral CA protein. Blair, W. HIV capsid is a tractable target for small molecule therapeutic intervention. Shi, J. Small-molecule inhibition of human immunodeficiency virus type 1 infection by virus capsid destabilization.

Matreyek, K. Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes. Viruses 5 , — Price, A. Host cofactors and pharmacologic ligands share an essential interface in HIV-1 capsid that is lost upon disassembly. Bhattacharya, A.

Garg, D. Advances in targeting nucleocapsid-nucleic acid interactions in HIV-1 therapy. Virus Res. Li, F. PA a potent HIV inhibitor that disrupts core condensation by targeting a late step in Gag processing. Provides the first description of the mechanism of action of an HIV-1 maturation inhibitor.

Zhou, J. Small-molecule inhibition of human immunodeficiency virus type 1 replication by specific targeting of the final step of virion maturation. Adamson, C. In vitro resistance to the human immunodeficiency virus type 1 maturation inhibitor PA Bevirimat. Nguyen, A. Retrovirology 8 , Waki, K. Structural and functional insights into the HIV-1 maturation inhibitor binding pocket.

Salzwedel, K. Maturation inhibitors: a new therapeutic class targets the virus structure. AIDS Rev. PubMed Google Scholar. Polymorphisms in Gag spacer peptide 1 confer varying levels of resistance to the HIV- 1 maturation inhibitor bevirimat. Retrovirology 7 , 36 Neil, S. Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu.

Van Damme, N. Cell Host Microbe 3 , — Together with reference , shows that tetherin blocks the release of mature particles from the plasma membrane and is counteracted by Vpu. The long cytoplasmic tail of gp41 is required in a cell type-dependent manner for HIV-1 envelope glycoprotein incorporation into virions. USA 97 , — Demonstrates that the cytoplasmic tail of HIV-1 gp41 is required for Env incorporation in physiologically relevant cell types.

Qi, M. Carlton, J. Samson, R. Snyder, J. Sengupta, P. Visualizing cell structure and function with point-localization superresolution imaging.

Cell 23 , — Milne, J. Cryo-electron microscopy—a primer for the non-microscopist. FEBS J. Martin-Fernandez, M. A 'pocket guide' to total internal reflection fluorescence.

Sekar, R. Fluorescence resonance energy transfer FRET microscopy imaging of live cell protein localizations. Deshmukh, L. Structure and dynamics of full-length HIV-1 capsid protein in solution. Morellet, N. Cashikar, A. Ganser-Pornillos, B. The structural biology of HIV assembly. Download references. The author thanks A. Ono, W. Hu, S. Van Engelenburg and members of the Freed laboratory for critical review of the manuscript and helpful discussions.

You can also search for this author in PubMed Google Scholar. Correspondence to Eric O. The electron-dense structure at the centre of the mature virus particle. The capsid is composed of an outer layer of capsid protein surrounding the viral RNA genome and the viral enzymes reverse transcriptase and integrase.

The morphological transition from the immature virus particle, in which uncleaved Gag proteins are aligned in a radial manner inside the viral membrane, to the mature particle, which contains a condensed, conical core. Env glycoproteins. The heterotrimeric complexes of surface glycoprotein gp and transmembrane glycoprotein gp41 that are packaged into the viral membrane and mediate receptor—co-receptor binding and fusion in the next round of infection.

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