The stoichiometry of Gag protein in HIV-1. - Wikidata - awgldk - TriplyDB

The stoichiometry of Gag protein in HIV-1.

The stoichiometry of Gag protein in HIV-1.

http://www.wikidata.org/entity/Q34328141

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Cryo-electron tomographic structure of an immunodeficiency virus envelope complex in situ Potent activity of the HIV-1 maturation inhibitor bevirimat in SCID-hu Thy/Liv mice Protein methylation is required to maintain optimal HIV-1 infectivity The human endosomal sorting complex required for transport (ESCRT-I) and its role in HIV-1 budding The host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminus HIV type 1 Gag as a target for antiviral therapy Dynamics of ESCRT protein recruitment during retroviral assembly Nucleic acid binding and chaperone properties of HIV-1 Gag and nucleocapsid proteins HIV-1 capsid: the multifaceted key player in HIV-1 infection Wrapping up the bad news: HIV assembly and release The choreography of HIV-1 proteolytic processing and virion assembly HIV-1 protease and reverse transcriptase control the architecture of their nucleocapsid partner KIF5B and Nup358 Cooperatively Mediate the Nuclear Import of HIV-1 during Infection Distribution and Redistribution of HIV-1 Nucleocapsid Protein in Immature, Mature, and Integrase-Inhibited Virions: a Role for Integrase in Maturation Electron tomography of HIV-1 infection in gut-associated lymphoid tissue Protease cleavage leads to formation of mature trimer interface in HIV-1 capsid Mobilization of HIV spread by diaphanous 2 dependent filopodia in infected dendritic cells Domain-swapped dimerization of the HIV-1 capsid C-terminal domain Allosteric Inhibition of Human Immunodeficiency Virus Integrase Structure of the Antiviral Assembly Inhibitor CAP-1 Complex with the HIV-1 CA Protein Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein Structural Convergence between Cryo-EM and NMR Reveals Intersubunit Interactions Critical for HIV-1 Capsid Function Structure of the HIV-1 Full-Length Capsid Protein in a Conformationally Trapped Unassembled State Induced by Small-Molecule Binding Structure of the immature retroviral capsid at 8 Å resolution by cryo-electron microscopy Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly Ty3 capsid mutations reveal early and late functions of the amino-terminal domain Investigation by atomic force microscopy of the structure of Ty3 retrotransposon particles.3D visualization of HIV virions by cryoelectron tomography Newly synthesized APOBEC3G is incorporated into HIV virions, inhibited by HIV RNA, and subsequently activated by RNase H Gag mutations strongly contribute to HIV-1 resistance to protease inhibitors in highly drug-experienced patients besides compensating for fitness loss Implications of CTL-mediated killing of HIV-infected cells during the non-productive stage of infection Characterization of a novel type of HIV-1 particle assembly inhibitor using a quantitative luciferase-Vpr packaging-based assay Efficient production of HIV-1 virus-like particles from a mammalian expression vector requires the N-terminal capsid domain The effect of chemical chaperones on the assembly and stability of HIV-1 capsid protein Large-scale functional purification of recombinant HIV-1 capsid Fates of retroviral core components during unrestricted and TRIM5-restricted infection Gag-Pol processing during HIV-1 virion maturation: a systems biology approach Mechanism of HIV-1 virion entrapment by tetherin Retroviral DNA Integration Role of the SP2 domain and its proteolytic cleavage in HIV-1 structural maturation and infectivity

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The stoichiometry of Gag protein in HIV-1.

http://www.wikidata.org/entity/Q34328141

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2004 nî lūn-bûn

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2004 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2004年の論文

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2004年論文

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2004年论文

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The stoichiometry of Gag protein in HIV-1.

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The stoichiometry of Gag protein in HIV-1.

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The stoichiometry of Gag protein in HIV-1.

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The stoichiometry of Gag protein in HIV-1.

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The stoichiometry of Gag protein in HIV-1.

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The stoichiometry of Gag protein in HIV-1.

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The stoichiometry of Gag protein in HIV-1.

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The stoichiometry of Gag protein in HIV-1.

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Nature Structural & Molecular Biology

P1476

The stoichiometry of Gag protein in HIV-1.

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P2093

Ingolf Gross

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John A G Briggs

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Marc C Johnson

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Martha N Simon

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Stephen D Fuller

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Volker M Vogt

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High levels of HIV-1 in plasma during all stages of infection determined by competitive PCR

Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein

HIV-1: fifteen proteins and an RNA

Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions.

Retrovirus capsid protein assembly arrangements.

Towards the structure of the human immunodeficiency virus: divide and conquer.

Efficient particle production by minimal Gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain.

Human immunodeficiency virus type 1 Vpr protein is incorporated into the virion in significantly smaller amounts than gag and is phosphorylated in infected cells

Organization of immature human immunodeficiency virus type 1

Characterization of Rous sarcoma virus Gag particles assembled in vitro.

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672-675

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10.1038/NSMB785

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7

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11

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Hans-Georg Kräusslich

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2004-06-20T00:00:00Z

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15208690

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