Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch - Wikidata - awgldk - TriplyDB

Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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HIV type 1 Gag as a target for antiviral therapy Lipids and membrane microdomains in HIV-1 replication Structure of the Myristylated Human Immunodeficiency Virus Type 2 Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Membrane Targeting Solution Structure of Calmodulin Bound to the Binding Domain of the HIV-1 Matrix Protein Membrane dynamics associated with viral infection Effect of Glu12-His89 Interaction on Dynamic Structures in HIV-1 p17 Matrix Protein Elucidated by NMR Endosomal trafficking of HIV-1 gag and genomic RNAs regulates viral egress.Analysis of the initiating events in HIV-1 particle assembly and genome packaging How HIV-1 Gag assembles in cells: Putting together pieces of the puzzle.SRp40 and SRp55 promote the translation of unspliced human immunodeficiency virus type 1 RNA The Role of Lipids in Retrovirus Replication.Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure.A large extension to HIV-1 Gag, like Pol, has negative impacts on virion assembly Matrix domain modulates HIV-1 Gag's nucleic acid chaperone activity via inositol phosphate binding.Myristate exposure in the human immunodeficiency virus type 1 matrix protein is modulated by pH.Identification of a small-molecule inhibitor of HIV-1 assembly that targets the phosphatidylinositol (4,5)-bisphosphate binding site of the HIV-1 matrix protein.Molecular mechanism of arenavirus assembly and budding.Assembly and replication of HIV-1 in T cells with low levels of phosphatidylinositol-(4,5)-bisphosphate.Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding.Matrix mediates the functional link between human immunodeficiency virus type 1 RNA nuclear export elements and the assembly competency of Gag in murine cells.Solution NMR characterizations of oligomerization and dynamics of equine infectious anemia virus matrix protein and its interaction with PIP2.Membrane binding and subcellular localization of retroviral Gag proteins are differentially regulated by MA interactions with phosphatidylinositol-(4,5)-bisphosphate and RNA.Gag localization and virus-like particle release mediated by the matrix domain of human T-lymphotropic virus type 1 Gag are less dependent on phosphatidylinositol-(4,5)-bisphosphate than those mediated by the matrix domain of HIV-1 Gag Molecular determinants that regulate plasma membrane association of HIV-1 Gag HIV-1 matrix protein binding to RNA.Structural and molecular determinants of HIV-1 Gag binding to the plasma membrane.NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix protein HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors.Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.A highly conserved residue in the C-terminal helix of HIV-1 matrix is required for envelope incorporation into virus particles Electrostatic interactions drive membrane association of the human immunodeficiency virus type 1 Gag MA domain Live-cell observation of cytosolic HIV-1 assembly onset reveals RNA-interacting Gag oligomers.Incorporation of high levels of chimeric human immunodeficiency virus envelope glycoproteins into virus-like particles.Dynamic Association between HIV-1 Gag and Membrane Domains.Mutations that mimic phosphorylation of the HIV-1 matrix protein do not perturb the myristyl switch Interaction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding.Analysis of small molecule ligands targeting the HIV-1 matrix protein-RNA binding site.Equine Infectious Anemia Virus Gag Assembly and Export Are Directed by Matrix Protein through trans-Golgi Networks and Cellular Vesicles.Discovery of a small-molecule antiviral targeting the HIV-1 matrix protein.Interleukin 2-inducible T cell kinase (ITK) facilitates efficient egress of HIV-1 by coordinating Gag distribution and actin organization.

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Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

http://www.wikidata.org/entity/Q27640933

description

2007 nî lūn-bûn

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2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年学术文章

@wuu

2007年学术文章

@zh-cn

2007年学术文章

@zh-hans

2007年学术文章

@zh-my

2007年学术文章

@zh-sg

2007年學術文章

@yue

name

Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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type

label

Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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Point mutations in the HIV-1 matrix protein turn off the myristyl switch

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prefLabel

Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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Point Mutations in the HIV-1 Matrix Protein Turn Off the Myristyl Switch

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J.JMB.2006.11.068

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Journal of Molecular Biology

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Point mutations in the HIV-1 matrix protein turn off the myristyl switch

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Andrew Kim

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Anjali Joshi

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Eric O Freed

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Erin Loeliger

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Jaime Miller

http://www.w3.org/2001/XMLSchema#string

Janet Tai

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Mellisa Liriano

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Michael F Summers

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Paz Luncsford

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P2860

The protein network of HIV budding

Myristoylation-dependent replication and assembly of human immunodeficiency virus 1

Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane

Role of capsid precursor processing and myristoylation in morphogenesis and infectivity of human immunodeficiency virus type 1

Identification of a membrane-binding domain within the amino-terminal region of human immunodeficiency virus type 1 Gag protein which interacts with acidic phospholipids

Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection

Differential membrane binding of the human immunodeficiency virus type 1 matrix protein

Plasma membrane is the site of productive HIV-1 particle assembly

Single amino acid changes in the human immunodeficiency virus type 1 matrix protein block virus particle production

Entropic switch regulates myristate exposure in the HIV-1 matrix protein

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574-585

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10.1016/J.JMB.2006.11.068

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2

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