About: Attachment of human immunodeficiency virus to cells and its inhibition

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Attachment of human immunodeficiency virus to cells and its inhibition
Creator	Pöhlmann, Stefan Tremblay, Michel Derdeyn, Cynthia Reeves, Jacqueline
source	PMC
abstract	The entry of enveloped viruses involves virus adsorption followed by close apposition of the viral and plasma membranes. This multistep process is initiated by specific binding interactions between glycoproteins in the viral envelope and appropriate receptors on the cell surface. In the case of HIV-1, attachment of virions to the cell surface is attributed to a high affinity interaction between envelope spike glycoproteins (Env, composed of the surface protein gp120 and the transmembrane protein gp41) and a complex made of the primary CD4 receptor and a seven-transmembrane co-receptor (e.g., CXCR4 or CCR5) (reviewed in [1]). Then a chain of dynamic events take place that enable the viral nucleocapsid to penetrate within the target cell following the destabilization of membrane microenvironment and the formation of a fusion pore.
has issue date	2007-01-01(xsd:dateTime)
bibo:doi	10.1007/978-3-7643-7783-0_3
has license	no-cc
sha1sum (hex)	370d71c728ead6af3f4a03fc131f4afca8520b74
schema:url	https://doi.org/10.1007/978-3-7643-7783-0_3
resource representing a document's title	Attachment of human immunodeficiency virus to cells and its inhibition
has PubMed Central identifier	PMC7123856
schema:publication	Entry Inhibitors in HIV Therapy
resource representing a document's body	covid:370d71c728ead6af3f4a03fc131f4afca8520b74#body_text
is schema:about of	named entity 'close' named entity 'co-receptor' named entity 'dynamic' named entity 'transmembrane protein' named entity 'adsorption' named entity 'membrane' named entity 'membranes' named entity 'viral' named entity 'spike' named entity 'interactions' named entity 'target cell' named entity 'process' named entity 'virions' named entity 'cell surface' named entity 'fusion pore' named entity 'CXCR4' named entity 'microenvironment' named entity 'gp41' named entity 'enveloped viruses' named entity 'gp120' named entity 'virus' named entity 'Ebola' named entity 'host cells' named entity 'antiviral activity' named entity 'Heparan sulfate proteoglycans' named entity 'HIV-1' named entity 'helper cells' named entity '7.5' named entity 'lectins' named entity 'DC-SIGN' named entity 'gp120' named entity 'cell type' named entity 'gene' named entity 'hybrid virus' named entity 'DC-SIGN' named entity 'Langerin' named entity 'virus' named entity 'mucosal' named entity 'cell types' named entity 'genotype' named entity 'microenvironment' named entity 'macrophages' named entity 'cell surface' named entity 'HIV-1' named entity 'HIV-1' named entity 'viral load' named entity 'simian immunodeficiency virus' named entity 'HIV-1' named entity 'HIV-1' named entity 'MHC' named entity 'DC-SIGN' named entity 'DC-SIGN' named entity 'endocytosed' named entity 'clinical study' named entity 'ICAM-1' named entity 'lectins' named entity 'HIV-1' named entity 'DCs' named entity 'virus' named entity 'HIV-1' named entity 'cell membrane' named entity 'lectins' named entity 'fusion inhibitor' named entity 'sinusoidal endothelial cells' named entity 'Env' named entity 'DC-SIGN' named entity 'sexual transmission' named entity 'HIV-1 infection' named entity 'amino acid' named entity 'lymphoid tissue' named entity 'binding sites' named entity 'DC-SIGN' named entity 'gp120' named entity 'siRNA' named entity 'liver' named entity 'virus envelope' named entity 'gp41' named entity 'HIV-1' named entity 'LFA-1' named entity 'adsorption'

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