Important Changes in Biochemical Properties and Function of Mutated LLP12 Domain of HIV-1 gp41
Author:
Publisher
Wiley
Subject
Molecular Medicine,Biochemistry,Drug Discovery,Pharmacology,Organic Chemistry
Reference25 articles.
1. Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity
2. Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins
3. Role of the Carboxy-Terminal Portion of the HIV-1 Transmembrane Protein in Viral Transmission and Cytopathogenicity
4. Mutational Analysis of Conserved Domains within the Cytoplasmic Tail of gp41 from Human Immunodeficiency Virus Type 1: Effects on Glycoprotein Incorporation and Infectivity
5. Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein increases env incorporation into particles and fusogenicity and infectivity
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4. Identifying possible sites for antibody neutralization escape: Implications for unique functional properties of the C-terminal tail of Human Immunodeficiency Virus Type 1 gp41;Immunology Letters;2016-07
5. Unique Functional Properties of Conserved Arginine Residues in the Lentivirus Lytic Peptide Domains of the C-terminal Tail of HIV-1 gp41;Journal of Biological Chemistry;2014-03
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