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One or more keywords matched the following properties of Markosyan, Ruben
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overview My Scopus ID is 6604074194. My NIH COMMONS name is RMARKOSYAN. Research Areas: Viral entry into cells: receptor-mediated fusion of virus to membranes, retroviral fusion in ebola, HIV, SFV and VSV, formation and evolution of fusion pores, mechanisms of insertion of viral proteins into membranes, mechanism for pH- dependence of membrane fusion protein activity, role of transmembrane potential across endosomal membrane for viral fusion, effect of redox potential in the regulation of fusion. My Faculty Profile at Rush University Medical Center: https://www.rushu.rush.edu/faculty/ruben-markosyan-phd My Laboratory: https://www.rushu.rush.edu/research/departmental-research/physiology-and-biophysics-research/laboratory-fredric-cohen-phd My NCBI Bibliography: https://www.ncbi.nlm.nih.gov/pubmed/?term=Markosyan+RM My Scopus: https://www.scopus.com/authid/detail.uri?authorId=6604074194 Education: PhD, Institute of Physiology, National Academy of Sciences of Armenia Master's degree, physics, Yerevan State University, Armenia Master's degree, medical cybernetics, Yerevan Polytechnic Institute, Armenia
One or more keywords matched the following items that are connected to Markosyan, Ruben
Item TypeName
Concept Vesicular stomatitis Indiana virus
Concept RNA Viruses
Concept Moloney murine leukemia virus
Concept Avian Sarcoma Viruses
Concept Lassa virus
Concept Semliki forest virus
Concept Virus Replication
Concept Virus Internalization
Concept Hemagglutinin Glycoproteins, Influenza Virus
Concept RNA Virus Infections
Concept Avian Leukosis Virus
Concept DNA Virus Infections
Concept Influenza A virus
Concept Receptors, Virus
Concept DNA Viruses
Academic Article Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement.
Academic Article Low pH is required for avian sarcoma and leukosis virus Env-induced hemifusion and fusion pore formation but not for pore growth.
Academic Article A study of low pH-induced refolding of Env of avian sarcoma and leukosis virus into a six-helix bundle.
Academic Article Ternary complex formation of human immunodeficiency virus type 1 Env, CD4, and chemokine receptor captured as an intermediate of membrane fusion.
Academic Article Fusion induced by a class II viral fusion protein, semliki forest virus E1, is dependent on the voltage of the target cell.
Academic Article The six-helix bundle of human immunodeficiency virus Env controls pore formation and enlargement and is initiated at residues proximal to the hairpin turn.
Academic Article IFITM proteins restrict viral membrane hemifusion.
Academic Article The transmembrane domain and acidic lipid flip-flop regulates voltage-dependent fusion mediated by class II and III viral proteins.
Academic Article Induction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a Trigger.
Academic Article Tension of membranes expressing the hemagglutinin of influenza virus inhibits fusion.
Academic Article Role of the cytoplasmic tail of ecotropic moloney murine leukemia virus Env protein in fusion pore formation.
Academic Article The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores.
Academic Article A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion.
Academic Article Evolution of intermediates of influenza virus hemagglutinin-mediated fusion revealed by kinetic measurements of pore formation.
Academic Article Human immunodeficiency virus type 1 Env with an intersubunit disulfide bond engages coreceptors but requires bond reduction after engagement to induce fusion.
Academic Article Interferon-induced transmembrane protein 3 blocks fusion of sensitive but not resistant viruses by partitioning into virus-carrying endosomes.
Academic Article Ginkgolic acid inhibits fusion of enveloped viruses.
Academic Article Author Correction: Ginkgolic acid inhibits fusion of enveloped viruses.
Academic Article The late endosome-resident lipid bis(monoacylglycero)phosphate is a cofactor for Lassa virus fusion.
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