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One or more keywords matched the following properties of Markosyan, Ruben
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 Membrane Fusion
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 Negative potentials across biological membranes promote fusion by class II and class III viral proteins.
Academic Article Tension of membranes expressing the hemagglutinin of influenza virus inhibits fusion.
Academic Article The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores.
Academic Article Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion.
Academic Article Evolution of intermediates of influenza virus hemagglutinin-mediated fusion revealed by kinetic measurements of pore formation.
Academic Article HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion 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.
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  • Membrane Fusion