The SARS-CoV Fusion Peptide Forms an Extended Bipartite Fusion Platform that Perturbs Membrane Order in a Calcium-Dependent Manner

Journal of Molecular Biology

Volumn 429, Issue 24, 2017, Pages 3875-3892

  Lai, Alex L ^a   Millet, Jean K ^a   Daniel, Susan ^b   Freed, Jack H ^a   Whittaker, Gary R ^a  

^a Department of Obstetrics Gynecology   (United States)

^b Cornell University   (United States)

Author keywords

coronavirus; electron spin resonance; membrane fusion; spike glycoprotein; viral entry

Indexed keywords

CALCIUM ION; VIRUS FUSION PROTEIN; VIRUS SPIKE PROTEIN; CALCIUM; CORONAVIRUS SPIKE GLYCOPROTEIN; PEPTIDE FRAGMENT; S PROTEIN, SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CALCIUM CELL LEVEL; CONTROLLED STUDY; ELECTRON SPIN RESONANCE; ENTHALPY; EXTRACELLULAR CALCIUM; ISOTHERMAL TITRATION CALORIMETRY; LIPID BILAYER; MEMBRANE BINDING; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SARS CORONAVIRUS; SEQUENCE ALIGNMENT; VIRUS ENTRY; CHEMISTRY; HEK293 CELL LINE; HUMAN; METABOLISM; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; BASE SEQUENCE; CALCIUM; HEK293 CELLS; HUMANS; MEMBRANE FUSION; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SARS VIRUS; SEQUENCE HOMOLOGY; SPIKE GLYCOPROTEIN, CORONAVIRUS; VIRUS INTERNALIZATION;

EID: 85032797005     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2017.10.017     Document Type: Article

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