Tryptophan-dependent membrane interaction and heteromerization with the internal fusion peptide by the membrane proximal external region of SARS-CoV spike protein

Biochemistry

Volumn 54, Issue 9, 2015, Pages 1819-1830

  Liao, Ying ^a,b   Zhang, Si Min ^a,c   Neo, Tuan Ling ^a   Tam, James P ^a  

^a NANYANG TECHNOLOGICAL UNIVERSITY   (Singapore)

^b INSTITUTE OF PLANT PROTECTION   (China)

^c KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; CROSSLINKING; DIMERS; DISEASES; HYDROPHOBICITY; MOBILE SECURITY; OLIGOMERIZATION; OLIGOMERS; PEPTIDES; PROTEINS;

CHEMICAL CROSS-LINKING; HETERO-OLIGOMERIZATION; HYDROPHOBIC SEQUENCES; IMMUNOFLUORESCENCE STAINING; MEMBRANE INTERACTIONS; SECONDARY STRUCTURES; SEVERE ACUTE RESPIRATORY SYNDROME; STRUCTURAL REARRANGEMENT;

MEMBRANES;

ALANINE; DIMER; HYBRID PROTEIN; INTERNAL FUSION PEPTIDE; OLIGOMER; PEPTIDE; PHENYLALANINE; SYNTHETIC PEPTIDE; TRYPTOPHAN; UNCLASSIFIED DRUG; VIRUS SPIKE PROTEIN; CORONAVIRUS SPIKE GLYCOPROTEIN; PEPTIDE FRAGMENT; PROTEIN BINDING; VIRUS FUSION PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AQUEOUS SOLUTION; ARTICLE; CONTROLLED STUDY; CROSS LINKING; HYDROPHOBICITY; IMMUNOFLUORESCENCE; MEMBRANE FUSION; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; SARS CORONAVIRUS; VIRUS ENTRY; VIRUS ENVELOPE; WILD TYPE; ANIMAL; CELL MEMBRANE; CHEMISTRY; CHLOROCEBUS AETHIOPS; GENETICS; METABOLISM; PHYSIOLOGY; PROTEIN DOMAIN; PROTEIN MULTIMERIZATION; VERO CELL LINE; VIROLOGY;

SARS CORONAVIRUS;

ALANINE; AMINO ACID SUBSTITUTION; ANIMALS; CELL MEMBRANE; CERCOPITHECUS AETHIOPS; PEPTIDE FRAGMENTS; PHENYLALANINE; PROTEIN BINDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; SARS VIRUS; SPIKE GLYCOPROTEIN, CORONAVIRUS; TRYPTOPHAN; VERO CELLS; VIRAL FUSION PROTEINS;

EID: 84924388647     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501352u     Document Type: Article

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