Terminal modifications of norovirus P domain resulted in a new type of subviral particles, the small P particles

Virology

Volumn 410, Issue 2, 2011, Pages 345-352

  Tan, Ming ^a,b   Fang, Ping An ^c   Xia, Ming ^a   Chachiyo, Teepanis ^c   Jiang, Wen ^c   Jiang, Xi ^a,b  

^a CINCINNATI CHILDREN'S HOSPITAL MEDICAL CENTER   (United States)

^b UNIVERSITY OF CINCINNATI COLLEGE OF MEDICINE   (United States)

^c PURDUE UNIVERSITY   (United States)

Author keywords

Calicivirus; Carbohydrate receptor; HBGAs; Host virus interaction; Norovirus

Indexed keywords

ARGININE; BLOOD GROUP ANTIGEN; CYSTEINE; GLYCINE DEHYDROGENASE (DECARBOXYLATING); HISTO BLOOD GROUP ANTIGEN; PROTEIN VP1; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYOELECTRON MICROSCOPY; CRYSTAL STRUCTURE; DIMERIZATION; GEL FILTRATION; GENE CLUSTER; GENE MAPPING; HUMAN; MORPHOGENESIS; NONHUMAN; NOROVIRUS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROCESSING; STRUCTURE ANALYSIS; VIRUS PARTICLE;

CHROMATOGRAPHY, GEL; CRYOELECTRON MICROSCOPY; HOST-PATHOGEN INTERACTIONS; HUMANS; MACROMOLECULAR SUBSTANCES; MODELS, MOLECULAR; MUTANT PROTEINS; NOROVIRUS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; VIRAL STRUCTURAL PROTEINS; VIRAL VACCINES; VIROSOMES; VIRUS ATTACHMENT;

CALICIVIRIDAE; NOROVIRUS;

EID: 78751706360     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2010.11.017     Document Type: Article

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