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Volumn 276, Issue 2, 2001, Pages 1057-1062

VLDL receptor fragments of different lengths bind to human rhinovirus HRV2 with different stoichiometry. An analysis of virus-receptor complexes by capillary electrophoresis

(5) Okun, Vadim M a Moser, Rosita a Ronacher, Bernhard a,b Kenndler, Ernst a Blaas, Dieter a

a UNIVERSITY OF VIENNA (Austria)

b Labor für Molekularbiologische DNA Analysen Ges m b H (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

MALTOSE BINDING PROTEIN; VERY LOW DENSITY LIPOPROTEIN RECEPTOR;

ARTICLE; BINDING SITE; CAPILLARY ELECTROPHORESIS; COMPLEX FORMATION; CONCENTRATION (PARAMETERS); HUMAN; HUMAN RHINOVIRUS; NONHUMAN; PRIORITY JOURNAL; QUANTITATIVE ASSAY; RECEPTOR BINDING; STOICHIOMETRY;

BINDING SITES; CARRIER PROTEINS; ELECTROPHORESIS, CAPILLARY; HUMANS; KINETICS; LIPOPROTEINS, VLDL; RECEPTORS, LDL; RECOMBINANT FUSION PROTEINS; RHINOVIRUS;

BACTERIA (MICROORGANISMS); HUMAN RHINOVIRUS SP.; RNA VIRUSES;

EID: 0035846992 PISSN: 00219258 EISSN: None Source Type: Journal
DOI: 10.1074/jbc.M008039200 Document Type: Article

Times cited : (36)

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