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Volumn 287, Issue 41, 2012, Pages 34304-34315

A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR)

Author keywords

[No Author keywords available]

Indexed keywords

ALLOSTERIC MECHANISMS; ALLOSTERIC REGULATION; DYNAMIC PROPERTY; EXTRACELLULAR MATRICES; HIGH AFFINITY BINDING; HYDROGEN-DEUTERIUM EXCHANGE; IN-VIVO; INTERVENTION THERAPY; MULTIDOMAIN STRUCTURE; N-TERMINAL DOMAINS; PROTEOLYTIC DEGRADATION; RECEPTOR COMPLEX; SMALL ANGLE X-RAY SCATTERING; STRUCTURAL MODELS; TRANSLATIONAL RESEARCH; TUMOR IMAGING; UROKINASE-TYPE PLASMINOGEN ACTIVATOR RECEPTORS (UPAR); VITRONECTIN;

EID: 84867242361     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.398404     Document Type: Article
Times cited : (46)

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