Fibulin 5 forms a compact dimer in physiological solutions

Journal of Biological Chemistry

Volumn 284, Issue 38, 2009, Pages 25938-25943

  Jones, Richard P O ^a   Wang, Ming Chuan ^b   Jowitt, Thomas A ^b   Ridley, Caroline ^b   Mellody, Kieran T ^b   Howard, Marjorie ^b   Wang, Tao ^a   Bishop, Paul N ^a,b   Lotery, Andrew J ^c   Kielty, Cay M ^b   Baldock, Clair ^b   Trump, Dorothy ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

^c UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AGE-RELATED MACULAR DEGENERATION; BINDING PARTNERS; CALCIUM BINDING; CIRCULAR DICHROISM; COMPACT STRUCTURES; ELASTIC TISSUES; EPIDERMAL GROWTH FACTORS; EQUILIBRIUM SEDIMENTATION; EXTRACELLULAR MATRIX PROTEIN; INTERMOLECULAR INTERACTIONS; PHYSIOLOGICAL CONDITION; PHYSIOLOGICAL SOLUTION; SMALL ANGLE X-RAY SCATTERING; TROPOELASTIN;

CALCIUM; DICHROISM; DIMERIZATION; FLUID DYNAMICS; LIGHT SCATTERING; MONOMERS; OLIGOMERIZATION; REFRACTION; SEDIMENTATION; SODIUM CHLORIDE; TISSUE; X RAY SCATTERING;

SCATTERING;

FIBULIN 5; TROPOELASTIN; CALCIUM; FBLN5 PROTEIN, HUMAN; SCLEROPROTEIN; SODIUM CHLORIDE;

ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; DIMERIZATION; GLYCOSYLATION; HUMAN; HUMAN CELL; LIGHT SCATTERING; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SEDIMENTATION; ULTRACENTRIFUGATION; CHEMISTRY; CUTIS LAXA; ELASTIC TISSUE; GENETICS; METABOLISM; MISSENSE MUTATION; PHYSIOLOGY; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; RADIATION SCATTERING; RETINA MACULA DEGENERATION; X RAY;

CALCIUM; CIRCULAR DICHROISM; CUTIS LAXA; ELASTIC TISSUE; EXTRACELLULAR MATRIX PROTEINS; HUMANS; MACULAR DEGENERATION; MUTATION, MISSENSE; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; SCATTERING, RADIATION; SODIUM CHLORIDE; TROPOELASTIN; X-RAYS;

EID: 70350004029     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.011627     Document Type: Article

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