Ankyrin recognizes both surface character and shape of the 14-15 di-repeat of β-spectrin

Biochemical and Biophysical Research Communications

Volumn 392, Issue 4, 2010, Pages 490-494

  La Borde, Penelope J ^a   Stabach, Paul R ^b   Simonović, Ivana ^a   Morrow, Jon S ^b   Simonović, Miljan ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

^b YALE UNIVERSITY   (United States)

Author keywords

Ankyrin; Erythrocyte membrane; Isothermal titration calorimetry; Spectrin

Indexed keywords

ANKYRIN; SPECTRIN; SPECTRIN BETA SUBUNIT; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ERYTHROCYTE MEMBRANE; GENE MUTATION; GENETIC POLYMORPHISM; HEMOLYTIC ANEMIA; ISOTHERMAL TITRATION CALORIMETRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

ANKYRINS; MUTATION; PROTEIN CONFORMATION; REPETITIVE SEQUENCES, NUCLEIC ACID; SPECTRIN;

EID: 76749133529     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.01.046     Document Type: Article

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