K
Kay S. Arnold
Researcher at University of California, San Francisco
Publications - 22
Citations - 2336
Kay S. Arnold is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Apolipoprotein B & LDL receptor. The author has an hindex of 19, co-authored 22 publications receiving 2281 citations. Previous affiliations of Kay S. Arnold include University of California, Berkeley.
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Journal ArticleDOI
Familial defective apolipoprotein B-100: low density lipoproteins with abnormal receptor binding
Thomas L. Innerarity,Karl H. Weisgraber,Kay S. Arnold,Robert W. Mahley,Ronald M. Krauss,Gloria Lena Vega,Scott M. Grundy +6 more
TL;DR: These studies indicate that the defective receptor binding results in inefficient clearance of LDL and the hypercholesterolemia observed in patients, which has been designated familial defective apolipoprotein B-100.
Journal ArticleDOI
Apolipoprotein B mRNA-editing protein induces hepatocellular carcinoma and dysplasia in transgenic animals.
Shinya Yamanaka,Maureen E. Balestra,Linda D. Ferrell,Jianglin Fan,Kay S. Arnold,Stacy Taylor,John M. Taylor,Thomas L. Innerarity +7 more
TL;DR: The findings compromise the potential use of APOBEC-1 for gene therapy to lower plasma levels of low density lipoproteins and suggests that aberrant editing of hepatic mRNAs involved in cell growth and regulation is the cause of the tumorigenesis.
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A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme.
TL;DR: A novel mRNA (NAT1 for novel APOBEC-1 target no. 1) that is extensively edited at multiple sites in mouse and rabbit livers is identified and its aberrant editing could contribute to the potent oncogenesis induced by overexpression of APOBec-1.
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Rate and equilibrium constants for binding of apo-E HDLc (a cholesterol-induced lipoprotein) and low density lipoproteins to human fibroblasts: Evidence for multiple receptor binding of apo-E HDLc
TL;DR: Kinetic studies indicated that each HDL(c) particle binds to multiple cell surface receptors at a ratio of 4:1 for LDL receptor binding, and association and dissociation rate constants for the lipoprotein-receptor complex were determined from the time course of binding at various lipop protein concentrations.
Journal ArticleDOI
Normalization of receptor binding of apolipoprotein E2. Evidence for modulation of the binding site conformation.
TL;DR: Results indicate that apo-E2 can attain full binding activity by the removal of the carboxyl-terminal one-third of the molecule and the addition of a positive charge at residue 158 of the molecules.