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Alexandra L. Brown

Researcher at National Institutes of Health

Publications -  36
Citations -  4336

Alexandra L. Brown is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Gene & Insulin-like growth factor-binding protein. The author has an hindex of 23, co-authored 33 publications receiving 4068 citations.

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Resveratrol Ameliorates Aging-Related Metabolic Phenotypes by Inhibiting cAMP Phosphodiesterases

TL;DR: It is reported that the metabolic effects of resveratrol result from competitive inhibition of cAMP-degrading phosphodiesterases, leading to elevated cAMP levels, and administration of PDE4 inhibitors may also protect against and ameliorate the symptoms of metabolic diseases associated with aging.
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hCds1-mediated phosphorylation of BRCA1 regulates the DNA damage response

TL;DR: It is reported that the human Cds1 kinase (hCds1/Chk2) regulates BRCA1 function after DNA damage by phosphorylating serine 988 of BRC a1, and it is shown that hCDS1 and BRCa1 interact and co-localize within discrete nuclear foci but separate after gamma irradiation.
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Developmental regulation of insulin-like growth factor II mRNA in different rat tissues.

TL;DR: Tissue-specific differences in the developmental regulation of the expression of IGF-II RNA exhibit intriguing temporal correlations with major maturational events in some tissues such as lung and muscle.
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A human Cds1-related kinase that functions downstream of ATM protein in the cellular response to DNA damage

TL;DR: The identification of a human cDNA encoding a protein that shares sequence, structural, and functional similarity to SpCds1 is reported, suggesting that the checkpoint function of HuCDS1 is conserved in yeast and mammals.
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Nucleotide Sequence and Expression of a cDNA Clone Encoding a Fetal Rat Binding Protein for Insulin-like Growth Factors

TL;DR: The rat IGF binding protein that is cloned appears to be a distinct member of a family of related IGF binding proteins, and it is postulate that the structurally distinct IGFbinding proteins may have different biological functions.