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Alan R. Kimmel
Researcher at National Institutes of Health
Publications - 127
Citations - 10872
Alan R. Kimmel is an academic researcher from National Institutes of Health. The author has contributed to research in topics: Dictyostelium & Lipid droplet. The author has an hindex of 53, co-authored 127 publications receiving 10376 citations. Previous affiliations of Alan R. Kimmel include University of California, Berkeley & University of California, San Diego.
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Journal ArticleDOI
Perilipin ablation results in a lean mouse with aberrant adipocyte lipolysis, enhanced leptin production, and resistance to diet-induced obesity
John T. Tansey,Carole Sztalryd,Jasmine Gruia-Gray,D. L. Roush,J. V. Zee,Oksana Gavrilova,Marc L. Reitman,Chu-Xia Deng,Cuiling Li,Alan R. Kimmel,Constantine Londos +10 more
TL;DR: The data reveal a major role for perilipin in adipose lipid metabolism and suggest perilipIn as a potential target for attacking problems associated with obesity.
Journal ArticleDOI
Perilipin A is essential for the translocation of hormone-sensitive lipase during lipolytic activation
Carole Sztalryd,Guoheng Xu,Heidi Dorward,John T. Tansey,Juan A. Contreras,Alan R. Kimmel,Constantine Londos +6 more
TL;DR: It is shown that HSL is basally associated with lipid droplet surfaces at a low level in perilipin nulls, but that stimulated translocation from the cytosol to lipid droplets is absent in adipocytes derived from embryonic fibroblasts of perilip in-null mice.
Journal ArticleDOI
A chemoattractant receptor controls development in Dictyostelium discoideum.
Peter S. Klein,Tzeli J. Sun,Charles L. Saxe,Alan R. Kimmel,Ronald L. Johnson,Peter N. Devreotes +5 more
TL;DR: The phenotype of the antisense transformants suggests that the cyclic AMP receptor is essential for development, and the deduced amino acid sequence of the receptor reveals a high percentage of hydrophobic residues grouped in seven domains, similar to the rhodopsins and other receptors believed to interact with G proteins.
Journal ArticleDOI
Perilipins, ADRP, and other proteins that associate with intracellular neutral lipid droplets in animal cells.
TL;DR: The properties, distribution, localization, and potential functions of perilipins and ADRP, as well as those of vimentin and the recently-described 'capsular' proteins, in lipid storage and metabolism are discussed.
Journal ArticleDOI
Perilipin A Increases Triacylglycerol Storage by Decreasing the Rate of Triacylglycerol Hydrolysis
Dawn L. Brasaemle,Dawn L. Brasaemle,Boris Rubin,Boris Rubin,Ingrid A. Harten,Jasmine Gruia-Gray,Alan R. Kimmel,Constantine Londos +7 more
TL;DR: It is concluded that perilipin A increases the triacylglycerol content of cells by forming a barrier that reduces the access of soluble lipases to stored lipids, thus inhibiting triacyLglycersol hydrolysis.