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Vangipuram S. Rangan

Researcher at Children's Hospital Oakland Research Institute

Publications -  16
Citations -  666

Vangipuram S. Rangan is an academic researcher from Children's Hospital Oakland Research Institute. The author has contributed to research in topics: Fatty acid synthase & Protein subunit. The author has an hindex of 14, co-authored 16 publications receiving 646 citations.

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Journal ArticleDOI

Structural organization of the multifunctional animal fatty-acid synthase.

TL;DR: The data permit refinement of the model for the fatty-acid synthase dimer and suggest that the malonyl/acetyl transferase and oxoacyl synthase of one subunit cooperate with the reductases, acyl carrier protein and thioesterase of the companion subunit in the formation of a center for fatty- acid synthesis.
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Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity.

TL;DR: A single candidate 4′-phosphopantetheine transferase, identified by BLAST searches of the human genome sequence data base, has been cloned, expressed, and characterized and appears to utilize a single, broad specificity enzyme for all posttrans lysine catabolism reactions.
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The human thioesterase II protein binds to a site on HIV-1 Nef critical for CD4 down-regulation.

TL;DR: Results, taken together with previous studies, identify a region on Nef critical for most of its known functions, however, not all Nef alleles bind to hTE with high affinity, so the role of hTE during HIV infection remains uncertain.
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Identification of an Inverted CCAAT Box Motif in the Fatty-acid Synthase Gene as an Essential Element for Mediation of Transcriptional Regulation by cAMP

TL;DR: The results suggest that essential to the regulation of FAS transcription by cAMP is the interaction of an inverted CCAAT box motif with a constitutively produced trans-acting factor that either itself undergoes modification in response to cAMP or associates with a protein that is produced or modified bycAMP exposure.
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Mapping the functional topology of the animal fatty acid synthase by mutant complementation in vitro.

TL;DR: The results are consistent with a model for the fatty acid synthase in which the substrate loading and condensation reactions are catalyzed by cooperation of an acyl carrier protein domain of one subunit with the malonyl/acetyltransferase or beta-ketoacyl synthase domains, respectively, of either subunit.