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Sigalit Boura-Halfon

Researcher at Weizmann Institute of Science

Publications -  33
Citations -  1994

Sigalit Boura-Halfon is an academic researcher from Weizmann Institute of Science. The author has contributed to research in topics: Insulin receptor & Insulin. The author has an hindex of 18, co-authored 31 publications receiving 1603 citations. Previous affiliations of Sigalit Boura-Halfon include Hebrew University of Jerusalem.

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Phosphorylation of IRS proteins, insulin action, and insulin resistance

TL;DR: A range of conditions that activate IRS kinases to phosphorylate IRS proteins on "hot spot" domains are reviewed and their implications on insulin signaling, insulin resistance and type 2 diabetes, an emerging epidemic of the 21st century are outlined.
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Brown-adipose-tissue macrophages control tissue innervation and homeostatic energy expenditure

TL;DR: A previously unappreciated homeostatic role for macrophages in the control of tissue innervation is reported, which might contribute to the phenotype by repulsion of sympathetic axons expressing the transmembrane semaphorin Sema6A.
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Re-evaluating microglia expression profiles using RiboTag and cell isolation strategies.

TL;DR: A side-by-side comparison of classical cell-sorting-based transcriptome sequencing and the ‘RiboTag’ method, which avoids cell retrieval from tissue context and yields translatome sequencing information is reported, indicating method-based biases, reveals observer effects and establishes RiboTag-based transl atome profiling as a valuable complement to standard sorting-based profiling strategies.
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Ablation of very long acyl chain sphingolipids causes hepatic insulin resistance in mice due to altered detergent-resistant membranes

TL;DR: It is concluded that the sphingolipid acyl chain composition of liver regulates insulin signaling by modifying insulin receptor translocation into membrane microdomains.
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Serine Phosphorylation Proximal to Its Phosphotyrosine Binding Domain Inhibits Insulin Receptor Substrate 1 Function and Promotes Insulin Resistance

TL;DR: The mutated seven Ser sites located proximal to the phosphotyrosine binding domain of insulin receptor substrate 1 (IRS-1) are mutated into Ala and suggest that S408 and additional Ser sites among the seven mutated Ser sites are targets for IRS-1 kinases that play a key negative regulatory role in IRS- 1 function and insulin action.