Avner Schlessinger
Icahn School of Medicine at Mount Sinai
5 Papers
Avner Schlessinger is an academic researcher from Icahn School of Medicine at Mount Sinai. The author has contributed to research in topics: Binding site & Structure–activity relationship. The author has an hindex of 5, co-authored 5 publications.
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Papers
Mutations in the Na(+)/citrate cotransporter NaCT (SLC13A5) in pediatric patients with epilepsy and developmental delay.
TL;DR: Additional SLC13A5 mutations are identified in patients with chronic epilepsy starting in the neonatal period, with the mutations producing inactive Na+/citrate transporters.
LAT1 activity of carboxylic acid bioisosteres: Evaluation of hydroxamic acids as substrates
Arik A. Zur,Huan-Chieh Chien,Evan Augustyn,Andrew Flint,Nathan Heeren,Karissa Finke,Christopher Hernandez,Logan Hansen,Sydney Miller,Lawrence Lin,Kathleen M. Giacomini,Claire Colas,Avner Schlessinger,Allen A. Thomas +13 more
TL;DR: The results lend support to a recent account that amino acid esters are LAT1 substrates, and that hydrogen bonding may be as important as charge for interaction with the transporter binding site.
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LAT-1 activity of meta -substituted phenylalanine and tyrosine analogs
Evan Augustyn,Karissa Finke,Arik A. Zur,Logan Hansen,Nathan Heeren,Huan-Chieh Chien,Lawrence Lin,Kathleen M. Giacomini,Claire Colas,Avner Schlessinger,Allen A. Thomas +10 more
TL;DR: It is found that lipophilicity was correlated with diminished substrate activity and increased inhibition of the transporter, and the synthesis and SAR of meta-substituted phenylalanine and tyrosine analogs is described.
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Structure activity relationships of benzylproline-derived inhibitors of the glutamine transporter ASCT2.
Kurnvir Singh,Rose Tanui,Armanda Gameiro,Gilad Eisenberg,Claire Colas,Avner Schlessinger,Christof Grewer +6 more
TL;DR: A systematic structure activity analysis of a series of substituted benzylproline derivatives resulted in compounds with characteristics of ASCT2 inhibitors, which are consistent with computational analysis based on docking of the inhibitors against an AsCT2 homology model.
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Mapping Functionally Important Residues in the Na+/Dicarboxylate Cotransporter, NaDC1.
TL;DR: The results of this study improve the understanding of substrate and ion recognition in the mammalian members of the SLC13 family and provide a framework for developing conformationally specific inhibitors against these transporters.