Singh, Satinder Kaur - Yale University - Biological & Biomedical Sciences

个人简介

Satinder was born in Boston, MA and moved, as a teenager, to Minneapolis, MN, with her family. She received her doctoral degree in Biochemistry & Molecular Biophysics from the University of Minnesota – Twin Cities, supported by an HHMI Predoctoral Fellowship. She has had a long-standing interest in the molecular mechanisms of neuropsychiatric disease, particularly in the role that the biogenic amines play. As a postdoctoral fellow, she combined her knowledge of neuropsychopharmacology and enzymology with X-ray crystallography to develop molecular models of transport and inhibition for LeuT, a bacterial orthologue of neurotransmitter sodium symporters (NSS). At Yale, Satinder has been concentrating on eukaryotic NSS members, specifically those that transport the biogenic amines serotonin (SERT) and dopamine (DAT). PhD University of Minnesota (2002) BS University of Minnesota (1995) Postdoctoral Fellow Oregon Health and Science University Postdoctoral Fellow Columbia University

研究领域

Antidepressive Agents; Depression; Epilepsy; gamma-Aminobutyric Acid; Glycine; Lipid Bilayers; Neurobiology; Neuropharmacology; Obsessive-Compulsive Disorder; Schizophrenia; Antipsychotic Agents; X-Ray Diffraction; Biogenic Monoamines; Protein Structure, Tertiary; Neurotransmitter Transport Proteins; Neuropsychiatry

近期论文

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Conformational dynamics of a neurotransmitter:sodium symporter in a lipid bilayer Adhikary, A., Deredge, D.L., Nagarajan, A., Forrest, L.R., Wintrode, P.L., and *Singh, S.K. (2017) Conformational dynamics of a neurotransmitter:sodium symporter in a lipid bilayer. Proc. Natl. Acad. Sci. USA, 114: E1786-E1795 Mechanism of paroxetine (Paxil) inhibition of the serotonin transporter. Davis, B.A., Nagaranjan, A., Forrest, L.R., and *Singh, S.K. (2016) Mechanism of paroxetine (Paxil) inhibition of the serotonin transporter. Scientific Reports, 6: 23789. Cryo-EM: Spinning the micelles away. *Singh, S.K. and *Sigworth, F.J. (2015) Cryo-EM: Spinning the micelles away. Structure, 23: 1561. Biophysical approaches to the study of LeuT, a prokaryotic homolog of neurotransmitter sodium symporters. *Singh, S.K. and Pal, A. (2015) Biophysical approaches to the study of LeuT, a prokaryotic homolog of neurotransmitter sodium symporters. Methods Enzymol., 557:167-198. Functionally important carboxyls in a bacterial homologue of the vesicular monoamine transporter (VMAT). Yaffe, D., Vergara-Jaque, A., Shuster, Y., Listov, D., Meena, S.R., Singh, S.K., Forrest, L.R., and *Schuldiner, S. (2014) Functionally important carboxyls in a bacterial homologue of the vesicular monoamine transporter (VMAT). J. Biol. Chem. 289: 34229-34240 Structure and regulatory interactions of the cytoplasmic terminal domains of serotonin transporter. Fenollar-Ferrer C., Stockner T., Schwarz T.C., Pal, A., Gotovina, J., Hofmaier, T., Jayaraman, K., Adhikary, S., Kudlacek, O., Mehdipour, A.R., Tavoulari, S., Rudnick, G., Singh, S.K., Konrat, R., *Sitte, H.H., and *Forrest, L.R. (2014) Structure and regulatory interactions of the cytoplasmic terminal domains of serotonin transporter. Biochemistry, 53: 5444-5460. Radioligand binding to nanodisc-reconstituted membrane transporters assessed by the scintillation proximity assay. Nasr, M.L. and *Singh, S.K. (2014) Radioligand binding to nanodisc-reconstituted membrane transporters assessed by the scintillation proximity assay. Biochemistry, 53: 4-6. Crystal structure and association behaviour of the GluR2 amino terminal domain. #Jin, R., #Singh, S.K., Gu, S., Furukawa, H., Sobolevsky, A.I., Zhou, J., Jin, Y., and *Gouaux, E. (2009) Crystal structure and association behaviour of the GluR2 amino terminal domain. EMBO J., 28:1812-1823. #EQUAL CONTRIBUTION LeuT: A prokaryotic stepping stone on the way to a eukaryotic neurotransmitter transporter structure. *Singh, S.K. (2008) LeuT: A prokaryotic stepping stone on the way to a eukaryotic neurotransmitter transporter structure. Channels, 2:380-389. A competitive inhibitor traps LeuT in an open-to-out conformation. Singh, S.K., Piscitelli, C.L., Yamashita, A., and *Gouaux, E. (2008) A competitive inhibitor traps LeuT in an open-to-out conformation. Science, 322:1655-61. Antidepressant binding site in a bacterial homologue of neurotransmitter transporters. Singh, S.K., Yamashita, A., and *Gouaux, E. (2007) Antidepressant binding site in a bacterial homologue of neurotransmitter transporters. Nature, 448:952-956. Subunit arrangement and function in NMDA receptors. Furukawa, H., Singh, S.K., Mancusso, R., and *Gouaux, E. (2005) Subunit arrangement and function in NMDA receptors. Nature, 438:185-192. Crystal structure of a bacterial homologue of Na+/Cl- -dependent neurotransmitter transporters.