Výsledky vyhledávání - "Brent R, Lyda"

Akademický článek

Discovery and Synthesis of Hydroxy-l-Proline Blockers of the Neutral Amino Acid Transporters SLC1A4 (ASCT1) and SLC1A5 (ASCT2)

Autor: Brent R. Lyda, Gregory P. Leary, Jill Farnsworth, Benjamin Seaver, Derek Silvius, Michael P. Kavanaugh, C. Sean Esslinger, Nicholas R. Natale

Publikováno v: Molecules, Vol 29, Iss 10, p 2330 (2024)

As a conformationally restricted amino acid, hydroxy-l-proline is a versatile scaffold for the synthesis of diverse multi-functionalized pyrrolidines for probing the ligand binding sites of biological targets. With the goal to develop new inhibitors

Externí odkaz: https://doaj.org/article/09739a5a115743fe8c51173f32001947

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Discovery and synthesis of hydroxy-L-proline based blockers of the neutral amino acid transporters SLC1A4 (ASCT1) and SLC1A5 (ASCT2)

Autor: Brent R. Lyda, Gregory P. Leary, Jill Farnsworth, Derek Silvius, Benjamin Seaver, C. Sean Esslinger, Nicholas R. Natale, Michael P. Kavanaugh

The conformationally restricted heterocycle hydroxy-L-proline is a versatile scaffold for the synthesis of diverse multi-functionalized pyrrolidines for probing the ligand binding sites of biological targets. With the goal to develop new inhibitors o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::16821e2ba966c8cf06206d75570da98d
https://doi.org/10.1101/2021.12.14.470456

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In Situ Reconstitution of the Adenosine A2A Receptor in Spontaneously Formed Synthetic Liposomes

Autor: Roberto J. Brea, Brent R. Lyda, Neal K. Devaraj, Libin Ye, R. Scott Prosser, Roger K. Sunahara, Christian M. Cole

Publikováno v: Journal of the American Chemical Society. 139:3607-3610

Cell transmembrane receptors play a key role in the detection of environmental stimuli and control of intracellular communication. G protein-coupled receptors constitute the largest transmembrane protein family involved in cell signaling. However, cu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ec2140164861a04a1f7a5ade1be96983
https://doi.org/10.1021/jacs.6b12830

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Mechanistic insights into allosteric regulation of the A2A adenosine G protein-coupled receptor by physiological cations

Autor: Adnan Sljoka, Régis Pomès, Chris Neale, Dmitry Pichugin, Scott Prosser, Libin Ye, Sacha Thierry Larda, Nobuyuki Tsuchimura, Oliver P. Ernst, Angel E. Garcia, Roger K. Sunahara, Brent R. Lyda

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Nature communications, vol 9, iss 1

Cations play key roles in regulating G-protein-coupled receptors (GPCRs), although their mechanisms are poorly understood. Here, 19F NMR is used to delineate the effects of cations on functional states of the adenosine A2A GPCR. While Na+ reinforces

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04985a17d490fa15d18c9d111f2c57ee
https://doi.org/10.1038/s41467-018-03314-9

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Structure-based discovery of selective positive allosteric modulators of antagonists for the M

Autor: Magdalena, Korczynska, Mary J, Clark, Celine, Valant, Jun, Xu, Ee Von, Moo, Sabine, Albold, Dahlia R, Weiss, Hayarpi, Torosyan, Weijiao, Huang, Andrew C, Kruse, Brent R, Lyda, Lauren T, May, Jo-Anne, Baltos, Patrick M, Sexton, Brian K, Kobilka, Arthur, Christopoulos, Brian K, Shoichet, Roger K, Sunahara

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America

Significance The orthosteric binding sites of the five muscarinic acetylcholine receptor (mAChR) subtypes are highly conserved, making the development of selective antagonists challenging. The allosteric sites of these receptors are more variable, al

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::f254ae8318eed68acc861d2d65acc92a
https://pubmed.ncbi.nlm.nih.gov/29453275

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Structure-based discovery of selective positive allosteric modulators of antagonists for the M 2 muscarinic acetylcholine receptor

Autor: Arthur Christopoulos, Jun Xu, Celine Valant, Weijiao Huang, Hayarpi Torosyan, Patrick M. Sexton, Brian K. Kobilka, Brian K. Shoichet, Andrew C. Kruse, Ee Von Moo, Sabine Albold, Brent R. Lyda, Dahlia R. Weiss, Lauren T. May, Mary J. Clark, Jo-Anne Baltos, Magdalena Korczynska, Roger K. Sunahara

Publikováno v: Proceedings of the National Academy of Sciences. 115

Subtype-selective antagonists for muscarinic acetylcholine receptors (mAChRs) have long been elusive, owing to the highly conserved orthosteric binding site. However, allosteric sites of these receptors are less conserved, motivating the search for a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4d66354dd46318cee06fa28f97597360
https://doi.org/10.1073/pnas.1718037115

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