Výsledky vyhledávání - "David D. McKee"

X-ray Crystal Structure of the Liver X Receptor β Ligand Binding Domain

Autor: Millard H. Lambert, Randy K. Bledsoe, Boggs Sharon Davis, Jason Nichols, Shawn P. Williams, John T. Moore, Jon L. Collins, Timothy M. Willson, Ann B. Miller, David D. McKee, Michael A. Watson, Derek J. Parks, Linda B. Moore, Bruce Wisely

Publikováno v: Journal of Biological Chemistry. 278:27138-27143

The x-ray crystal structures of the human liver X receptor β ligand binding domain complexed to sterol and nonsterol agonists revealed a perpendicular histidinetryptophan switch that holds the receptor in its active conformation. Hydrogen bonding in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1b805b51c3cf75b118fcd22e4f6f97c8
https://doi.org/10.1074/jbc.m302260200

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Crystal Structure of the Glucocorticoid Receptor Ligand Binding Domain Reveals a Novel Mode of Receptor Dimerization and Coactivator Recognition

Autor: Thomas G. Consler, Kenneth H. Pearce, Chris J. Delves, Thomas B. Stanley, John T. Moore, Randy K. Bledsoe, Millard H. Lambert, Eugene L. Stewart, Valerie G. Montana, Derek J. Parks, David D. McKee, Christopher J. Apolito, H. Eric Xu, Timothy M. Willson

Publikováno v: Cell. 110:93-105

Transcriptional regulation by the glucocorticoid receptor (GR) is mediated by hormone binding, receptor dimerization, and coactivator recruitment. Here, we report the crystal structure of the human GR ligand binding domain (LBD) bound to dexamethason

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcf8f401a1be5048b1f1a377acb71026
https://doi.org/10.1016/s0092-8674(02)00817-6

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Pharmacophore Analysis of the Nuclear Oxysterol Receptor LXRα

Autor: Timothy M. Willson, Michael A. Watson, Randy K. Bledsoe, Jonathon S. Russel, Thomas A. Spencer, Jon L. Collins, Dansu Li, John T. Moore, Derek J. Parks, Linda B. Moore, Thomas G. Consler, Cristin M. Galardi, Millard H. Lambert, David D. McKee

Publikováno v: Journal of Medicinal Chemistry. 44:886-897

A cell-free assay was developed for the orphan nuclear receptor LXRalpha that measures the ligand-dependent recruitment of a peptide from the steroid receptor coactivator 1 (SRC1) to the nuclear receptor. Using this ligand-sensing assay (LiSA), the s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::062c6bd9d9a67bcd5efe125c72b9f14f
https://doi.org/10.1021/jm0004749

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Structure of the Tie2 RTK Domain

Autor: David D. McKee, Roderick G. Davis, John T. Moore, Byron Ellis, Lisa M. Shewchuk, William D. Holmes, Anne M. Hassell, Earnest Horne, Sue H. Kadwell

Publikováno v: Structure. 8:1105-1113

Background: Angiogenesis, the formation of new vessels from the existing vasculature, is a critical process during early development as well as in a number of disease processes. Tie2 (also known as Tek) is an endothelium-specific receptor tyrosine ki

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ff6d448312d095521df95e452e5b2c4
https://doi.org/10.1016/s0969-2126(00)00516-5

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Mode of binding of folate analogs to thymidylate synthase. Evidence for two asymmetric but interactive substrate binding sites

Autor: David D. McKee, R Ferone, B.B. Yates, Mary H. Hanlon, W.S. Dallas, I K Dev

Publikováno v: Journal of Biological Chemistry. 269:1873-1882

Human thymidylate synthase is a polymeric protein composed of two subunits with identical primary structures. In this study we determined the binding affinities of 5,10-methylene tetrahydropteroyltetraglutamate (folate substrate) and a group of close

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::63e169ea8edd2d35c09b6835a77b9e57
https://doi.org/10.1016/s0021-9258(17)42108-9

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ChemInform Abstract: (1-Pyrenylmethyl)amino Alcohols, a New Class of Antitumor DNA Intercalators. Discovery and Initial Amine Side Chain Structure- Activity Studies

Autor: Kenneth W. Bair, Vincent C. Knick, Michael Cory, Richard L. Tuttle, David D. McKee

Publikováno v: ChemInform. 22

In the series of 1-pyrenylmethylamines studied in this work the relationships among structure, interaction with DNA, and murine antitumor activity were examined. Binding studies show that all of these 1-pyrenylmethylamine derivatives bind to some ext

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1140423ae171d18d6f54202cb4dec008
https://doi.org/10.1002/chin.199108167

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X-ray crystal structures of the estrogen-related receptor-gamma ligand binding domain in three functional states reveal the molecular basis of small molecule regulation

Autor: Thomas G. Consler, William J. Zuercher, David D. McKee, Lisa A. Orband-Miller, Aaron B. Miller, Timothy M. Willson, Liping Wang, Millard H. Lambert, Robert T. Nolte

Publikováno v: The Journal of biological chemistry. 281(49)

X-ray crystal structures of the ligand binding domain (LBD) of the estrogen-related receptor-gamma (ERRgamma) were determined that describe this receptor in three distinct states: unliganded, inverse agonist bound, and agonist bound. Two structures w

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f29328931901c4804bec5c7ebd83ba20
https://pubmed.ncbi.nlm.nih.gov/16990259

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X-ray crystal structure of the liver X receptor beta ligand binding domain: regulation by a histidine-tryptophan switch

Autor: Shawn, Williams, Randy K, Bledsoe, Jon L, Collins, Sharon, Boggs, Millard H, Lambert, Ann B, Miller, John, Moore, David D, McKee, Linda, Moore, Jason, Nichols, Derek, Parks, Mike, Watson, Bruce, Wisely, Timothy M, Willson

Publikováno v: The Journal of biological chemistry. 278(29)

The x-ray crystal structures of the human liver X receptor beta ligand binding domain complexed to sterol and nonsterol agonists revealed a perpendicular histidinetryptophan switch that holds the receptor in its active conformation. Hydrogen bonding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5b8d31d1b6cfa775d81190d52d32791e
https://pubmed.ncbi.nlm.nih.gov/12736258

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Interaction of Galpha 12 and Galpha 13 with the cytoplasmic domain of cadherin provides a mechanism for beta -catenin release

Autor: David D. McKee, Patrick J. Casey, Timothy A. Fields, Thomas E. Meigs

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 98(2)

The G12 subfamily of heterotrimeric G proteins, comprised of the alpha-subunits Galpha12 and Galpha13, has been implicated as a signaling component in cellular processes ranging from cytoskeletal changes to cell growth and oncogenesis. In an attempt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74e8253e68f00e75dea38eb56d1c0c49
https://pubmed.ncbi.nlm.nih.gov/11136230

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The pregnane X receptor: a promiscuous xenobiotic receptor that has diverged during evolution

Autor: Nicholas C. O. Tomkinson, G. Bruce Wisely, John T. Moore, Timothy M. Willson, David D. McKee, Steven A. Kliewer, Millard H. Lambert, Stacey A. Jones, Geraldine A. Hamilton, Jennifer L. Shenk, Linda B. Moore, Edward L. LeCluyse

Publikováno v: Molecular endocrinology (Baltimore, Md.). 14(1)

Transcription of genes encoding cytochrome P450 3A (CYP3A) monooxygenases is induced by a variety of xenobiotics and natural steroids. There are marked differences in the compounds that induce CYP3A gene expression between species. Recently, the mous

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae88d8eff7c6e38940b06ef72afc2c47
https://pubmed.ncbi.nlm.nih.gov/10628745

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