Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Thomas L. Emmons"'
Autor:
James R. Kiefer, Joseph W. Leone, Alfredo G. Tomasselli, Robin A. Weinberg, Akshay Patny, H. David Fischer, Cynthia D. Sommers, Jennifer A. Gormley, Timothy E. Benson, Horng-Chih Huang, E.J. Jacobsen, Jacqueline E. Day, Thomas L. Emmons, Jill Chrencik, Iris K. Leung, Jeffrey L. Hirsch, Tenbrink Ruth E, Jennifer M. Williams, Brian Korniski, Troii Hall
Publikováno v:
Journal of Molecular Biology. 400:413-433
Janus kinases (JAKs) are critical regulators of cytokine pathways and attractive targets of therapeutic value in both inflammatory and myeloproliferative diseases. Although the crystal structures of active JAK1 and JAK2 kinase domains have been repor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b19fab0c9dc63112be2b1f9f66fc065
https://doi.org/10.1016/j.jmb.2010.05.020
https://doi.org/10.1016/j.jmb.2010.05.020
Autor:
Thomas L. Emmons, Alfredo G. Tomasselli, Robin A. Weinberg, H. David Fischer, Jill Chrencik, Brian Korniski, Jacqueline E. Day, Stacy Brown, Joseph W. Leone, Ann D. Wrightstone, Cynthia D. Sommers, Jeffrey L. Hirsch, Arthur J. Wittwer, Troii Hall, Jennifer A. Gormley
Publikováno v:
Biochemical and Biophysical Research Communications. 396:543-548
The Janus kinase family consists of four members: JAK-1, -2, -3 and TYK-2. While JAK-2 and JAK-3 have been well characterized biochemically, there is little data on TYK-2. Recent work suggests that TYK-2 may play a critical role in the development of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4568dae04b1e101103ca4b31d2d17487
https://doi.org/10.1016/j.bbrc.2010.04.141
https://doi.org/10.1016/j.bbrc.2010.04.141
Autor:
Thomas L. Emmons, James R. Kiefer, Joseph W. Leone, John F. Schindler, Melissa S. Harris, Jacqueline E. Day, Siradanahalli Guru, Alfredo G. Tomasselli, Robin A. Weinberg, Sandra Lightle, H. David Fischer, Jeffrey L. Hirsch, Jill Chrencik, Jennifer A. Gormley, Jennifer M. Williams, Matthew J. Saabye, Troii Hall
Publikováno v:
Protein Expression and Purification. 69:54-63
Janus-associated kinases (JAKs) play critical roles in cytokine signaling, and have emerged as viable therapeutic targets in inflammation and oncology related diseases. To date, targeting JAK proteins with highly selective inhibitor compounds have re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68adb1eba9066345bc1000db1eef31a2
https://doi.org/10.1016/j.pep.2009.09.011
https://doi.org/10.1016/j.pep.2009.09.011
Autor:
Beverly A. Reitz, Joseph W. Leone, Michael J. Bienkowski, Daniel F. Curran, Karl J. Mathis, Thomas L. Emmons, Jacqueline E. Day, Mary E. Shuck, Mark C. Walker, Alfredo G. Tomasselli, H. David Fischer
Publikováno v:
Protein Expression and Purification. 65:133-139
Soluble guanylate cyclase (sGC) has been purified from 100 L cell culture infected by baculovirus using the newer and highly effective titerless infected-cells preservation and scale-up (TIPS) method. Successive passage of the enzyme through DEAE, Ni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::429666b5c5f068867bf311b4dcaba1ae
https://doi.org/10.1016/j.pep.2009.01.001
https://doi.org/10.1016/j.pep.2009.01.001
Autor:
Beverly A. Reitz, Thomas L. Emmons, Alfredo G. Tomasselli, H. David Fischer, Michael J. Bienkowski, S. Edward Lee, David Wasilko, Karl J. Mathis, Kim Jonelle Stutzman-Engwall
Publikováno v:
Protein Expression and Purification. 65:122-132
Compounds capable of stimulating soluble guanylate cyclase (sGC) activity might become important new tools to treat hypertension. While rational design of these drugs would be aided by elucidation of the sGC three-dimensional structure and molecular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d67ccc292e9fe1d6be21cbe94fae775
https://doi.org/10.1016/j.pep.2009.01.002
https://doi.org/10.1016/j.pep.2009.01.002
Autor:
A. M. Mildner, R. L. Heinrikson, H. D. Fischer, J. M. Lull, Thomas L. Emmons, Alfredo G. Tomasselli, J. W. Leone
Publikováno v:
Protein & Peptide Letters. 16:121-131
Evidence for a key role of beta-amyloid (Abeta) in Alzheimer's disease has led to considerable interest in potential therapeutic strategies targeting enzymes involved in processing the amyloid precursor protein (APP). Beta-site APP Cleaving Enzyme (B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::153494af09ae75bfc3776dbf2125b283
https://doi.org/10.2174/092986609787316180
https://doi.org/10.2174/092986609787316180
Autor:
Timothy E. Benson, Michael J. Bienkowski, Tenbrink Ruth E, Alice Laborde, D. Bryan Prince, Joseph B. Moon, Steven W. Kortum, Thomas L. Emmons, Alfredo G. Tomasselli, Donna J. Paddock
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 17:3378-3383
The design and synthesis of a novel series of potent BACE1 hydroxyethylamine inhibitors. These inhibitors feature hydrogen bonding substituents at the C-5 position of the isophthalamide ring with improved selectivity over cathepsin D.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::329853e7edfb397bc11c47aeb2ba4871
https://doi.org/10.1016/j.bmcl.2007.03.096
https://doi.org/10.1016/j.bmcl.2007.03.096
Autor:
John N. Freskos, Yvette M. Fobian, Timothy E. Benson, Michael J. Bienkowski, David L. Brown, Thomas L. Emmons, Robert Heintz, Alice Laborde, Joseph J. McDonald, Brent V. Mischke, John M. Molyneaux, Joseph B. Moon, Patrick B. Mullins, D. Bryan Prince, Donna J. Paddock, Alfredo G. Tomasselli, Gregory Winterrowd
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 17:73-77
We describe a novel series of potent inhibitors of human beta-secretase. These compounds possess the hydroxyethyl amine transition state isostere. A 2.5A crystal structure of inhibitor 32 bound to BACE is provided.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48e643373fd67faba63c23379fdd0447
https://doi.org/10.1016/j.bmcl.2006.09.092
https://doi.org/10.1016/j.bmcl.2006.09.092
Autor:
Thomas L. Emmons, John K. Kawooya, Susan C D’Andrea, Patricia A Gonzalez-DeWhitt, Melissa C Camp
Publikováno v:
Analytical Biochemistry. 323:103-113
The 43-amino acid Alzheimer's amyloid-beta peptide (Abeta peptide) retains a predominantly alpha-helix and beta-strand structure in sodium dodecyl sulfate (SDS) solution. This conformer has a high tendency to aggregate during conventional SDS-polyacr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31d8d1be9ddeea9338cf38cb6b5b5195
https://doi.org/10.1016/j.ab.2003.08.027
https://doi.org/10.1016/j.ab.2003.08.027
Autor:
June M. Lull, Carol A. Bannow, Riqiang Yan, Alfredo G. Tomasselli, Thomas L. Emmons, Isam Qahwash, Michael Jerome Bienkowski, Kam F. Fok, Clark W. Smith, Joseph W. Leone, Yifeng Lu, Robert L. Heinrikson
Publikováno v:
Journal of Neurochemistry. 84:1006-1017
The involvement of β-secretase (BACE1; β-site APP-cleaving enzyme) in producing the β-amyloid component of plaques found in the brains of Alzheimer's patients, has fueled a major research effort to characterize this protease. Here, we describe wor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::918f105b854f505ed1ea7223d2f1ff7c
https://doi.org/10.1046/j.1471-4159.2003.01597.x
https://doi.org/10.1046/j.1471-4159.2003.01597.x