Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Charles E. Aldinger"'
Autor:
Cyril Broccardo, Giovanna Chimini, Robert J. Aiello, Lori Royer, Jeffery de Wet, Christopher A. Gabel, Tom Turi, Omar L. Francone, John D. McNeish, Charles E. Aldinger, Marsha L. Roach, Kenneth L. Hoppe, Deborah Jean Guyot
Publikováno v:
Proceedings of the National Academy of Sciences. 97:4245-4250
Recently, the human ATP-binding cassette transporter-1 (ABC1) gene has been demonstrated to be mutated in patients with Tangier disease. To investigate the role of the ABC1 protein in an experimental in vivo model, we used gene targeting in DBA-1J em
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e894409cb6691ecc241a995ad2bf609
https://doi.org/10.1073/pnas.97.8.4245
https://doi.org/10.1073/pnas.97.8.4245
Autor:
Kelvin Cooper, Karen W. Hoover, Christine A. Kennedy, Wester Ronald Thure, Michael L. Mangiapane, Donald L. Bussolotti, Helen Berke, Mularski Christian J, Paul Da Silva Jardine, Albert L. Rauch, Janet A. LaFlamme, Philip A. Carpino, Michael Burkard, Charles E. Aldinger, George T. Magnus-Ayritey
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 4:133-138
The syntheses and biological activities of dihydropyridine angiotensin II (AII) antagonists are described. Compounds such as 12 are examples of a new, structurally distinct class of AT(in1-selective agents.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ef80cfada0f40be71605d888f8d48bb2
https://doi.org/10.1016/s0960-894x(01)81135-5
https://doi.org/10.1016/s0960-894x(01)81135-5
Autor:
Charles E. Aldinger, Todd W. Siegel, Larson Eric R, Thomas A. Beyer, Michael F. Dee, Banavara L. Mylari, David H. Singleton, William James Zembrowski
Publikováno v:
ChemInform. 22
A new working hypothesis that there is a hitherto unrecognized binding site on the aldose reductase (AR) enzyme with strong affinity for benzothiazoles was pursued for the design of novel, potent aldose reductase inhibitors (ARIs). The first applicat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f21eff51b0124f77bbd25a2b4d114057
https://doi.org/10.1002/chin.199122162
https://doi.org/10.1002/chin.199122162
Autor:
Charles E. Aldinger, Michael Burkard, C. A. Kennedy, R. T. Wester, K. Cooper, Michael L. Mangiapane, Donald L. Bussolotti, Helen Berke, P. Da Silva Jardine, A. L. Rauch, K. W. Hoover, C. J. Mularski, G. T. Magnus‐Ayritey, Philip A. Carpino, Janet A. LaFlamme
Publikováno v:
ChemInform. 25
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a654b73de627e347b8aeb2aec4d4175
https://doi.org/10.1002/chin.199426177
https://doi.org/10.1002/chin.199426177
Autor:
Todd W. Siegel, Thomas A. Beyer, William James Zembrowski, Banavara L. Mylari, Charles E. Aldinger
Publikováno v:
Journal of Medicinal Chemistry. 35:2155-2162
Benzothiazole side chains featured in zopolrestat (1a) and its congeners were incorporated into oxophthalazineacetic acid replacements, including indazole, pyridazinone, and pyridopyridazinone with a pendant acetic acid moiety. Potent aldose reductas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5693f016b2ac741757a81cd962f0c164
https://doi.org/10.1021/jm00090a002
https://doi.org/10.1021/jm00090a002
Autor:
Thomas A. Beyer, William James Zembrowski, Todd W. Siegel, Charles E. Aldinger, Michael F. Dee, Pamela J. Scott, Banavara L. Mylari
Publikováno v:
Journal of Medicinal Chemistry. 35:457-465
A broad structure-activity program was undertaken in search of effective surrogates for the key benzothiazole side chain of the potent aldose reductase inhibitor, zopolrestat (1). A structure-driven approach was pursued, which spanned exploration of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91b2684c05d6ddc6fc2c437a60eb0484
https://doi.org/10.1021/jm00081a006
https://doi.org/10.1021/jm00081a006
Autor:
Lori Royer, Roy L. Kerlin, Cheryl Myers Hayward, Ingrid M. Pruimboom-Brees, Jatinder Singh, Peter J. O'Brien, William J. Reagan, James Kenneth Loy, Christopher D. Kane, Dominique Brees, Charles E. Aldinger, Mehrdad Haghpassand, Omar L. Francone, Scott W. Bagley
Peroxisomal proliferator-activated receptor (PPAR)-alpha is a ligand-activated transcriptional factor that regulates genes involved in lipid metabolism and energy homeostasis. PPAR-alpha activators, including fibrates, have been used to treat dyslipi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed8ec780b156c2bf3f84cfb55fba60e6
https://europepmc.org/articles/PMC1698838/
https://europepmc.org/articles/PMC1698838/
Autor:
Thomas A. Beyer, Jon Bordner, Philip B. Inskeep, Douglas F. Burdi, Todd W. Siegel, Charles E. Aldinger, Christopher A. Lipinski, Donald L. Bussolotti
Publikováno v:
Journal of medicinal chemistry. 35(12)
The hypothesis that clinical side effects of the aldose reductase inhibitor (ARI) sorbinil were related to its hydantoin ring led to a bioisosteric analysis and replacement of the hydantoin by a spiro hydroxy acetic acid moiety as in 40. These hydrox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3eeed56009e5f466c7fec7cfd0874b2
https://pubmed.ncbi.nlm.nih.gov/1613744
https://pubmed.ncbi.nlm.nih.gov/1613744
Publikováno v:
Metabolism. 28:456-461
In some tissues containing aldose reductase, increased flux through the polyol pathway has been implicated as being causative in diabetic complications (e.g., cataracts, peripheral neuropathy). We have found CP-45,634 (d-6-fluoro-spiro[chroman-4,4′
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c66b6f901ab214264488510e8065d66e
https://doi.org/10.1016/0026-0495(79)90056-8
https://doi.org/10.1016/0026-0495(79)90056-8
Publikováno v:
Metabolism: clinical and experimental. 35(4 Suppl 1)
Increased flux of glucose through the polyol pathway with resultant resultant accumulation of tissue sorbitol is implicated in the pathogenesis of the chronic complications of diabetes. Sorbinil is a potent inhibitor of aldose reductase (the first en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f49971353ecfc5539daecbe6870c033c
https://pubmed.ncbi.nlm.nih.gov/3515121
https://pubmed.ncbi.nlm.nih.gov/3515121