Zobrazeno 1 - 10
of 12
pro vyhledávání: '"David W. Kuo"'
Autor:
Kenny K. Wong, David W. Kuo, Barbara Azzolina, James Mu, Xiling Yuan, John R. Thompson, Mohamed El-Sherbeini, Joel P. Berger, Eric S. Muise, Yejun Tan
Publikováno v:
Molecular Pharmacology. 74:403-412
Adipose tissue is a metabolically responsive endocrine organ that secretes a myriad of adipokines. Antidiabetic drugs such as peroxisome proliferator-activated receptor (PPAR) gamma agonists target adipose tissue gene expression and correct hyperglyc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d5a480182fd4874ce777d3abe7e6ed2
https://doi.org/10.1124/mol.108.044826
https://doi.org/10.1124/mol.108.044826
Publikováno v:
Journal of the American Chemical Society. 121:1175-1178
The first six cytoplasmic intermediates of murein biosynthesis (2−7) have been prepared in high yield (>60%) and at preparative scale (10−100 mg) using purified enzymes of the murein biosynthetic p...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89ee9b0edb778a03d52a7c02e40a82a7
https://doi.org/10.1021/ja983850b
https://doi.org/10.1021/ja983850b
Autor:
Randall R. Eversole, Richard K. Harrison, Soumya P. Sahoo, Sander G. Mills, Lisa M. Niedzwiecki, Scott A. Polo, B. Chang, Charles G. Caldwell, Maria Izquierdo-Martin, Thomas J. Lanza, Philippe L. Durette, Tsau-Yen Lin, Ross L. Stein, William K. Hagmann, David W. Kuo
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 6:323-328
The matrix metalloproteinase stromelysin-1 (MMP-3) is inhibited more strongly by peptidyl phosphinic acid 7 than by its corresponding phosphonamidate and phosphonate analogs. Extending a benzyl group at P′ 1 to a phenylethyl group in 8 further incr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ff9296779e0d601aecee6bbaae03e09b
https://doi.org/10.1016/0960-894x(96)00023-6
https://doi.org/10.1016/0960-894x(96)00023-6
Autor:
C. S. Burgey, Liesch J, Shrenik K. Shah, David W. Kuo, Renee M. Chabin, B G Green, Alan L. Maycock, Gale P, Sander G. Mills, Dennis J. Underwood
Publikováno v:
Biochemistry. 34:14331-14343
The monocyclic beta-lactams reported by Knight et al. [Knight, W. B., et al. (1992) Biochemistry 31, 8160; Chabin, R., et al. (1993) Biochemistry 32, 8970] as inhibitors of human leucocyte elastase (HLE) produce stable HLE-inhibitor complexes that sl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a21c8c4964ff8ea7e572ee6a061a7fee
https://doi.org/10.1021/bi00044a010
https://doi.org/10.1021/bi00044a010
Autor:
Filippo Russo, Renee M. Chabin, W. B. Knight, Salvatore Guccione, David W. Kuo, Giuseppe Romeo
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 4:2399-2404
A novel thiazinoindole tricyclic ring system was designed as potential inhibitors of serine proteases. The compounds were synthesized by ring closure at 80–90°C in poliphosphoric acid of the appropriate N′-alkyl or aryl substituted indolylthiour
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b6be4448adf80668703c68af64ed74a0
https://doi.org/10.1016/s0960-894x(01)80398-x
https://doi.org/10.1016/s0960-894x(01)80398-x
Publikováno v:
Biochemistry. 33:8347-8354
Bacterial leader peptidase (LPase) is a potential target for the development of novel anti-infective agents, but to data only peptides based upon natural macromolecular substrates have been reported as inhibitors. In this work is described a continuo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::145c6eee5292ed80c1cc7490b63a2bdb
https://doi.org/10.1021/bi00193a023
https://doi.org/10.1021/bi00193a023
Autor:
William K. Hagmann, Maria Izquierdo-Martin, Tsau-Yen Lin, Ross L. Stein, Richard K. Harrison, Philippe L. Durette, David W. Kuo, Joanne F. Kinneary, Joung L. Goulet
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 4:1221-1224
A series of phosphinic acid-containing peptide inhibitors of human stromelysin-1 (MMP-3) were prepared. The P1 through P3 subsites were varied in a systematic manner on analogs possessing an invariant P1′-P3′ segment. The in vitro activity of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eed374c79819c380fdb8837543ab7d30
https://doi.org/10.1016/s0960-894x(01)80334-6
https://doi.org/10.1016/s0960-894x(01)80334-6
Autor:
Hollis R. Williams, Corey J. Wilson, Patrick R. Griffin, David W. Kuo, H.K. Chan, W. B. Knight
Publikováno v:
Archives of Biochemistry and Biophysics. 303:274-280
The report by Zimmerman et al. (J. Biol. Chem. 257, 1982, 6529-6536) that the active site of Escherichia coli leader peptidase (LPase) is located in the periplasm led us to explore the possibility that soluble, active short forms of LPase could be pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02e0db1b899c1f052078faf3c335cc42
https://doi.org/10.1006/abbi.1993.1283
https://doi.org/10.1006/abbi.1993.1283
Autor:
Filippo Russo, Giuseppe Romeo, Salvatore Guccione, David W. Kuo, Renee M. Chabin, W. B. Knight
Publikováno v:
ChemInform. 26
A novel thiazinoindole tricyclic ring system was designed as potential inhibitors of serine proteases. The compounds were synthesized by ring closure at 80–90°C in poliphosphoric acid of the appropriate N′-alkyl or aryl substituted indolylthiour
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::39c824a2103104bf9ced6cd718a23c3c
https://doi.org/10.1002/chin.199519158
https://doi.org/10.1002/chin.199519158
Specificity, stability, and potency of monocyclic beta-lactam inhibitors of human leucocyte elastase
Autor:
H. Weston, W. B. Knight, Alan L. Maycock, Paul E. Finke, Gale P, C P Dorn, B G Green, David W. Kuo, Westler Wm, Renee M. Chabin
Publikováno v:
Biochemistry. 31(35)
Stable, potent, highly specific, time-dependent monocyclic beta-lactam inhibitors of human leucocyte elastase (HLE) are described. The heavily substituted beta-lactams are stable under physiological conditions including in the presence of enzymes of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f23aee439cff4fdeb396d4b47a44d23c
https://pubmed.ncbi.nlm.nih.gov/1525156
https://pubmed.ncbi.nlm.nih.gov/1525156