Výsledky vyhledávání - "KellyAnn D. Pryor"

Discovery of Potent and Selective Dipeptidyl Peptidase IV Inhibitors Derived from β-Aminoamides Bearing Subsituted Triazolopiperazines

Publikováno v: Journal of Medicinal Chemistry. 51:589-602

A series of beta-aminoamides bearing triazolopiperazines have been discovered as potent, selective, and orally active dipeptidyl peptidase IV (DPP-4) inhibitors by extensive structure-activity relationship (SAR) studies around the triazolopiperazine

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea47e684c0a487b035f98caae89783bb
https://doi.org/10.1021/jm070330v

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Design, synthesis, and biological evaluation of triazolopiperazine-based β-amino amides as potent, orally active dipeptidyl peptidase IV (DPP-4) inhibitors

Autor: Ann E. Weber, Reshma A. Patel, Joseph K. Wu, Aleksandr Petrov, Frank Marsilio, Jennifer E. Kowalchick, KellyAnn D. Pryor, Nancy A. Thornberry, Barbara Leiting, Kathryn A. Lyons, Giovanna Scapin, Huaibing He, George J. Eiermann, Dooseop Kim

Publikováno v: Bioorganic & Medicinal Chemistry Letters. 17:5934-5939

Various beta-amino amides containing triazolopiperazine heterocycles have been prepared and evaluated as potent, selective, orally active dipeptidyl peptidase IV (DPP-4) inhibitors. These compounds display excellent oral bioavailability and good over

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e4b1107f9d56431f26f4262e6b4530a
https://doi.org/10.1016/j.bmcl.2007.07.100

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Triazolopiperazine-amides as dipeptidyl peptidase IV inhibitors: Close analogs of JANUVIA™ (sitagliptin phosphate)

Autor: Joseph K. Wu, KellyAnn D. Pryor, Ann E. Weber, George J. Eiermann, Reshma A. Patel, Dooseop Kim, Jinyou Xu, Nancy A. Thornberry, Anthony Mastracchio, Scott D. Edmondson, Jennifer E. Kowalchick, Huaibing He, Barbara Leiting, Kathryn A. Lyons

Publikováno v: Bioorganic & Medicinal Chemistry Letters. 17:3373-3377

A series of beta-aminoamides bearing triazolopiperazines has been prepared and evaluated as potent, selective, orally active dipeptidyl peptidase IV (DPP-4) inhibitors. Efforts at optimization of the beta-aminoamide series, which ultimately led to th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::599f25f09625a28655ac50e27db98260
https://doi.org/10.1016/j.bmcl.2007.03.098

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Purification, crystallization and preliminary X-ray analysis ofEscherichia coliUDP-N-acetylmuramoyl:L-alanine ligase (MurC)

Autor: Edward N. Baker, KellyAnn D. Pryor, Clyde A. Smith, Barbara Leiting, Taru Deva

Publikováno v: Acta Crystallographica Section D Biological Crystallography. 59:1510-1513

UDP-N-acetylmuramoyl:L-alanine ligase (MurC) is involved in the pathway leading from UDP-N-glucosamine to the UDP-N-acetylmuramoyl:pentapeptide unit, which is the building block for the peptidoglycan layer found in all bacterial cell walls. The pathw

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7a5b89d963324a5fe53a12699514244
https://doi.org/10.1107/s090744490301285x

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[Untitled]

Autor: Stephan K. Grant, KellyAnn D. Pryor, Barbara Leiting, John F. O'Connell

Publikováno v: Journal of Biomolecular NMR. 13:311-324

The NMR structure of the peptide deformylase (PDF) (1‐150) from Escherichia coli, which is an essential enzyme that removes the formyl group from nascent polypeptides and represents a potential target for drug discovery, was determined using 15 N/

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::499cec8990524671687f63dd2c75775c
https://doi.org/10.1023/a:1008311502626

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Genetic ablation or pharmacological blockade of dipeptidyl peptidase IV does not impact T cell-dependent immune responses

Autor: KellyAnn D. Pryor, Gene Porter, George J. Eiermann, Yan-Yan Cui, Kalpit A. Vora, Dennis M. Zaller, Roche Peng

Publikováno v: BMC Immunology, Vol 10, Iss 1, p 19 (2009)
BMC Immunology

Background Current literature suggests that dipeptidyl peptidase IV (DPP-IV; CD26) plays an essential role in T-dependent immune responses, a role that could have important clinical consequences. To rigorously define the role of DPP-IV in the immune

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6e5dda34dea8be1c0c85d428e7ddd0e
http://www.biomedcentral.com/1471-2172/10/19

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Inhibition of dipeptidyl-peptidase IV does not increase circulating IGF-1 concentrations in growing pigs

Autor: KellyAnn D. Pryor, Donald Thompson, G. J. Hickey, Kathy Lyons, Barbara Leiting, Terry D. Faidley

Publikováno v: Experimental biology and medicine (Maywood, N.J.). 231(8)

The enzyme dipeptidyl peptidase-IV (DPP-IV) inactivates a variety of bioactive peptides, including glucagon-like peptide-1 (GLP-1) and growth hormone releasing hormone (GHRH). Inhibiting DPP-IV in order to increase circulating GLP-1 is of interest as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d98a6943ce715ad54d241bbf63f1ef6d
https://pubmed.ncbi.nlm.nih.gov/16946406

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Catalytic properties and inhibition of proline-specific dipeptidyl peptidases II, IV and VII

Autor: Nancy A. Thornberry, Jonathan A. Ellman, Richard T. Cummings, Charles S. Craik, Frank Marsilio, Joseph K. Wu, KellyAnn D. Pryor, Barbara Leiting, Reshma A. Patel

Publikováno v: The Biochemical journal. 371(Pt 2)

There is currently intense interest in the emerging group of proline-specific dipeptidases, and their roles in the regulation of biological processes. Dipeptidyl peptidase IV (DPP-IV) is involved in glucose metabolism by contributing to the regulatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58b84364a8181b366b3b08d13144b325
https://pubmed.ncbi.nlm.nih.gov/12529175

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One-day enzymatic synthesis and purification of UDP-N- [1-14C]acetyl-glucosamine

Autor: Suzanne S. Eveland, KellyAnn D. Pryor, Barbara Leiting, Matt S. Anderson

Publikováno v: Analytical biochemistry. 256(2)

UDP-GlcN[1-14C]Ac was synthesized in a single enzymatic reaction from [1-14C]acetate and commercially available precursors on both a microcurie (micromole) and a millicurie (millimole) scale. The reaction was catalyzed by the action of acetyl coenzym

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17c71cdb04476e58929e5e1bb1cbc183
https://pubmed.ncbi.nlm.nih.gov/9473276

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