Results 151 to 160 of about 12,907 (206)

Antidiabetic Effects of <i>Ecklonia cava</i> and Dieckol via DPP-IV Inhibition and Glucose Transport Regulation. [PDF]

Mar Drugs
Suryaningtyas IT, Shafura N, Pangestuti R, Jung WK, Je JY.   +4 more
europepmc   +1 more source

SGLT2 Inhibitor Use and Cardiorenal Outcomes in Type 2 Diabetes With Liver Cirrhosis.

JAMA Netw Open
Chung MC, Yu TM, Wu LY, Wu MJ, Shieh JJ, Chung CJ.   +5 more
europepmc   +1 more source

Potent non-nitrile dipeptidic dipeptidyl peptidase IV inhibitors [PDF]

Bioorganic & Medicinal Chemistry Letters, 2007
The synthesis and structure-activity relationships of novel dipeptidyl peptidase IV inhibitors replacing the classical cyanopyrrolidine P1 group with other small nitrogen heterocycles are described. A unique potency enhancement was achieved with beta-branched natural and unnatural amino acids, particularly adamantylglycines, linked to a (2S,3R)-2,3 ...
Ligaya M, Simpkins, Scott, Bolton, Zulan, Pi, James C, Sutton, Chet, Kwon, Guohua, Zhao, David R, Magnin, David J, Augeri, Timur, Gungor, David P, Rotella, Zhong, Sun, Yajun, Liu, William S, Slusarchyk, Jovita, Marcinkeviciene, James G, Robertson, Aiying, Wang, Jeffrey A, Robl, Karnail S, Atwal, Robert L, Zahler, Rex A, Parker, Mark S, Kirby, Lawrence G, Hamann   +21 more
openaire   +3 more sources

A three-dimensional pharmacophore model for dipeptidyl peptidase IV inhibitors [PDF]

European Journal of Medicinal Chemistry, 2008
Dipeptidyl peptidase IV (DPP-IV) is a valid drug target for type-2 diabetes and DPP-IV inhibitors have been proven to efficiently improve glucose tolerance. In our study, 3D pharmacophore models were generated using a training set of 22 DPP-IV inhibitors.
I-Lin, Lu, Keng-Chang, Tsai, Yi-Kun, Chiang, Weir-Torn, Jiaang, Ssu-Hui, Wu, Neeraj, Mahindroo, Chia-Hui, Chien, Shiow-Ju, Lee, Xin, Chen, Yu-Sheng, Chao, Su-Ying, Wu   +10 more
openaire   +3 more sources

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Fluoropyrrolidine amides as dipeptidyl peptidase IV inhibitors

Bioorganic & Medicinal Chemistry Letters, 2004
Amides derived from fluorinated pyrrolidines and 4-substituted cyclohexylglycine analogues have been prepared and evaluated as inhibitors of dipeptidyl dipeptidase IV (DP-IV). Analogues which incorporated (S)-3-fluoropyrrolidine showed good selectivity for DP-IV over quiescent cell proline dipeptidase (QPP).
Charles G, Caldwell, Ping, Chen, Jiafang, He, Emma R, Parmee, Barbara, Leiting, Frank, Marsilio, Reshma A, Patel, Joseph K, Wu, George J, Eiermann, Aleksandr, Petrov, Huaibing, He, Kathryn A, Lyons, Nancy A, Thornberry, Ann E, Weber   +13 more
openaire   +3 more sources

A potent dipeptide inhibitor of dipeptidyl peptidase IV

Bioorganic & Medicinal Chemistry Letters, 1998
A series of novel potent inhibitors of dipeptidyl peptidase IV (DPP-IV) has been developed. A brief structure-activity relationship of the inhibitors was investigated. The dipeptide TSL-225, tryptophyl-1,2,3,4-tetrahydroisoquinoline-3-carboxylic acid, was identified with the critical structure for the inhibitory activity.
M, Yamada, C, Okagaki, T, Higashijima, S, Tanaka, T, Ohnuki, T, Sugita   +5 more
openaire   +2 more sources

Suppression of arthritis by the inhibitors of dipeptidyl peptidase IV

International Journal of Immunopharmacology, 1997
Dipeptidyl peptidase IV (DP IV, CD26) is a serine exoprotease which selectively cleaves the penultimate proline residue of polypeptides. This enzyme is also expressed as a surface marker on activated T cells. In order to assess the relevance of DP IV in immunological disorders, we evaluated the in vivo effects of specific DP IV inhibitors using two ...
S, Tanaka, T, Murakami, H, Horikawa, M, Sugiura, K, Kawashima, T, Sugita   +5 more
openaire   +2 more sources

Recent patents of dipeptidyl peptidase IV inhibitors

Expert Opinion on Therapeutic Patents, 2011
The serine exopeptidase DPP IV is a dual protein able to work as an enzyme and an interacting protein. The incretin molecules glucagon-like peptide 1 (GLP-1) and glucose-dependent insulinotropic peptide (GIP) are hydrolyzed by DPP IV into inactive forms, which are unable to promote insulin secretion.
Laura, Mendieta, Teresa, Tarrago, Ernest, Giralt   +2 more
openaire   +2 more sources