Dipeptidyl peptidase-4 inhibitors: Novel mechanism of actions

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The Nonglycemic Actions of Dipeptidyl Peptidase-4 Inhibitors

A cell surface serine protease, dipeptidyl peptidase 4 (DPP-4), cleaves dipeptide from peptides containing proline or alanine in the N-terminal penultimate position. Two important incretin hormones, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic peptide (GIP), enhance meal-stimulated insulin secretion from pancreatic β-cells, but are inactivated by DPP-4. Diabetes and hype...

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Dipeptidyl Peptidase-4 Inhibitors and Bone Fractures

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Dipeptidyl-peptidase-4 inhibitors for treatment of type 2 diabetes.

OBJECTIVE To assess the efficacy and safety of dipeptidyl peptidase-4 (DPP-4) inhibitors compared with metformin as monotherapy, or with other commonly used hypoglycaemic drugs combined with metformin, in adults with type 2 diabetes mellitus. DESIGN Systematic review and meta-analysis of randomised controlled trials. DATA SOURCES Medline, Embase, the Cochrane Library, conference proceedings...

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Navigating the chemical space of dipeptidyl peptidase-4 inhibitors

This study represents the first large-scale study on the chemical space of inhibitors of dipeptidyl peptidase-4 (DPP4), which is a potential therapeutic protein target for the treatment of diabetes mellitus. Herein, a large set of 2,937 compounds evaluated for their ability to inhibit DPP4 was compiled from the literature. Molecular descriptors were generated from the geometrically optimized lo...

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Dipeptidyl Peptidase-4 Inhibitor

In the United States, nearly 13% of adults aged 20 years and older have type 2 diabetes mellitus (T2DM), and its prevalence is still increasing (1,2). Microvascular and macrovascular abnormalities are common in patients with T2DM and are related to the severity and duration of hyperglycemia (3–5). Thus, treatment of hyperglycemia is an important way to prevent or delay diabetic vascular complic...

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ژورنال

عنوان ژورنال: Indian Journal of Endocrinology and Metabolism

سال: 2014

ISSN: 2230-8210

DOI: 10.4103/2230-8210.141319