Anagliptin, a potent dipeptidyl peptidase IV inhibitor: its single-crystal structure and enzyme interactions - Wikidata - awgldk - TriplyDB

Anagliptin, a potent dipeptidyl peptidase IV inhibitor: its single-crystal structure and enzyme interactions

Anagliptin, a potent dipeptidyl peptidase IV inhibitor: its single-crystal structure and enzyme interactions

http://www.wikidata.org/entity/Q27701492

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Antidiabetic treatment with gliptins: focus on cardiovascular effects and outcomes Comprehensive analysis of the Co-structures of dipeptidyl peptidase IV and its inhibitor Predicting DPP-IV inhibitors with machine learning approaches.Anagliptin ameliorates albuminuria and urinary liver-type fatty acid-binding protein excretion in patients with type 2 diabetes with nephropathy in a glucose-lowering-independent manner.Dipeptidyl Peptidase-4 Inhibitor Anagliptin Prevents Intracranial Aneurysm Growth by Suppressing Macrophage Infiltration and Activation.Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues.

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P2860

Anagliptin, a potent dipeptidyl peptidase IV inhibitor: its single-crystal structure and enzyme interactions

http://www.wikidata.org/entity/Q27701492

description

2015 nî lūn-bûn

@nan

2015 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Anagliptin, a potent dipeptidy ...... ucture and enzyme interactions

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Anagliptin, a potent dipeptidy ...... ucture and enzyme interactions

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Anagliptin, a potent dipeptidy ...... ucture and enzyme interactions

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Anagliptin, a potent dipeptidy ...... ucture and enzyme interactions

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Anagliptin, a potent dipeptidy ...... ucture and enzyme interactions

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Anagliptin, a potent dipeptidy ...... ucture and enzyme interactions

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14756366.2014.1002402

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Journal of Enzyme Inhibition and Medicinal Chemistry

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Anagliptin, a potent dipeptidy ...... ucture and enzyme interactions

@en

P2093

Mitsuru Oka

http://www.w3.org/2001/XMLSchema#string

Ryo Takahashi

http://www.w3.org/2001/XMLSchema#string

Shino Okada

http://www.w3.org/2001/XMLSchema#string

Tomoko Motoyama

http://www.w3.org/2001/XMLSchema#string

Yoshika Yasuda

http://www.w3.org/2001/XMLSchema#string

Yukihisa S Watanabe

http://www.w3.org/2001/XMLSchema#string

Yuko Kojima

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog

The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold

The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism

Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV

Discovery of alogliptin: a potent, selective, bioavailable, and efficacious inhibitor of dipeptidyl peptidase IV

Involvement of DPP-IV catalytic residues in enzyme-saxagliptin complex formation

Synthesis and biological evaluation of homopiperazine derivatives with beta-aminoacyl group as dipeptidyl peptidase IV inhibitors

Fused bicyclic heteroarylpiperazine-substituted L-prolylthiazolidines as highly potent DPP-4 inhibitors lacking the electrophilic nitrile group

Discovery and preclinical profile of teneligliptin (3-[(2S,4S)-4-[4-(3-methyl-1-phenyl-1H-pyrazol-5-yl)piperazin-1-yl]pyrrolidin-2-ylcarbonyl]thiazolidine): a highly potent, selective, long-lasting and orally active dipeptidyl peptidase IV inhibitor

A comparative study of the binding modes of recently launched dipeptidyl peptidase IV inhibitors in the active site

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10.3109/14756366.2014.1002402

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6

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30

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2015-12-01T00:00:00Z

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crystal structure