Interkingdom Pharmacology of Angiotensin-I Converting Enzyme Inhibitor Phosphonates Produced by Actinomycetes - Wikidata - awgldk - TriplyDB

Interkingdom Pharmacology of Angiotensin-I Converting Enzyme Inhibitor Phosphonates Produced by Actinomycetes

Interkingdom Pharmacology of Angiotensin-I Converting Enzyme Inhibitor Phosphonates Produced by Actinomycetes

http://www.wikidata.org/entity/Q27684235

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Discovery of Anti-Hypertensive Oligopeptides from Adlay Based on In Silico Proteolysis and Virtual Screening.Identification of bioactive peptide from Oreochromis niloticus skin gelatin.Crystal structure of a peptidyl-dipeptidase K-26-DCP from Actinomycete in complex with its natural inhibitor.Phosphonic acid: preparation and applications.

P2860

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P2860

Interkingdom Pharmacology of Angiotensin-I Converting Enzyme Inhibitor Phosphonates Produced by Actinomycetes

http://www.wikidata.org/entity/Q27684235

description

2014 nî lūn-bûn

@nan

2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年学术文章

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2014年学术文章

@zh-cn

2014年学术文章

@zh-hans

2014年学术文章

@zh-my

2014年学术文章

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2014年學術文章

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name

Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

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Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

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Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

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Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

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Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

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Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

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Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

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Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

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Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

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P1433

ACS Medicinal Chemistry Letters

P1476

Interkingdom Pharmacology of A ...... ates Produced by Actinomycetes

@en

P2093

Akif Mohd

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Edward D Sturrock

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Glenna J Kramer

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Sylva L U Schwager

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P2860

Crystal structure of the human angiotensin-converting enzyme-lisinopril complex

Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning

Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides

The two homologous domains of human angiotensin I-converting enzyme are both catalytically active

The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors

Crystal structure of a phosphonotripeptide K-26 in complex with angiotensin converting enzyme homologue (AnCE) from Drosophila melanogaster

The N Domain of Human Angiotensin-I-converting Enzyme: THE ROLE OF N-GLYCOSYLATION AND THE CRYSTAL STRUCTURE IN COMPLEX WITH AN N DOMAIN-SPECIFIC PHOSPHINIC INHIBITOR, RXP407

Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme

Natural products as sources of new drugs over the 30 years from 1981 to 2010

RXP 407, a phosphinic peptide, is a potent inhibitor of angiotensin I converting enzyme able to differentiate between its two active sites.

P304

346-351

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scholarly article

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10.1021/ML4004588

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4

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5

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Geoffrey Masuyer

K. Ravi Acharya

Brian O Bachmann

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2014-04-10T00:00:00Z

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262886161

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24900839

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Aagianik kimischri

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4027624

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