Novel mechanism of inhibition of human angiotensin-I-converting enzyme (ACE) by a highly specific phosphinic tripeptide - Wikidata - awgldk - TriplyDB

Novel mechanism of inhibition of human angiotensin-I-converting enzyme (ACE) by a highly specific phosphinic tripeptide

Novel mechanism of inhibition of human angiotensin-I-converting enzyme (ACE) by a highly specific phosphinic tripeptide

http://www.wikidata.org/entity/Q27667064

about

Crystal structures of highly specific phosphinic tripeptide enantiomers in complex with the angiotensin-I converting enzyme The toxicity of angiotensin converting enzyme inhibitors to larvae of the disease vectors Aedes aegypti and Anopheles gambiae Serine protease inhibition by a silanediol peptidomimetic.Emerging drugs which target the renin-angiotensin-aldosterone system.Insight into the interactive residues between two domains of human somatic Angiotensin-converting enzyme and Angiotensin II by MM-PBSA calculation and steered molecular dynamics simulation.

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P2860

Novel mechanism of inhibition of human angiotensin-I-converting enzyme (ACE) by a highly specific phosphinic tripeptide

http://www.wikidata.org/entity/Q27667064

description

2011 nî lūn-bûn

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2011 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մայիսին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Novel mechanism of inhibition ...... specific phosphinic tripeptide

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Novel mechanism of inhibition ...... specific phosphinic tripeptide

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Novel mechanism of inhibition ...... specific phosphinic tripeptide

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type

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Novel mechanism of inhibition ...... specific phosphinic tripeptide

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Novel mechanism of inhibition ...... specific phosphinic tripeptide

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Novel mechanism of inhibition ...... specific phosphinic tripeptide

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Novel mechanism of inhibition ...... specific phosphinic tripeptide

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Novel mechanism of inhibition ...... specific phosphinic tripeptide

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Novel mechanism of inhibition ...... specific phosphinic tripeptide

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Biochemical Journal

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Novel mechanism of inhibition ...... specific phosphinic tripeptide

@en

P2093

Colin S Anthony

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Edward D Sturrock

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Fabrice Beau

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Mohd Akif

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Sylva L Schwager

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

Vincent Dive

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

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 hemoregulatory peptide N-acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme

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

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

Processing of X-ray diffraction data collected in oscillation mode

Probing the basis of domain-dependent inhibition using novel ketone inhibitors of Angiotensin-converting enzyme

Characterization of domain-selective inhibitor binding in angiotensin-converting enzyme using a novel derivative of lisinopril

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

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53-59

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scholarly article

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10.1042/BJ20102123

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1

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436

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K. Ravi Acharya

Bertrand Czarny

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2011-05-01T00:00:00Z

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21352096

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3086271

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