Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding. - Wikidata - wikimedia - TriplyDB

Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

http://www.wikidata.org/entity/Q37335609

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ACE phenotyping in human heart.ACE Phenotyping as a Guide Toward Personalized Therapy With ACE Inhibitors.ACE phenotyping in Gaucher disease.

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Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

http://www.wikidata.org/entity/Q37335609

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

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bilimsel makale

@tr

scientific article published on 13 October 2016

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

@en

Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

@nl

type

label

Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

@en

Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

@nl

prefLabel

Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

@en

Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

@nl

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Scientific Reports

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Lysozyme and bilirubin bind to ACE and regulate its conformation and shedding.

@en

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Andrew B Nesterovitch

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

David E Schwartz

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

Eleftheria Letsiou

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

Henry T Akinbi

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

Joe G N Garcia

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

Olga A Kost

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

Olga V Kryukova

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

Randal O Dull

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

Richard D Minshall

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

Sergei M Danilov

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

P2860

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

A modern understanding of the traditional and nontraditional biological functions of angiotensin-converting enzyme

Signaling via the angiotensin-converting enzyme results in the phosphorylation of the nonmuscle myosin heavy chain IIA

HMDB 3.0--The Human Metabolome Database in 2013

Angiotensin I-converting enzyme mutation (Trp1197Stop) causes a dramatic increase in blood ACE

Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes

Shedding of somatic angiotensin-converting enzyme (ACE) is inefficient compared with testis ACE despite cleavage at identical stalk sites

The human serum proteome: display of nearly 3700 chromatographically separated protein spots on two-dimensional electrophoresis gels and identification of 325 distinct proteins.

An angiotensin I-converting enzyme mutation (Y465D) causes a dramatic increase in blood ACE via accelerated ACE shedding

Fine epitope mapping of monoclonal antibody 5F1 reveals anticatalytic activity toward the N domain of human angiotensin-converting enzyme.

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34913

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

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scholarly article

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10.1038/SREP34913

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6

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Heinrich Lünsdorf

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2016-10-13T00:00:00Z

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27734897

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5062130

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