Skip to main navigation
Skip to search
Skip to main content
Search All UT System Experts
University of Texas Southwestern Medical Center Home
Home
Profiles
Research units
Equipment
Research output
Search by expertise, name or affiliation
Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum
Noriaki Emoto,
Masashi Yanagisawa
Molecular Genetics
Molecular Genetics
Research output
:
Contribution to journal
›
Article
›
peer-review
437
Scopus citations
Overview
Fingerprint
Fingerprint
Dive into the research topics of 'Endothelin-converting enzyme-2 is a membrane-bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum'. Together they form a unique fingerprint.
Sort by
Weight
Alphabetically
Medicine & Life Sciences
phosphoramidon
100%
Endothelin-Converting Enzymes
99%
Endothelin-1
70%
Metalloproteases
70%
Membranes
38%
WS 79089B
28%
Cricetulus
20%
Ovary
17%
human KEL protein
15%
Enzymes
14%
big endothelin 2
12%
Complementary DNA
10%
Endothelin-3
9%
trans-Golgi Network
8%
Neprilysin
8%
Captopril
7%
Secretory Pathway
7%
Molecular Cloning
7%
Endothelins
7%
Coculture Techniques
6%
Amino Acid Sequence
6%
In Vitro Techniques
5%
Cattle
5%
Peptides
4%
Chemical Compounds
Endothelin-1
97%
Phosphoramidon
30%
pH Value
27%
Big Endothelin
17%
Endothelin-2
17%
Endothelin-3
16%
Thiorphan
16%
Captopril
12%
Complementary DNA
9%
Amino Acid Sequence
8%
Peptide
5%
Protein
3%
Surface
2%