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| description
| - artículu científicu espublizáu en 1989 (ast)
- vědecký článek publikovaný v roce 1989 (cs)
- наукова стаття, опублікована в січні 1989 (uk)
- 1989 թվականի հունվարին հրատարակված գիտական հոդված (hy)
- 1989 թուականի Յունուարին հրատարակուած գիտական յօդուած (hyw)
- vedecký článok (publikovaný 1989/01/02) (sk)
- مقالة علمية (نشرت في 2-1-1989) (ar)
- article scientifique publié en 1989 (fr)
- scientific journal article (en)
- im Januar 1989 veröffentlichter wissenschaftlicher Artikel (de)
- wetenschappelijk artikel (gepubliceerd op 1989/01/02) (nl)
- 1989 ജനുവരി 2 നു പ്രസിദ്ധീകരിച്ച ശാസ്ത്ര ലേഖനം (ml)
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| language of work or name
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| language of work or name
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| cites work
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| cites work
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| author name string
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| author name string
| - M. Eulitz
- M. Schube
- W. Gebhard
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| rdfs:label
| - cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (en)
- cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (nl)
- cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (ast)
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| skos:prefLabel
| - cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (en)
- cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (nl)
- cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (ast)
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| name
| - cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (en)
- cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (nl)
- cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (ast)
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| title
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| title
| - cDNA cloning and complete primary structure of the small, active subunit of human carboxypeptidase N (kininase 1) (en)
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| page(s)
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| page(s)
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| instance of
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| PubMed ID
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| PubMed ID
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| PubMed ID
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| published in
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| published in
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| issue
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| volume
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| DOI
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| DOI
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| DOI
| - 10.1111/J.1432-1033.1989.TB14488.X
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| ResearchGate publication ID
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| ResearchGate publication ID
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| is about
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| is cites work
of | - Human carboxypeptidase E. Isolation and characterization of the cDNA, sequence conservation, expression and processing in vitro
- Induced and spontaneous mutations at Ser202 of carboxypeptidase E. Effect on enzyme expression, activity, and intracellular routing
- The C-terminal region of carboxypeptidase E involved in membrane binding is distinct from the region involved with intracellular routing
- Pathophysiology of the kallikrein-kinin system in mammalian nervous tissue.
- Molecular cloning and partial characterization of rat procarboxypeptidase R and carboxypeptidase N
- Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary
- Interaction between duck hepatitis B virus and a 170-kilodalton cellular protein is mediated through a neutralizing epitope of the pre-S region and occurs during viral infection
- Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity
- The kallikrein-kininogen-kinin system: lessons from the quantification of endogenous kinins.
- A eukaryotic transcriptional repressor with carboxypeptidase activity
- gp180, a protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activity
- Purification and characterization of a developmentally regulated carboxypeptidase from Mucor racemosus
- The silver gene of Drosophila melanogaster encodes multiple carboxypeptidases similar to mammalian prohormone-processing enzymes
- Purification and characterization of arginine carboxypeptidase produced by Porphyromonas gingivalis
- Characterization of Aplysia carboxypeptidase E
- Regulation of carboxypeptidase E. Effect of pH, temperature and Co2+ on kinetic parameters of substrate hydrolysis
- Structure and function of human plasma carboxypeptidase N, the anaphylatoxin inactivator
- Fabry disease: characterisation of the plasma proteome pre- and post-enzyme replacement therapy.
- Glu300 of rat carboxypeptidase E is essential for enzymatic activity but not substrate binding or routing to the regulated secretory pathway
- Dissecting carboxypeptidase E: properties, functions and pathophysiological roles in disease.
- Molecular structure and alternative splicing of the human carboxypeptidase M gene
- Primary structure of carboxypeptidase T: delineation of functionally relevant features in Zn-carboxypeptidase family
- Plasmin alters the activity and quaternary structure of human plasma carboxypeptidase N.
- Enzymic characterization of a novel member of the regulatory B-like carboxypeptidase with transcriptional repression function: stimulation of enzymic activity by its target DNA
- New nucleotide sequence data on the EMBL File Server
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| is cites work
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