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Cell-Membrane-Localizing Fluorescence Probes for Aminopeptidase N

ACS Sensors, 2023
Aminopeptidase N (APN), a transmembrane ectoenzyme, plays multifunctional roles in cell survival and migration, angiogenesis, blood pressure regulation, and viral uptake. Abnormally high levels of the enzyme can be found in some tumors and injured liver and kidney.
Yun Jae Yang, Mingchong Dai, Kyo Han Ahn
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Betulinic Acid Inhibits Aminopeptidase N Activity

Planta Medica, 1998
The triterpene betulinic acid inhibits the activity of aminopeptidase N (EC 3.4.11.2) in a dose-dependent manner. An IC50 of 7.3 +/- 1.4 microM was determined for betulinic acid. This inhibitory activity is higher than that of bestatin' (IC50 = 16.9 +/- 4.1 microM), a well known inhibitor of this enzyme.
M F, Melzig, H, Bormann
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Human aortic endothelial cell aminopeptidase N

Immunopharmacology, 1996
Aminopeptidase N (AmN) (EC 3.4.11.2) may function in part to degrade peptide hormones (Bausback and Ward, 1986; Kenny et al., 1989; Palmeiri et al., 1985; Ryan et al., 1993). AmN is capable of degrading angiotensin III, Lys-bradykinin, enkephalins and some enkephalin higher homologs (Bausback and Ward, 1986).
A, Papapetropoulos   +6 more
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Enkephalin Metabolism by Microglia Aminopeptidase N (CD13)

Journal of Neurochemistry, 1995
Abstract: Rat microglia in culture showed a high capacity to degrade neuropeptides compared with other glial cells. Leu‐enkephalin was readily hydrolyzed to free tyrosine and Gly‐Gly‐Phe‐Leu. Inhibition experiments and immunostaining revealed that aminopeptidase N (CD13) on the surface of microglia was responsible for enkephalin cleavage. Endopeptidase‐
R, Lucius, J, Sievers, R, Mentlein
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Differential Inhibition of Aminopeptidase A and Aminopeptidase N by New .beta.-Amino Thiols

Journal of Medicinal Chemistry, 1994
Aminopeptidase A (APA) is a highly selective peptidase, which cleaves the N-terminal Glu or Asp residues of biologically active peptides, and has therefore been proposed to be involved in angiotensin II and CCK8 metabolism. Highly potent and selective APA inhibitors are consequently required to study the physiological regulation of these two peptides ...
Chauvel, Eric   +5 more
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Structure and Expression of Aminopeptidase N

1997
Aminopeptidase N (APN) is a very abundant membrane protein in the microvillar membrane of the small intestinal absorptive epithelial cell the enterocyte 1, 2. APN is an ectopeptidase and from its position in the brush border membrane it faces the small intestinal lumen.
Kokholm, K   +3 more
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An aminopeptidase N deficiency in dog small intestine

Research in Veterinary Science, 1997
This study has identified a naturally occurring, specific deficiency of a brush border aminopeptidase N (ApN) in the small intestines of five clinically healthy dogs. ApN activity in mucosal homogenates of dog small intestine was reduced significantly in deficient animals (13.4 (1.1) nmol min-1 mg-1 protein, n = 5, P < 0.002) compared to healthy ...
P W, Pemberton   +3 more
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