Results 161 to 170 of about 25,591 (179)

The Structure and Main Functions of Aminopeptidase N

Current Medicinal Chemistry, 2007
Aminopeptidase N (APN)/CD13 is a type II metalloprotease that belongs to the M1 family of the MA clan, which consists of 967 amino acids with a short N-terminal cytoplasmic domain, a single transmembrane part, and a large cellular ectodomain containing the active site. APN has a molecular weight of 110,000.
Yepeng, Luan, Wenfang, Xu
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Photoaffinity labeling of membrane-bound porcine aminopeptidase n

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
To investigate the possible role of aminopeptidase N (alpha-aminoacyl-peptide hydrolase (microsomal), EC 3.4.11.2) in the transport of amino acids from oligopeptides, the modified amino acids Phe(N3) and Phe(N3, I) and the tetrapeptides Phe(N3) or Phe(N3, I)-L-or-DAla-Gly-Gly have been synthesized.
D, Gratecos, L, Varesi, M, Knibiehler, M, Sémériva   +3 more
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Rabbit intestinal aminopeptidase N. Purification and molecular properties

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1980
The detergent and protease forms of rabbit intestinal aminopeptidase N were purfied for chemical investigations and future specific immunological labeling of the enzyme in situ. The purification of the detergent form required a special technique called 'reverse immunoabsorbant chromatography'.
H, Feracci, S, Maroux
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Human aminopeptidase N is encoded by 20 exons

Mammalian Genome, 1996
Aminopeptidase ...
Lerche, C, Vogel, L K, Shapiro, L H, Norén, Ove, Sjöström, H   +4 more
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Discovery of Bioluminogenic Probes for Aminopeptidase N Imaging

Analytical Chemistry, 2014
To find an approach that can image the hydrolysis activity of aminopeptidase N (APN) both in vitro and in vivo, three bioluminescent probes have been well designed and synthesized herein. All of them can be recognized and hydrolyzed by APN to produce bioluminescence emission in the presence of firefly luciferase.
Jing, Li, Laizhong, Chen, Wenxiao, Wu, Wei, Zhang, Zhao, Ma, Yanna, Cheng, Lupei, Du, Minyong, Li   +7 more
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Aminopeptidase N during the ontogeny of the chick

Differentiation, 2006
Little is known about the production and function of metallopeptidases in embryonic development. One such enzyme, aminopeptidase N (APN), is present in several epithelia, the brain and angiogenic vessels in adults. APN promotes vascular growth and endothelial cell proliferation in physiological and pathological models of angiogenesis.
Gabin, Sihn, Katia, Savary, Annie, Michaud, Marie-Claude, Fournie-Zaluski, Bernard P, Roques, Pierre, Corvol, Jean-Marie, Gasc   +6 more
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Distribution and biosynthesis of aminopeptidase n and dipeptidyl aminopeptidase IV in rat small intestine

Biochimica et Biophysica Acta (BBA) - General Subjects, 1983
The regional, cellular and subcellular distribution patterns of aminopeptidase N and dipeptidyl aminopeptidase IV were examined in rat small intestine. Aminopeptidase N of brush border membrane had maximal activity in the upper and middle intestine, while dipeptidyl aminopeptidase IV had a more uniform distribution profile with relatively high activity
S, Miura, I S, Song, A, Morita, R H, Erickson, Y S, Kim   +4 more
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Aminopeptidase N/CD13 and haematopoietic cells

Haema, 2003
Several cell-surface antigens defined by the cluster of differentiation (CD) nomenclature have been defined as proteins with enzymatic activity. An important example is CD13, aminopeptidase N (APN ; EC 3.4.11.2). It is a zinc-dependent membrane-bound ectopeptidase that cleaves N-terminal neutral amino acids of various peptides.
Gabrilovac, Jelka, Breljak, Davorka, Boranić, Milivoj   +2 more
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Design of Aminopeptidase N Inhibitors as Anti-cancer Agents

Journal of Medicinal Chemistry, 2018
Aminopeptidase N (APN) is an important metalloenzyme. It regulates multivariate cellular functions by different mechanisms such as enzymatic cleavage of peptides. This may play a role in endocytosis and regulate signal transduction. APN, a member of the M1 zinc metallopeptidase family, plays crucial roles in a variety of functions such as migration and
Sk. Abdul Amin, Nilanjan Adhikari, Tarun Jha   +2 more
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Proteolytic Fragmentation of Aminopeptidase N

Biochemical Society Transactions, 1999
Lisa D. Other, Nigel M. Hooper
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