Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules.
about
Identification of human aminopeptidase O, a novel metalloprotease with structural similarity to aminopeptidase B and leukotriene A4 hydrolasePurification, characterization, and cloning of a cytosolic aspartyl aminopeptidaseMolecular cloning and expression of rat liver aminopeptidase BGlucose transporter Glut3 is targeted to secretory vesicles in neurons and PC12 cellsMolecular characterization of a puromycin-insensitive leucyl-specific aminopeptidase, PILS-APAminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modellingCharacterization of a novel zinc-containing, lysine-specific aminopeptidase from the hyperthermophilic archaeon Pyrococcus furiosusAminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase.Aminopeptidase A inhibitors as potential central antihypertensive agentsInactivation of Caenorhabditis elegans aminopeptidase DNPP-1 restores endocytic sorting and recycling in tat-1 mutantsCathepsin L plays a major role in cholecystokinin production in mouse brain cortex and in pituitary AtT-20 cells: protease gene knockout and inhibitor studies.Ultrastructural localization and distribution of Nardilysin in mammalian male germ cells.Puromycin insensitive leucyl-specific aminopeptidase (PILSAP) is involved in the activation of endothelial integrins.Two novel metallopeptidases with a specificity for basic residues: functional properties, structure and cellular distribution.Aminopeptidase B is structurally related to leukotriene-A4 hydrolase but is not a bifunctional enzyme with epoxide hydrolase activity.Leukotriene A4 hydrolase: a critical role of glutamic acid-296 for the binding of bestatin.Cathepsin L expression is directed to secretory vesicles for enkephalin neuropeptide biosynthesis and secretion.Secretory vesicle aminopeptidase B related to neuropeptide processing: molecular identification and subcellular localization to enkephalin- and NPY-containing chromaffin granules.Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (NC-IUBMB). Enzyme Nomenclature. Recommendations 1992. Supplement 4: corrections and additions (1997).
P2860
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P2860
Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules.
description
1995 nî lūn-bûn
@nan
1995 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@ast
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@en
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@nl
type
label
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@ast
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@en
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@nl
prefLabel
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@ast
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@en
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@nl
P2093
P1476
Aminopeptidase-B in the rat te ...... n in the seminiferous tubules.
@en
P2093
Créminon C
Pierotti AR
Segrétain D
P304
P356
10.1016/0303-7207(95)03529-G
P577
1995-04-01T00:00:00Z