about
Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidaseCharacterization of the Plasmodium falciparum M17 leucyl aminopeptidase. A protease involved in amino acid regulation with potential for antimalarial drug developmentInhibition of APN/CD13 leads to suppressed progressive potential in ovarian carcinoma cells.Blocking macrophage leukotriene b4 prevents endothelial injury and reverses pulmonary hypertension.Development of Synthetic Aminopeptidase N/CD13 Inhibitors to Overcome Cancer Metastasis and Angiogenesis.Gelatin degradation assay reveals MMP-9 inhibitors and function of O-glycosylated domain.Aminopeptidase N (CD13) as a target for cancer chemotherapy.Activity of hydrolytic enzymes in tumour cells is a determinant for anti-tumour efficacy of the melphalan containing prodrug J1.Chemical target validation studies of aminopeptidase in malaria parasites using alpha-aminoalkylphosphonate and phosphonopeptide inhibitorsRNA interference targeting leucine aminopeptidase blocks hatching of Schistosoma mansoni eggs.The Activity of a Hexameric M17 Metallo-Aminopeptidase Is Associated With Survival of Mycobacterium tuberculosis.Positioning of aminopeptidase inhibitors in next generation cancer therapy.Resveratrol, a red wine polyphenol, suppresses pancreatic cancer by inhibiting leukotriene A₄hydrolase.Generation of AMBER force field parameters for zinc centres of M1 and M17 family aminopeptidases.CD13/Aminopeptidase N overexpression by basic fibroblast growth factor mediates enhanced invasiveness of 1F6 human melanoma cells.Biotransformation of beta-endorphin and possible therapeutic implications.Expression and function of aminopeptidase N/CD13 produced by fibroblast-like synoviocytes in rheumatoid arthritis: role of CD13 in chemotaxis of cytokine-activated T cells independent of enzymatic activityMolecular cloning and characterization of a M17 leucine aminopeptidase of Cryptosporidium parvum.Biochemical characteristics and modulation by external and internal factors of aminopeptidase-N activity in the hepatopancreas of a euryhaline burrowing crab.Aminopeptidase N (CD13) regulates tumor necrosis factor-alpha-induced apoptosis in human neutrophils.Combinatorial multicomponent access to natural-products-inspired peptidomimetics: discovery of selective inhibitors of microbial metallo-aminopeptidases.Bestatin, an inhibitor of aminopeptidases, provides a chemical genetics approach to dissect jasmonate signaling in Arabidopsis.QSAR studies of aminopeptidase N/CD13 (APN) inhibitors with the scaffold 3-phenylpropane-1,2-diamine and molecular docking
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մարտին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Bestatin as an experimental tool in mammals.
@ast
Bestatin as an experimental tool in mammals.
@en
Bestatin as an experimental tool in mammals.
@nl
type
label
Bestatin as an experimental tool in mammals.
@ast
Bestatin as an experimental tool in mammals.
@en
Bestatin as an experimental tool in mammals.
@nl
prefLabel
Bestatin as an experimental tool in mammals.
@ast
Bestatin as an experimental tool in mammals.
@en
Bestatin as an experimental tool in mammals.
@nl
P356
P1476
Bestatin as an experimental tool in mammals.
@en
P2093
P356
10.2174/1389200013338748
P407
P577
2001-03-01T00:00:00Z