ArticleAntiviral research1997
Bestatin-mediated inhibition of leucine aminopeptidase may hinder HIV infection.
Article in Antiviral research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 71 citations in OpenAlex.
- Article
- Phosphinotripeptidic Inhibitors of Leucylaminopeptidases.International journal of molecular sciences · 2021Article
- Article
- Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of aspartyl aminopeptidase from the apeB gene of Pseudomonas aeruginosa.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Metallo-aminopeptidase inhibitors.Biochimie · 2010Review
- Heterologous expression and purification of Vibrio proteolyticus (Aeromonas proteolytica) aminopeptidase: a rapid protocol.Protein expression and purification · 2009Article
- Experimental evidence for a metallohydrolase mechanism in which the nucleophile is not delivered by a metal ion: EPR spectrokinetic and structural studies of aminopeptidase from Vibrio proteolyticus.The Biochemical journal · 2007Article
- Silver(I) triflate-catalyzed direct synthesis of N-PMP protected alpha-aminopropargylphosphonates from terminal alkynes.Organic letters · 2007Article
- CD13/aminopeptidase N in collagen vascular diseases.Rheumatology international · 2003Article
- Structurally distinct active sites in the copper(II)-substituted aminopeptidases from Aeromonas proteolytica and Escherichia coli.Journal of the American Chemical Society · 2002Article
- Computer-aided design and activity prediction of leucine aminopeptidase inhibitors.Journal of computer-aided molecular design · 2000Article
- A bicarbonate ion as a general base in the mechanism of peptide hydrolysis by dizinc leucine aminopeptidase.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Structure-based approach to alter the substrate specificity of Bacillus subtilis aminopeptidase.PrionArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bestatin, an inhibitor of leucine aminopeptidase (LAPase), significantly decreased HIV infection as reflected by a reduced number of positive immunofluorescent cells, p24 levels, reverse transcriptase activity and the number of proviral copies found in Bestatin-treated cells. Cellular and extracellular LAPase activity in infected cells was higher than the LAPase activity found in uninfected cells. However, cellular and extracellular LAPase activity as well as total protein kinase C activity was lower in Bestatin-treated cells. Conversely, the incubation of human lymphocytic HUT78 cells with LAPase promotes HIV infectivity. The possible role of LAPase in the pathophysiology of HIV was assessed by determining LAPase serum levels in HIV infected patients. LAPase activity levels were three orders of magnitude greater in sera obtained from HIV patients than those detected in sera of uninfected individuals. Although Bestatin reduced HIV infection, a moderate decrease in the reverse transcriptase activity of chronically-infected H9 human T-lymphocytic cells was observed. Based on the higher levels of LAPase present in the serum of HIV patients and on the combined inhibitory effect of Bestatin on LAPase and on protein kinase C activities, we suggest that LAPase may play an important role in the early events of HIV infection such as viral entry.
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