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papillon-lefevre disease/protease
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In vitro and structural evaluation of PL-100 as a potential second-generation HIV-1 protease inhibitor.
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OBJECTIVE
HIV-1 protease inhibitors (PIs) are key components of HIV therapy. PL-100 is a novel lysine sulphonamide that demonstrates potent antiviral activity against multiresistant HIV-1 strains as well as a higher genetic barrier for development of resistance mutations compared with
PL-100, a novel HIV-1 protease inhibitor displaying a high genetic barrier to resistance: an in vitro selection study.
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The development of new HIV inhibitors with distinct resistance profiles is essential in order to combat the development of multi-resistant viral strains. A drug discovery program based on the identification of compounds that are active against drug-resistant viruses has produced PL-100, a novel
In vitro antiviral activity and cross-resistance profile of PL-100, a novel protease inhibitor of human immunodeficiency virus type 1.
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Despite the success of highly active antiretroviral therapy, the current emergence and spread of drug-resistant variants of human immunodeficiency virus (HIV) stress the need for new inhibitors with distinct properties. We designed, produced, and screened a library of compounds based on an original
Potential COVID-19 papain-like protease PL pro inhibitors: repurposing FDA-approved drugs
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Using the crystal structure of SARS-CoV-2 papain-like protease (PLpro) as a template, we developed a pharmacophore model of functional centers of the PLpro inhibitor-binding pocket. With this model, we conducted data mining of the conformational database of FDA-approved drugs.
Signal peptide peptidases: a family of intramembrane-cleaving proteases that cleave type 2 transmembrane proteins.
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Five genes encode the five human signal peptide peptidases (SPPs), which are intramembrane-cleaving aspartyl proteases (aspartyl I-CLiPs). SPPs have been conserved through evolution with family members found in higher eukaryotes, fungi, protozoa, arachea, and plants. SPPs are related to the
Approaches to the design of HIV protease inhibitors with improved resistance profiles.
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OBJECTIVE
This review describes current approaches to HIV protease inhibitor design, with a focus on improving their profile against drug-resistant mutants. Potential explanations for the flat resistance profile of some potent protease inhibitors and discrepancies between the apparent fold change of
[Novel view of the structure of the non-catalytic N-terminal region of ATP-dependent LonA proteases].
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ATP-Dependent Lon proteases are components of the protein quality control system, which maintains a keeping of cellular proteome. Lon family consists of two subfamilies A and B, differing in subunit architecture and intracellular location. The reinterpretation of the domain organization of the
Resistance to newly approved and investigational protease inhibitors.
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OBJECTIVE
The aim of this paper was to review recent literature on the HIV-1 genotypic and phenotypic resistance determinants of therapeutic response to newly approved protease inhibitors and the viral resistance pathways to these and to investigational protease inhibitors.
RESULTS
Published papers
Tipranavir: the first nonpeptidic protease inhibitor for the treatment of protease resistance.
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BACKGROUND
Despite the availability of a growing number of potent antiretroviral agents, efforts to completely suppress viral replication in patients with HIV-1 infection are limited because of the increasing risk of resistance. Tipranavir (TPV) is the first in a class of antiretroviral agents known
Predicting drug resistance of the HIV-1 protease using molecular interaction energy components.
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Drug resistance significantly impairs the efficacy of AIDS therapy. Therefore, precise prediction of resistant viral mutants is particularly useful for developing effective drugs and designing therapeutic regimen. In this study, we applied a structure-based computational approach to predict mutants
Gastric retention and stability of lipidized Bowman-Birk protease inhibitor in mice.
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Bowman-Birk protease inhibitor (BBI) was modified with a reversible lipidizing agent. The palmitoylated product, Pal-BBI, and BBI were iodinated and orally administered to mice using a gavage needle. A prolonged retention of Pal-BBI was found in the stomach. Furthermore, a significant amount of
Enterotoxigenicity of mature 45-kilodalton and processed 35-kilodalton forms of hemagglutinin protease purified from a cholera toxin gene-negative Vibrio cholerae non-O1, non-O139 strain.
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Cholera toxin gene-negative Vibrio cholerae non-O1, non-O139 strain PL-21 is the etiologic agent of cholera-like syndrome. Hemagglutinin protease (HAP) is one of the major secretory proteins of PL-21. The mature 45-kDa and processed 35-kDa forms of HAP were purified in the presence and absence of
Neuroprotective role of (Val(8))GLP-1-Glu-PAL in an in vitro model of Parkinson's disease.
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The growth factor glucagon-like peptide-1 (GLP-1) is neuroprotective in several animal models of neurodegeneration. Here, we analyzed the neuroprotective effects of a novel protease-resistant GLP-1 analogue, (Val(8))GLP-1-Glu-PAL, which has advantages over older analogues, such as improvement of
Antimicrobial activity of a 48-kDa protease (AMP48) from Artocarpus heterophyllus latex.
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OBJECTIVE
Artocarpus heterophyllus (jackfruit) is a latex producing plant. Plant latex is produced from secretory cells and contains many intergradients. It also has been used in folk medicine. This study aimed to purify and characterize the biological activities of a protease from jackfruit
The effect of oral protease administration in the rat remnant kidney model.
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It has been demonstrated that intraperitoneal administration of proteolytic enzymes ameliorates the progression of renal diseases in various animal models. In the present study, we employed the rat remnant kidney model to study the effectiveness of oral administration of proteases. Twenty male
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