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broad/protease

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Broad-spectrum allosteric inhibition of herpesvirus proteases.

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Herpesviruses rely on a homodimeric protease for viral capsid maturation. A small molecule, DD2, previously shown to disrupt dimerization of Kaposi's sarcoma-associated herpesvirus protease (KSHV Pr) by trapping an inactive monomeric conformation and two analogues generated through carboxylate

Structural basis for broad specificity in alpha-lytic protease mutants.

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Binding pocket mutants of alpha-lytic protease (Met 192----Ala and Met 213----Ala) have been constructed recently in an effort to create a protease specific for Met just prior to the scissile bond. Instead, mutation resulted in proteases with extraordinarily broad specificity profiles and high

Characterization of a broad pH range protease of Candida caseinolytica.

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OBJECTIVE The study of a protease secreted by Candida caseinolytica for use in future industrial applications. RESULTS Growth of Candida caseinolytica on a medium containing milk induced a rapid production of an extracellular enzyme able to hydrolyse casein. The crude extract was applied to both

Quantifying missing (phospho)proteome regions with the broad-specificity protease subtilisin.

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Despite huge efforts to map the human proteome using mass spectrometry the overall sequence coverage achieved to date is still below 50%. Reasons for missing areas of the proteome comprise protease-resistant domains including the lack/excess of enzymatic cleavage sites, nonunique peptide sequences,

Novel broad-spectrum activity-based probes to profile malarial cysteine proteases.

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Clan CA cysteine proteases, also known as papain-like proteases, play important roles throughout the malaria parasite life cycle and are therefore potential drug targets to treat this disease and prevent its transmission. In order to study the biological function of these proteases and to chemically

Identification of broad-based HIV-1 protease inhibitors from combinatorial libraries.

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Clinically approved inhibitors of the HIV-1 protease function via a competitive mechanism. A particular vulnerability of competitive inhibitors is their sensitivity to increases in substrate concentration, as may occur during virion assembly, budding and processing into a mature infectious viral

The Arabidopsis AtSTE24 is a CAAX protease with broad substrate specificity.

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Following prenylation, the proteins are subject to two prenyl-dependent modifications at their C-terminal end, which are required for their subcellular targeting. First, the three C-terminal residues of the CAAX box prenylation signaling motif are removed, which is followed by methylation of the

Broad Susceptibility of Nucleolar Proteins and Autoantigens to Complement C1 Protease Degradation.

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Anti-nuclear autoantibodies, which frequently target the nucleoli, are pathogenic hallmarks of systemic lupus erythematosus (SLE). Although the causes of these Abs remain broad and ill-defined, a genetic deficiency in C1 complex (C1qC1r2C1s2) or C4 is able to induce these Abs. Considering a recent

A new broad-spectrum protease inhibitor from the entomopathogenic bacterium Photorhabdus luminescens.

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A new protease inhibitor was purified to apparent homogeneity from a culture medium of Photorhabdus luminescens by ammonium sulfate precipitation and preparative isoelectric focusing followed by affinity chromatography. Ph. luminescens, a bacterium symbiotically associated with the insect-parasitic

A fluorescent oligopeptide energy transfer assay with broad applications for neutral proteases.

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A fluorescent peptide substrate to explore the protease specificity for the amino acid regions C- and N-terminal to the cleavage site has been designed. Intramolecular quenching of indole fluorescence by an N-terminal dansyl group separated by six amino acid residues forms the basis of this assay.

Correction: Novel broad-spectrum activity-based probes to profile malarial cysteine proteases.

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[This corrects the article DOI: 10.1371/journal.pone.0227341.].

Protease activation of alpha2-macroglobulin modulates a chaperone-like action with broad specificity.

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Alpha2-macroglobulin (alpha2M) is a major human blood glycoprotein best known for its ability to inhibit a broad spectrum of proteases by a unique trapping method. This action induces an "activated" conformation of alpha2M with an exposed binding site for the low-density lipoprotein receptor,

In silico characterization of broad range proteases produced by Serratia marcescens EGD-HP20.

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In the present study, Serratia marcescens EGD-HP20 strain was demonstrated to utilize poultry waste comprising of both white non-melanized and dark/brown melanized poultry feathers. The potential of the isolate to hydrolyze diverse keratinous wastes was further corroborated by comparative genomics

ZapA, a possible virulence factor from Proteus mirabilis exhibits broad protease substrate specificity.

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The opportunistic bacterium Proteus mirabilis secretes a metalloprotease, ZapA, considered to be one of its virulence factors due to its IgA-degrading activity. However, the substrate specificity of this enzyme has not yet been fully characterized. In the present study we used fluorescent peptides

Broad-spectrum inhibitors against 3C-like proteases of feline coronaviruses and feline caliciviruses.

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Feline infectious peritonitis and virulent, systemic calicivirus infection are caused by certain types of feline coronaviruses (FCoVs) and feline caliciviruses (FCVs), respectively, and are important infectious diseases with high fatality rates in members of the Felidae family. While FCoV and FCV
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