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dental caries/protease

Odkaz sa uloží do schránky
Strana 1 od 914 výsledky

Human immunodeficiency virus protease ligand specificity conferred by residues outside of the active site cavity.

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To gain greater understanding of the structural basis of human immunodeficiency virus (HIV) protease ligand specificity, we have crystallized and determined the structures of the HIV-1 protease (Val32Ile, Ile47Val, Val82Ile) triple mutant and simian immunodeficiency virus (SIV) protease in complex
Trypsin (Try), plasma kallikrein (KK) and plasmin activities together with coagulation factor XII (F XII, Hageman factor), high-molecular-weight kininogen (HMWK), plasma prekallikrein (PKK), alpha 2-macroglobulin (alpha 2-M), C1 inhibitor (C1Inh), and functional plasma kallikrein inhibition (KKI)
BACKGROUND The purpose of this study was to evaluate the loss of heterozygosity (LOH) in chromosomes 17p13 (p53 gene) and in 18q21 (mammary serine protease inhibitor [maspin] gene), and the expression of both genes in tissues, in patients with oral cavity squamous cell carcinoma

Cavities tell more than sequences: exploring functional relationships of proteases via binding pockets.

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Computational approaches play an increasingly important role for the analysis and prediction of selectivity profiles. As most of the successfully administered small molecule drugs bind in depressions on the surface of proteins, physicochemical properties of the pocket-exposed amino acids play a

Induction of a selective and persistent extravasation of neutrophils into the peritoneal cavity by tryptase mouse mast cell protease 6.

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Recombinant mouse mast cell protease 6 (mMCP-6) was generated to study the role of this tryptase in inflammatory reactions. Seven to forty-eight hours after the i.p. injection of recombinant mMCP-6 into BALB/c, mast cell-deficient WCB6F1-Sl/Sl(d), C5-deficient, or mMCP-5-null mice, the number of

Engineering an anion-binding cavity in antichymotrypsin modulates the "spring-loaded" serpin-protease interaction.

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Expressed in a kinetically trapped folding state, a serpin couples the thermodynamic driving force of a massive beta-sheet rearrangement to the inhibition of a target protease. Hence, the serpin-protease interaction is the premier example of a "spring-loaded" protein-protein interaction. Amino acid

The effect of cavity-filling mutations on the thermostability of Bacillus stearothermophilus neutral protease.

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Cavities in the hydrophobic core of the neutral protease of Bacillus stearothermophilus were analyzed using a three-dimensional model that was inferred from the crystal structure of thermolysin, the highly homologous neutral protease of B. thermoproteolyticus (85% sequence identity). Site-directed

Identification of a loop outside the active site cavity of the human immunodeficiency virus proteases which confers inhibitor specificity.

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We have investigated the inhibitor specificity for the proteases of the human immunodeficiency viruses, types 1 and 2. Using a series of related inhibitors, the P1' side chain was confirmed to play a significant role in determining both the absolute and relative affinity for the enzymes. To further

Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex.

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Human herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) are responsible for herpes labialis (cold sores) and genital herpes, respectively. They encode a serine protease that is required for viral replication, and represent a viable target for therapeutic intervention. Here, we report the

Crystal structures of a multidrug-resistant human immunodeficiency virus type 1 protease reveal an expanded active-site cavity.

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The goal of this study was to use X-ray crystallography to investigate the structural basis of resistance to human immunodeficiency virus type 1 (HIV-1) protease inhibitors. We overexpressed, purified, and crystallized a multidrug-resistant (MDR) HIV-1 protease enzyme derived from a patient failing

Identification of human salivary protease activity toward mucin: differences with caries.

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A protease activity directed toward high molecular weight salivary mucus glycoprotein was identified in the secretion of human submandibular salivary gland. The protease exhibited maximum activity at pH 7.0-7.4, and following ammonium sulfate fractionation yielded an active enzyme at 60% saturation

Control of mucin molecular forms expression by salivary protease: differences with caries.

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1. A protease activity capable of degradation of the high mol. wt salivary mucus glycoprotein to a low mol. wt glycoprotein form was identified in human submandibular gland secretion. 2. The protease exhibited optimum activity at pH 7.0-7.4, and gave on SDS-PAGE under reducing conditions two major

Influence of protease inhibitors on the degradation of sound, sclerotic and caries-affected demineralized dentin.

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The aim of this study was to evaluate influence of protease inhibitors on degradation of sound, sclerotic and caries-affected dentin. Thirty-nine molars were used, thirteen for each dentin condition. Three slices were obtained from each tooth, each one immersed in the following different solutions

Structure of rhomboid protease in complex with β-lactam inhibitors defines the S2' cavity.

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Rhomboids are evolutionarily conserved serine proteases that cleave transmembrane proteins within the membrane. The increasing number of known rhomboid functions in prokaryotes and eukaryotes makes them attractive drug targets. Here, we describe structures of the Escherichia coli rhomboid GlpG in

[Protease activity of microflora in the oral cavity of patients with periodontitis].

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Microbial spectrum and non-specific as well as specific IgA1 protease activity of isolated microorganisms were investigated in gingival liquid of patients with periodontitis. Microorganisms from the gingival liqud of these patients belonged to conditional-pathogenic obligate and facultatively
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