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Pagina 1 a partire dal 7243 risultati
Epizootic necrotic enteritis in wild geese.
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Outbreaks of a disease characterized by severe necrotic enteritis occurred among Canada geese (Branta canadensis), lesser snow geese (Anser caerulescens), Ross' geese (A. rossi), and white-fronted geese (A. albifrons) on lakes in Saskatchewan and Manitoba during the autumn of 1983, 1984 and 1985.
A novel alkaline protease from wild edible mushroom Termitomyces albuminosus.
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A protease with a molecular mass of 30 kDa and the N-terminal sequence of GLQTNAPWGLARSS, was isolated from fresh fruiting bodies of the wild edible mushroom Termitomyces albuminosus. The purification protocol included ion exchange chromatography on DEAE-cellulose, Q-Sepharose, SP-Sepharose and
Electrophoretic and spectral characterization of wild type and mutant adenovirus protease.
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The P137L mutation in the adenovirus type 2 protease results in a temperature-sensitive protein-trafficking phenotype expressed during infection but not in vitro. Homology-derived secondary structure prediction placed the mutation within an externally disposed loop. Circular dichroism and urea
Aspartic proteases of Plasmodium vivax are highly conserved in wild isolates.
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The plasmepsins are the aspartic proteases of malaria parasites. Treatment of aspartic protease inhibitor inhibits hemoglobin hydrolysis and blocks the parasite development in vitro suggesting that these proteases might be exploited their potentials as antimalarial drug targets. In this study, we
Pentacycloundecane-based inhibitors of wild-type C-South African HIV-protease.
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In this study, we present the first account of pentacycloundecane (PCU) peptide based HIV-protease inhibitors. The inhibitor exhibiting the highest activity made use of a natural HIV-protease substrate peptide sequence, that is, attached to the cage (PCU-EAIS). This compound showed nanomolar IC(50)
Improved purification protocol for wild-type and mutant human foamy virus proteases.
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Wild-type and an active site mutant (S25T) human foamy virus (HFV) proteases were expressed in fusion with maltose binding protein in Escherichia coli. The mutant enzyme contained a Ser to Thr mutation in the -Asp-Ser-Gly- active site triplet of the enzyme, which forms the "fireman's grip" between
Helvellisin, a novel alkaline protease from the wild ascomycete mushroom Helvella lacunosa.
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A 33.5-kDa serine protease designated as helvellisin was isolated from dried fruiting bodies of the wild ascomycete mushroom Helvella lacunosa. It was purified by using a procedure which entailed ion exchange chromatography on DEAE-cellulose, CM-Sepharose, Q-Sepharose, and FPLC-gel filtration on
Shiga toxin-producing Escherichia coli in wild ungulates.
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Shiga toxin-producing Escherichia coli (STEC) are zoonotic pathogens that live in the gastrointestinal tract of wildlife and cattle without causing disease. In humans, their colonization and infection lead to life-threatening disease. We investigated the occurrence of STEC in wild ungulates (wild
Crystal structure of wild-type human procathepsin K.
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Cathepsin K is a lysosomal cysteine protease belonging to the papain superfamily. It has been implicated as a major mediator of osteoclastic bone resorption. Wild-type human procathepsin K has been crystallized in a glycosylated and a deglycosylated form. The latter crystals diffract better, to 3.2
Carbonylhydrazide-based molecular tongs inhibit wild-type and mutated HIV-1 protease dimerization.
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We have designed and synthesized new molecular tongs based on a rigid naphthalene scaffold and evaluated their antidimer activity on HIV-1 protease (PR). We inserted carbonylhydrazide and oligohydrazide (azatide) fragments into their peptidomimetic arms to reduce hydrophobicity and increase
Cytokine suppression of protease activation in wild-type p53-dependent and p53-independent apoptosis.
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M1 myeloid leukemic cells overexpressing wild-type p53 undergo apoptosis. This apoptosis can be suppressed by some cytokines, protease inhibitors, and antioxidants. We now show that induction of apoptosis by overexpressing wild-type p53 is associated with activation of interleukin-1beta-converting
Flap-site Fragment Restores Back Wild-type Behaviour in Resistant Form of HIV Protease.
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HIV-1 protease (HIV-PR) performs a vital step in the virus life cycle which makes it an excellent target for drug therapy. However, due to the error-prone of HIV reverse transcriptase, mutations in HIV-PR often occur, inducing drug-resistance to inhibitors. Some HIV-PR mutations can make the flaps
Recovery of the wild type atomic flexibility in the HIV-1 protease double mutants.
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The emergence of drug resistant mutations due to the selective pressure exerted by antiretrovirals, including protease inhibitors (PIs), remains a major problem in the treatment of AIDS. During PIs therapy, the occurrence of primary mutations in the wild type HIV-1 protease reduces both the affinity
Isolation and characterization of protease producing bacteria from upper respiratory tract of wild chicken.
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Bacterial samples isolated from the upper respiratory tract of a healthy broiler chicken and a wild chicken suffering from influenza which were collected locally revealed proteolytic activity as detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and zymogram analysis.
Protease and helicase domains are related to the temperature sensitivity of wild-type rubella viruses.
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Wild-type rubella viruses grow well at 39°C (non-temperature sensitivity: non-ts), while vaccine strains do not (temperature sensitivity: ts). Histidine at position 1042 of the p150 region of the KRT vaccine strain was found to be responsible for ts, while wild-type viruses had tyrosine at position
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