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A retrospective controlled study of thiol disulfide homeostasis as a novel marker in Crimean Congo hemorrhagic fever.

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OBJECTIVE Crimean Congo hemorrhagic fever (CCHF) is the second most common hemorrhagic fever worldwide. This study aimed to evaluate the oxidant-antioxidant balance of patients with CCHF by detecting dynamic thiol disulfide homeostasis (TDH), which is a novel oxidative stress marker, and other

Modulation of the structure, catalytic activity, and fidelity of African swine fever virus DNA polymerase X by a reversible disulfide switch.

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African swine fever virus polymerase X (pol X) is the smallest DNA polymerase known (174 amino acids), and its tertiary structure resembles the C-terminal half of prototypical X-family pol beta, which includes a catalytic dNTP-binding site (palm domain) and a finger domain. This structural

Can the Thiol/Disulfide Imbalance Be a Predictor of Colchicine Resistance in Familial Mediterranean Fever?

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Familial Mediterranean fever (FMF) is a chronic autoinflammatory condition characterized by fever attacks and recurrent polyserositis. Subclinical inflammation that persists during attack-free periods can result in oxidative stress (OS) damage. Thiol groups bind to reactive oxygen radicals and

Abnormal disulfide-linked oligomerization results in ER retention and altered signaling by TNFR1 mutants in TNFR1-associated periodic fever syndrome (TRAPS).

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Tumor necrosis factor (TNF) receptor-associated periodic syndrome (TRAPS) is an autosomal dominant systemic autoinflammatory disease associated with heterozygous mutations in TNF receptor 1 (TNFR1). Here we examined the structural and functional alterations caused by 9 distinct TRAPS-associated

Mode of inactivation of arenaviruses by disulfide-based compounds.

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Several disulfide-based compounds, including intermolecular aromatic disulfides of the type Ph-S-S-Ph and dithianes with the sulfur atoms tethered in a ring structure, have shown effective inhibitory activity against the arenaviruses Junin (JUNV), agent of Argentine hemorrhagic fever, and Tacaribe

A unique DNA-binding mode of African swine fever virus AP endonuclease.

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African swine fever virus (ASFV) is highly contagious and can cause lethal disease in pigs. ASFV is primarily replicated in the cytoplasm of pig macrophages, which is oxidative and caused constant damage to ASFV genome. ASFV AP endonuclease (AsfvAP) catalyzes DNA cleavage reaction at the

[Role of nonspecific factors in the therapeutic action of general hyperthermia in oncologic diseases].

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A study was made of the indices of hemodynamics, the immune status and thiol-disulfide system of the blood of cancer patients subjected to artificial total hyperthermia-hyperglycemia. The authors revealed the phase nature of the body response to total hyperthermia resulting in stimulation of the

RNase of classical swine fever virus: biochemical characterization and inhibition by virus-neutralizing monoclonal antibodies.

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The structural glycoprotein E0 of classical swine fever virus (CSFV) possesses an intrinsic RNase activity. Here we present the first comprehensive biochemical characterization of E0, using a recombinant glycoprotein expressed in insect cells. We were able to show that the presence of neither

Restoration of glycoprotein Erns dimerization via pseudoreversion partially restores virulence of classical swine fever virus.

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The classical swine fever virus (CSFV) represents one of the most important pathogens of swine. The CSFV glycoprotein Erns is an essential structural protein and an important virulence factor. The latter is dependent on the RNase activity of this envelope protein and, most likely, its secretion from

Analysis of disulfides present in the membrane proteins of the West Nile flavivirus.

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Recently the primary structure of the structural proteins of the flaviviruses West Nile (WN) virus (Castle et al., 1985; Wengler et al., 1985) and yellow fever (YF) virus (Rice et al., 1985) have been determined. As a first step in a further characterization of the organization of the structural

The African swine fever virus prenyltransferase is an integral membrane trans-geranylgeranyl-diphosphate synthase.

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In a previous study, it was shown that the protein encoded by the gene B318L of African swine fever virus (ASFV) is a trans-prenyltransferase that catalyzes in vitro the condensation of farnesyl diphosphate and isopentenyl diphosphate to synthesize geranylgeranyl diphosphate and longer chain prenyl

A targeting theranostics nanomedicine as an alternative approach for hyperthermia perfusion.

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Real-time monitoring drug-release is often regarded crucial in theranostics nanomedicine design, since it provides precise establishment of spatio-temporal activation of the drug-release in vitro and in vivo. A symmetrical self-immolative drug-dye conjugation (DDC) prodrug is developed in this study

Intriguing olfactory proteins from the yellow fever mosquito, Aedes aegypti.

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Four antennae-specific proteins (AaegOBP1, AaegOBP2, AaegOBP3, and AaegASP1) were isolated from the yellow fever mosquito, Aedes aegypti and their full-length cDNAs were cloned. RT-PCR indicated that they are expressed in female and, to a lesser extent, in male antennae, but not in control tissues

Virus-host interactions in African swine fever: the attachment to cellular receptors.

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Biochemical and morphological techniques have shown that African swine fever virus (ASFV) enters susceptible cells by a mechanism of receptor-mediated endocytosis. The virus binds to a specific, saturable site in the cell and this interaction is required for a productive infection. A structural ASFV

African swine fever virus pB119L protein is a flavin adenine dinucleotide-linked sulfhydryl oxidase.

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Protein pB119L of African swine fever virus belongs to the Erv1p/Alrp family of sulfhydryl oxidases and has been described as a late nonstructural protein required for correct virus assembly. To further our knowledge of the function of protein pB119L during the virus life cycle, we have investigated

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