Experiences in the introduction of bedaquiline pretomanid linezolid for drug-resistant tuberculosis in Kyrgyzstan.

Settings: In Kyrgyzstan, drug-resistant tuberculosis poses a significant challenge. Recognizing the potential of the BPaL regimen, the World Health Organization recommended its use for selected drug-resistant TB cases under operational research conditions in 2020.

Objective: This report presents experiences and results from the BPaL operational research under the LIFT-TB project in Kyrgyzstan.

[EFFICIENT TREATMENT OF CHRONIC RESPIRATORY INSUFFICIENCY IN PATIENTS WITH KYPHOSCOLIOSIS].

We report efficient treatment of chronic respiratory insufficiency in patients with congenital kyphoscoliosis by non-invasive auxiliary ventilation and low-flow oxygen therapy. It proved possible to effectively control severe chronic respiratory insufficiency under conditions of a pulmonological ward without application of means and measures of intensive therapy.

[Immunohistochemical study of adhesive molecules Her-2/neu in nonendometrial carcinoma of corpus uteri].

46 cases of nonendometrial carcinoma of the corpus uteri have been studied. The expressions of E-cadherin, alpha and beta-catenins were detected by immunohistochemical method. The high level of studied markers expression was founded out in clear cell carcinoma, whereas the less expression was detected in the corpus uteri of patients with serous, papillary, undifferentiated and mixed cancer.

Sulfhydryl reactivity demonstrates different conformational states for arrestin, arrestin activated by a synthetic phosphopeptide, and constitutively active arrestin.

The sulfhydryl groups of the three cysteines in bovine arrestin react with DTNB very slowly (over a period of several hours). In the presence of the synthetic phosphopeptide comprising the fully phosphorylated carboxyl-terminal 19 amino acids of bovine rhodopsin, the reactivity of one of the sulfhydryls was enhanced while that of another was greatly reduced. Since this synthetic peptide was shown to activate arrestin with respect to its binding to unphosphorylated, light-activated rhodopsin, the reactivity of the sulfhydryl groups of a constitutively active R175Q arrestin mutant was examined.

The sequence of arrestins from rod and cone photoreceptors in the frogs Rana catesbeiana and Rana pipiens. Localization of gene transcripts by reverse-transcription polymerase chain reaction on isolated photoreceptors.

Members of the arrestin protein family are known to participate in the inactivation of rhodopsin and other heptahelical receptors. Arrestins bind to the activated and phosphorylated state of these receptors, consequently blocking the ability of the receptors to activate the guanine-nucleotide-binding protein (G protein). We have determined the sequences of four retinal arrestins from two species of frog, Rana catesbeiana and Rana pipiens.

Synthetic phosphopeptide from rhodopsin sequence induces retinal arrestin binding to photoactivated unphosphorylated rhodopsin.

A synthetic heptaphosphopeptide comprising the fully phosphorylated carboxyl terminal phosphorylation region of bovine rhodopsin, residues 330-348, was found to induce a conformational change in bovine arrestin. This caused an alteration of the pattern of limited proteolysis of arrestin similar to that induced by binding phosphorylated rhodopsin or heparin. Unlike heparin, the phosphopeptide also induced light-activated binding of arrestin to both unphosphorylated rhodopsin in disk membranes as well as to endoproteinase Asp-N-treated rhodopsin (des 330-348).

1H-15N-NMR studies of bacteriorhodopsin Halobacterium halobium. Conformational dynamics of the four-helical bundle.

Series of uniformly and selectively 15N-labeled bacteriorhodopsins of Halobacterium halobium (strain ET 1001) were obtained and a 1H-15N-NMR study was performed in methanol/chloroform (1:1) and 0.1 M NH4CHOO, medium which mimics that in the membrane in vivo. Less than half of the cross-peaks expected from the amino acid sequence of uniformly 15N-labeled bacteriorhodopsin were observed, using heteronuclear 1H-15N coherence spectroscopy.

[Spatial structure of (1-36)bacterioopsin solubilized in a methanol-chloroform mixture with sodium dodecylsulfate micelles].

Spatial structures of proteolytic segment A (sA) of bacterioopsin of Halobacterium halobium (residues 1-36) solubilized in the mixture of methanol-chloroform (1:1), 0.1 M LiClO4 or in perdeuteriated sodium dodecyl sulfate (SDS) micelles, were determined by 2D 1H-NMR techniques. Most of the resonances in 1H-NMR spectra of fragment A were assigned using DQF-COSY, TOCSY and NOESY spectra.

Sequence-specific resonance assignment and secondary structure of (1-71) bacterioopsin.

The conformation of chymotryptic fragment C2 of bacteriohodopsin (residues 1-71) was studied by 2D 1H NMR. The fragment was solubilized in a mixture of chloroform/methanol (1:1), 0.1 M LiClO4.

Sequence-specific 1H-NMR assignment and conformation of proteolytic fragment 163-231 of bacterioopsin.

Proteolytic fragment 163-231 of bacterioopsin was isolated from Halobacterium halobium purple membrane treated with NaBH4 and papain under nondenaturing conditions. Two-dimensional 1H-NMR spectra of (163-231)-bacterioopsin solubilized in chloroform/methanol (1:1), 0.1 M LiClO4 indicated the existence of one predominant conformation.