Adaptation of and Protocol for the Validation of the Alcohol Use Disorders Identification Test (AUDIT) in the Russian Federation for Use in Primary Healthcare.

AIMS: To adapt and validate the Alcohol Use Disorders Identification Test (AUDIT) for use in the Russian Federation and countries with Russian-speaking populations by. METHODS: Systematic review of past use and validation of the Russian-language AUDIT. Interviews to be conducted with experts to identify problems encountered in the use of existing Russian-language AUDIT versions. A pilot study using a revised translation of the Russian-language AUDIT that incorporates country-specific drinking patterns in the Russian Federation. RESULTS AND CONCLUSIONS: The systematic review identified over 60 different Russian-language AUDIT versions without systematic validation studies. The main difficulties encountered with the use of the AUDIT in the Russian Federation were related to the lack of:A revised version of the Russian-language AUDIT was created based on the pilot studies, and was validated in primary healthcare facilities in all regions in 2019/2020.

A purple-blue chromoprotein from Goniopora tenuidens belongs to the DsRed subfamily of GFP-like proteins.

A number of recently cloned chromoproteins homologous to the green fluorescent protein show a substantial bathochromic shift in absorption spectra. Compared with red fluorescent protein from Discosoma sp. (DsRed), mutants of these so-called far-red proteins exhibit a clear red shift in emission spectra as well. Here we report that a far-red chromoprotein from Goniopora tenuidens (gtCP) contains a chromophore of the same chemical structure as DsRed. Denaturation kinetics of both DsRed and gtCP under acidic conditions indicates that the red form of the chromophore (absorption maximum at 436 nm) converts to the GFP-like form (384 nm) by a one-stage reaction. Upon neutralization, the 436-nm form of gtCP, but not the 384-nm form, renaturates instantly, implying that the former includes a chromophore in its intact state. gtCP represents a single-chain protein and, upon harsh denaturing conditions, shows three major bands in SDS/PAGE, two of which apparently result from hydrolysis of an acylimine C=N bond. Instead of having absorption maxima at 384 nm and 450 nm, which are characteristic for a GFP-like chromophore, fragmented gtCP shows a different spectrum, which presumably corresponds to a 2-keto derivative of imidazolidinone. Mass spectra of the chromophore-containing peptide from gtCP reveal an additional loss of 2 Da relative to the GFP-like chromophore. Tandem mass spectrometry of the chromopeptide shows that an additional bond is dehydrogenated in gtCP at the same position as in DsRed. Altogether, these data suggest that gtCP belongs to the same subfamily as DsRed (in the classification of GFP-like proteins based on the chromophore structure type).