Publications by authors named "Andrianova A"

Notre recherche visait à mettre en lumière les pratiques bientraitantes des préposées aux bénéficiaires en milieux d'hébergement pour aînés au Québec. L'objet de l'article est de faire ressortir la dichotomie entre les définitions de la bientraitance et son opérationnalisation. Dans la première partie, la notion de bientraitance dans le cadre de deux politiques gouvernementales québécoises est présentée.

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The heterogeneous and recalcitrant structure of lignin hinders its practical application. Here, we describe how new approaches to lignin characterization can reveal structural details that could ultimately lead to its more efficient utilization. A suite of methods, which enabled mass balance closure, the evaluation of structural features, and an accurate molecular weight (MW) determination, were employed and revealed unexpected structural features of the five alkali lignin fractions obtained with preparative size-exclusion chromatography (SEC).

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ATP-dependent Lon proteases are key participants in the quality control system that supports the homeostasis of the cellular proteome. Based on their unique structural and biochemical properties, Lon proteases have been assigned in the MEROPS database to three subfamilies (A, B, and C). All Lons are single-chain, multidomain proteins containing an ATPase and protease domains, with different additional elements present in each subfamily.

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The concept of 'bientraitance'(good treatment) of older adults was introduced in Quebec policy a few years prior to the pandemic, and its significance from the perspectives of those directly involved in care remains underexplored. Centring these perspectives, this article presents findings from a study of the meanings, practices and conditions of good treatment. Data was collected at three different residential care settings through world cafés with residents, staff, management, volunteers and family members ( = 61) and through interviews with care aides ( = 13).

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The objective of the study was to investigate alkali lignin polymerization/depolymerization pathways in subcritical water (SW) without additives. Following a SW treatment at 200, 250, 275 and 300 °C, the products were subjected to a comprehensive suite of analyses addressing the product speciation and molecular weight (MW) distribution. The MW reduction (1.

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ATP-dependent Lon protease of (Lon), which belongs to the superfamily of AAA proteins, is a key component of the cellular proteome quality control system. It is responsible for the cleavage of mutant, damaged, and short-lived regulatory proteins that are potentially dangerous for the cell. Lon functions as a homooligomer whose subunits contain a central characteristic AAA module, a C-terminal protease domain, and an N-terminal non-catalytic region composed of the actual N-terminal domain and the inserted α-helical domain.

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Objective Identify the diagnostic markers of the severe MV changes in patients with ischemic mitral regurgitation (IMR) and suggest a modification of the echocardiography (EchoCG) algorithm.Materials and Methods A two-stage examination of 65 patients with mild (n=22), moderate (n=22), and severe (n=21) IMR was performed using two-dimensional (2D) transthoracic EchoCG with dopplerography, 2D and three-dimensional (3D) transesophageal EchoCG (TEE). 4D MV-Assessment in off-line mode was made in TomTec Imaging Systems GmbH, Germany.

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Rationale: Lignin occurs in a broad range of forms, e.g., native as the main support for plant walls, and processed, for which its structure depends on the nature of the industrial isolation method, such as in paper production or in biorefineries.

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Le vieillissement de la population invite à étudier les résidences privées pour aînés, notamment sous l'angle du lien social. Après leur emménagement en résidence, plusieurs aînés veulent continuer de participer activement à la société. Cette recherche qualitative exploratoire a pour objectif de mieux comprendre les perceptions et les expériences d'aînés vivant dans une résidence privée par rapport à leur participation sociale, sur le plan de leurs relations interpersonnelles et de leurs activités de loisirs.

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Multiple chronic conditions (MCCs) such as diabetes, hypertension, heart disease, arthritis, asthma, and common respiratory problems are prevalent in over one-fourth of Americans, and separate drugs are prescribed to manage each of the diseases. The nutritive crop seeds loaded with multiple drugs could be a cheap and sustainable alternative to drugs produced by pharmaceutical companies. Our long-term goal is to produce chickpea seeds containing comparable dosages of multiple drugs regularly prescribed for managing MCC.

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Molecular beam (MB) time-of-flight mass spectrometry has been used to investigate thermal decomposition of triolein, to reveal the mechanisms of low temperature soot/coke formation characteristic for triglycerides (TGs). Mass detected pyrolysis products were observed at incremented temperatures using both VUV single photon ionization (general product detection) and REMPI based selective detection of aromatic products. To augment the simple mass characterizations, we have employed stoichiometric considerations; we have supplemented the analysis further by using the detailed information available from product analysis of batch reactor TG cracking.

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LonA proteases and ClpB chaperones are key components of the protein quality control system in bacterial cells. LonA proteases form a unique family of ATPases associated with diverse cellular activities (AAA ) proteins due to the presence of an unusual N-terminal region comprised of two domains: a β-structured N domain and an α-helical domain, including the coiled-coil fragment, which is referred to as HI(CC). The arrangement of helices in the HI(CC) domain is reminiscent of the structure of the H1 domain of the first AAA module of ClpB chaperones.

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Triacyl-, diacyl- and monoacylglycerols (TAGs, DAGs, MAGs) along with monocarboxylic acids (MCAs) are intermediate products in many triacylglycerol oil-to-biofuel conversion pathways. Accumulation of these compounds leads to poor biofuel characteristics and may result in fuel system damage. We developed a method for simultaneous identification and quantification of a wide range of MCAs (C-C), MAGs, DAGs, and TAGs.

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The capability to characterize lignin, lignocellulose, and their degradation products is essential for the development of new renewable feedstocks. Electrospray ionization high-resolution time-of-flight mass spectrometry (ESI-HR TOF-MS) method was developed expanding the lignomics toolkit while targeting the simultaneous detection of low and high molecular weight (MW) lignin species. The effect of a broad range of electrolytes and various ionization conditions on ion formation and ionization effectiveness was studied using a suite of mono-, di-, and triarene lignin model compounds as well as kraft alkali lignin.

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Characterization of lignin and its degradation products, more specifically determination of their molecular weight (MW) distribution, is essential for assessment and applications of these potentially renewable phenolics. Several representative gel filtration and gel permeation systems were evaluated in this work focusing on understanding of undesired secondary non-SEC interactions while utilizing four sets of commercially available polymeric standards as well as low-MW lignin model compounds including diarene standards synthesized in-house. The gel permeation column with a nonpolar highly cross-linked porous polystyrene/divinylbenzene-based stationary phase provided the most effective separation by MW for both low and high MW model compounds.

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Unlike previous lignin biodegradation studies, white rot fungi were used to produce functional biopolymers from Kraft lignin. Lignin-based polymers (hydrogel precursors) partially soluble in both aqueous and organic solvents were produced employing a relatively fast (6 days) enzymation of Kraft lignin with basidiomycetes, primarily Coriolus versicolor, pre-grown on kenaf/lignin agar followed by either vacuum evaporation or acid precipitation. After drying followed by a treatment with alkaline water, this intermediate polymer became a pH-sensitive anionic hydrogel insoluble in either aqueous or organic solvents.

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Multidomain ATP-dependent Lon protease of (Ec-Lon) is one of the key enzymes of the quality control system of the cellular proteome. A recombinant form of Ec-Lon with deletion of the inserted characteristic α-helical HI(CC) domain (Lon-dHI(CC)) has been prepared and investigated to understand the role of this domain. A comparative study of the ATPase, proteolytic, and peptidase activities of the intact Lon protease and Lon-dHI(CC) has been carried out.

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ATP-dependent Lon protease of E. coli (Ec-Lon) is a key enzyme of the quality control system of the cell proteome. Ec-Lon subunit comprises N-terminal non-catalytic region, ATPase module and proteolytic domain (serine-lysine endopeptidase).

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ATP-Dependent protease LonA from E. coli (Ec-Lon), belonging to the superfamily of AAA+ proteins, is a key member of the protein quality control system in bacterial cells. Ec-Lon functions as homohexamer and degrades abnormal and defective polypeptides as well as a number of regulatory proteins by the processive mechanism.

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Homooligomeric ATP-dependent LonA proteases are bifunctional enzymes belonging to the superfamily of AAA+ proteins. Their subunits are formed by five successively connected domains: N-terminal (N), α-helical (HI(CC)), nucleotide binding (NB), the second α-helical (H) and proteolytic (P). The presence of the inserted HI(CC) domain defines the uniqueness of LonA proteases among AAA+ proteins.

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We carried out chymotryptic digestion of multimeric ATP-dependent Lon protease from Escherichia coli. Four regions sensitive to proteolytic digestion were located in the enzyme and several fragments corresponding to the individual structural domains of the enzyme or their combinations were isolated. It was shown that (i) unlike the known AAA(+) proteins, the ATPase fragment (A) of Lon has no ATPase activity in spite of its ability to bind nucleotides, and it is monomeric in solution regardless of the presence of any effectors; (ii) the monomeric proteolytic domain (P) does not display proteolytic activity; (iii) in contrast to the inactive counterparts, the AP fragment is an oligomer and exhibits both the ATPase and proteolytic activities.

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Deletion of the transmembrane domain (TM-domain) of Archaeoglobus flggidus LonB protease (AfLon) was shown to result in uncontrollable activation of the enzyme proteolytic site and in vivo autolysis yielding a stable and functionally inactive fragment consisting of both alpha-helical and proteolytic domains (alphaP). The deltaTM-AfLonTM-S590A enzyme form, obtained by site-directed mutagenesis of the catalytic Ser residue, is capable of recombination with the alphaP fragment. The mixed oligomers were shown to be proteolytically active, which indicates a crucial role of subunit interactions in the activation of the AfLon proteolytic site.

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