Publications by authors named "G D S Csizmadia"

Human activity recognition (HAR) using machine learning (ML) methods has been a continuously developed method for collecting and analyzing large amounts of human behavioral data using special wearable sensors in the past decade. Our main goal was to find a reliable method that could automatically detect various playful and daily routine activities in children. We defined 40 activities for ML recognition, and we collected activity motion data by means of wearable smartwatches with a special SensKid software.

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Protein and lipid membrane interactions play fundamental roles in a large number of cellular processes (e.g. signalling, vesicle trafficking, or viral invasion).

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Automated monitoring of the movements and behaviour of animals is a valuable research tool. Recently, machine learning tools were applied to many species to classify units of behaviour. For the monitoring of wild species, collecting enough data for training models might be problematic, thus we examine how machine learning models trained on one species can be applied to another closely related species with similar behavioural conformation.

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Transmembrane proteins include membrane channels, pores, and receptors and, as such, comprise an important part of the proteome, yet our knowledge about them is much less complete than about soluble, globular proteins. An important aspect of transmembrane protein structure is their exact position within the lipid bilayer, a feature hard to investigate experimentally at the atomic level. Here we describe MemBlob, a novel approach utilizing difference electron density maps obtained by cryo-EM studies of transmembrane proteins.

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Summary: The identification of transmembrane helices in transmembrane proteins is crucial, not only to understand their mechanism of action but also to develop new therapies. While experimental data on the boundaries of membrane-embedded regions are sparse, this information is present in cryo-electron microscopy (cryo-EM) density maps and it has not been utilized yet for determining membrane regions. We developed a computational pipeline, where the inputs of a cryo-EM map, the corresponding atomistic structure, and the potential bilayer orientation determined by TMDET algorithm of a given protein result in an output defining the residues assigned to the bulk water phase, lipid interface and the lipid hydrophobic core.

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