Publications by authors named "Alexander L Chernorudskiy"

Calcium signaling plays an important role in cell survival by influencing mitochondria-related processes such as energy production and apoptosis. The endoplasmic reticulum (ER) is the main storage compartment for cell calcium (Ca; ~60-500μM), and the Ca released by the ER has a prompt effect on the homeostasis of the juxtaposed mitochondria. Recent findings have highlighted a close connection between ER redox and Ca signaling that is mediated by Ca-handling proteins.

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Ubiquitylation, a widespread and important posttranslational modification of eukaryotic proteins, regulates a multitude of critical cellular processes, both in normal and pathological conditions. A classical view of how ubiquitylation regulates protein function involves recognition of ubiquitin-encoded signals by specific ubiquitin-binding domains. However, evidence suggests the existence of direct effects of ubiquitylation, which occur through its impact on protein-protein interactions that do not involve specific ubiquitin receptors.

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Summary: VSDocker is an original program that allows using AutoDock4 for optimized virtual ligand screening on computer clusters or multiprocessor workstations. This tool is the first implementation of parallel high-performance virtual screening of ligands for MS Windows-based computer systems.

Availability: VSDocker 2.

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Tyrphostin AG1478 is known as a specific and reversible inhibitor of TK (tyrosine kinase) activity of the EGFR [EGF (epidermal growth factor) receptor]. It is attractive as an anticancer agent for cancers with elevated EGFR TK levels. However, post-application effects of AG1478 are not well studied.

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Background: Post-translational protein modification with ubiquitin, or ubiquitylation, is one of the hottest topics in a modern biology due to a dramatic impact on diverse metabolic pathways and involvement in pathogenesis of severe human diseases. A great number of eukaryotic proteins was found to be ubiquitylated. However, data about particular ubiquitylated proteins are rather disembodied.

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