Eduard V. Bocharov

ORCID: 0000-0002-3635-1609
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About
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Research Areas
  • Protein Structure and Dynamics
  • Lipid Membrane Structure and Behavior
  • HER2/EGFR in Cancer Research
  • Glycosylation and Glycoproteins Research
  • Monoclonal and Polyclonal Antibodies Research
  • RNA and protein synthesis mechanisms
  • Enzyme Structure and Function
  • Alzheimer's disease research and treatments
  • Computational Drug Discovery Methods
  • Ion channel regulation and function
  • Toxin Mechanisms and Immunotoxins
  • Receptor Mechanisms and Signaling
  • Advanced NMR Techniques and Applications
  • Peptidase Inhibition and Analysis
  • Chemical Reactions and Isotopes
  • Bacterial Genetics and Biotechnology
  • Chemical Synthesis and Analysis
  • Protein Kinase Regulation and GTPase Signaling
  • Neuroscience and Neuropharmacology Research
  • Venomous Animal Envenomation and Studies
  • Axon Guidance and Neuronal Signaling
  • RNA Research and Splicing
  • Insect and Pesticide Research
  • Nicotinic Acetylcholine Receptors Study
  • Hemoglobin structure and function

Institute of Bioorganic Chemistry
2016-2025

Moscow Institute of Physics and Technology
2018-2024

Moscow Power Engineering Institute
2020-2024

Russian Academy of Sciences
2000-2024

Institute of Bioorganic Chemistry
2023

Moscow Aviation Institute
2023

Kurchatov Institute
2013-2019

A. N. Nesmeyanov Institute of Organoelement Compounds
2013

N.D. Zelinsky Institute of Organic Chemistry
2013

Institute of Molecular Genetics
2013

Proper lateral dimerization of the transmembrane domains receptor tyrosine kinases is required for biochemical signal transduction across plasma membrane. The spatial structure dimeric domain growth factor ErbB2 embedded into lipid bicelles was obtained by solution NMR, followed molecular dynamics relaxation in an explicit bilayer. segments associate a right-handed α-helical bundle through N-terminal tandem GG4-like motif Thr652-X3-Ser656-X3-Gly660, providing explanation pathogenic power...

10.1074/jbc.m709202200 article EN cc-by Journal of Biological Chemistry 2008-01-05

BNip3 is a prominent representative of apoptotic Bcl-2 proteins with rather unique properties initiating an atypical programmed cell death pathway resembling both necrosis and apoptosis. Many family modulate the permeability state outer mitochondrial membrane by forming homo- hetero-oligomers. The structure dynamics homodimeric transmembrane domain were investigated aid solution NMR in lipid bicelles molecular energy relaxation explicit bilayer. right-handed parallel helix-helix hydrogen...

10.1074/jbc.m701745200 article EN cc-by Journal of Biological Chemistry 2007-04-06

Eph receptors are found in a wide variety of cells developing and mature tissues represent the largest family receptor tyrosine kinases, regulating cell shape, movements, attachment. The kinases conduct biochemical signals across plasma membrane via lateral dimerization which their transmembrane domains play an important role. Structural-dynamic properties homodimeric domain EphA1 were investigated with aid solution NMR lipid bicelles molecular dynamics explicit bilayer. segments associate...

10.1074/jbc.m803089200 article EN cc-by Journal of Biological Chemistry 2008-08-27

Erb-b2 receptor tyrosine kinase (HER2) transmembrane domain (TMD) mutations (HER2V659E, HER2G660D) have previously been identified in lung adenocarcinomas, but their frequency and clinical significance is unknown.We prospectively analyzed 8551 consecutive adenocarcinomas using hybrid capture-based comprehensive genomic profiling (CGP) at the request of individual treating physicians for purpose making therapy decisions.We 15 cases (0.18%) HER2 TMD (HER2V659E/D, through CGP adenocarcinomas....

10.1016/j.jtho.2016.11.2224 article EN cc-by-nc-nd Journal of Thoracic Oncology 2016-11-27

APPjmtm and bind by nuclear magnetic resonance (View interaction).

10.1016/j.febslet.2012.04.062 article EN FEBS Letters 2012-05-11

Based on the 1H-15N NMR spectroscopy data, three-dimensional structure and internal dynamic properties of ribosomal protein L7 from Escherichia coli were derived. The dimer in solution can be described as a set three distinct domains, tumbling rather independently linked via flexible hinge regions. dimeric N-terminal domain (residues 1-32) consists two antiparallel α-α-hairpins forming symmetrical four-helical bundle, whereas identical C-terminal domains 52-120) adopt compact α/β-fold. There...

10.1074/jbc.m313384200 article EN cc-by Journal of Biological Chemistry 2004-04-01

Alzheimer's disease affects people all over the world, regardless of nationality, gender or social status. An adequate study requires essential understanding molecular fundamentals pathogenesis. The amyloid β-peptide, which forms plaques in brain with disease, is product sequential cleavage a single-span membrane precursor protein (APP). More than half APP mutations found to be associated familial are located its transmembrane domain. pathogenic presumably affect structural-dynamic...

10.32607/20758251-2011-3-1-69-76 article EN Acta Naturae 2011-03-15

The epidermal growth factor receptor (EGFR) family is an important class of tyrosine kinases, mediating a variety cellular responses in normal biological processes and pathological states multicellular organisms. Different modes dimerization the human EGFR transmembrane domain (TMD) different membrane mimetics recently prompted us to propose novel signal transduction mechanism based on protein-lipid interaction. However, experimental evidence for it was originally obtained with slightly TMD...

10.1021/acs.biochem.6b01085 article EN Biochemistry 2017-03-14

Abstract Neuraminidase 1 (NEU1) is a lysosomal sialidase catalyzing the removal of terminal sialic acids from sialyloconjugates. A plasma membrane-bound NEU1 modulating plethora receptors by desialylation, has been consistently documented last ten years. Despite growing interest scientific community to NEU1, its membrane organization not understood and current structural biochemical data cannot account for such localization. By combining molecular biology analyses with biophysics...

10.1038/srep38363 article EN cc-by Scientific Reports 2016-12-05

Alzheimer's disease (AD) pathogenesis is correlated with the membrane content of various lipid species, including cholesterol, whose interactions amyloid precursor protein (APP) have been extensively explored. Amyloid-β peptides triggering AD are products APP cleavage by secretases, which differ depending on and secretase location relative to ordered or disordered microdomains. We used high-resolution NMR probe cholesterol analog transmembrane domain in two membrane-mimicking systems...

10.3390/ijms26020553 article EN International Journal of Molecular Sciences 2025-01-10

Toll‐like receptors (TLRs) are important players in the innate immune system. Binding of pathogen‐related molecules to extracellular domains TLRs initiates signalosome assembly, a key event signal transduction. Despite extensive research on individual receptor domains, mechanism assembly remains unclear. Recent evidence suggests that intracellular TIR domain TLR1 binds zinc ions, with cysteines playing pivotal role binding and activation. This study explores zinc‐binding ability TLR2 (TLR2...

10.1002/1873-3468.70026 article EN other-oa FEBS Letters 2025-03-03

Introduction. The structure of dihydroquercetin (DHQ) is characterized by two chiral centers at positions 2 and 3 the benzopyran cycle, resulting in possible diastereomers: trans - cis -isomers. Therefore, development methods for qualitative quantitative control DHQ diastereomers analyzed samples essential patient safety management. Nuclear magnetic resonance (NMR) spectroscopy one physicochemical that can be used this purpose. Aim. study objective was to accumulate analytical structural...

10.33380/2305-2066-2024-13-2-1751 article EN cc-by Drug development & registration 2024-05-08

The scorpion toxin BeKm-1 is unique among a variety of known short toxins affecting potassium channels in its selective action on ether-a-go-go-related gene (ERG)-type channels. shares the common molecular scaffold with other toxins. spatial structure resolved by NMR consists α-helix and triple-stranded antiparallel β-sheet. By mutagenesis study we identified residues that are important for binding to human ERG K+ (HERG) channel. most critical (Tyr-11, Lys-18, Arg-20, Lys-23) located...

10.1074/jbc.m204083200 article EN cc-by Journal of Biological Chemistry 2002-11-01
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