M. S. Yurkova

ORCID: 0009-0007-5658-0891
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About
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Research Areas
  • Enzyme Structure and Function
  • Protein purification and stability
  • Heat shock proteins research
  • Protein Structure and Dynamics
  • Monoclonal and Polyclonal Antibodies Research
  • Toxin Mechanisms and Immunotoxins
  • Transgenic Plants and Applications
  • Viral Infectious Diseases and Gene Expression in Insects
  • RNA modifications and cancer
  • Biochemical and Molecular Research
  • DNA Repair Mechanisms
  • Microbial Metabolic Engineering and Bioproduction
  • RNA and protein synthesis mechanisms
  • Antimicrobial Peptides and Activities
  • Hepatitis B Virus Studies
  • Bacteriophages and microbial interactions
  • Insect and Pesticide Research
  • Protein Kinase Regulation and GTPase Signaling
  • Bacillus and Francisella bacterial research
  • Advanced Proteomics Techniques and Applications
  • Prenatal Screening and Diagnostics
  • Blood Coagulation and Thrombosis Mechanisms
  • vaccines and immunoinformatics approaches
  • Ion channel regulation and function
  • Chemical Synthesis and Analysis

Russian Academy of Sciences
2017-2023

Federal Center Research Fundamentals of Biotechnology
2017-2023

A N Bach Institute of Biochemistry
2019-2023

Biotechnology Research Center
2021

University of Tripoli
2021

Peoples' Friendship University of Russia
2019

Russian Research Center for Molecular Diagnostics and Therapy
2004-2011

Russian Scientific Center of Radiology and Surgical Technologies
2004

Florida State University
2000

Wayne State University
1997

Previous studies have shown that membrane type 1-matrix metalloproteinase (MT1-MMP) (MMP-14) initiates pro-MMP-2 activation in a process is tightly regulated by the level of tissue inhibitor (TIMP)-2. However, given difficulty modulating TIMP-2 levels, direct effect on MT1-MMP processing and cellular system could not be established. Here, recombinant vaccinia viruses encoding full-length or were used to express alone combination with various levels mammalian cells. We show regulates amount...

10.1074/jbc.275.16.12080 article EN cc-by Journal of Biological Chemistry 2000-04-01

Background: Bovine colostrum (BC) is the first milk produced by a cow postpartum. It unique substance rich in antibodies that protects body against bacterial and viral pathogens. BC significantly contributes to human nutrition health, as its effectiveness certain viruses well-studied. Locally, cows are vaccinated with polyvalent inactivated vaccine diarrhea, bovine escherichiosis, rotavirus (BRoV), coronavirus (BCoV). contains high levels of these antigens, which provide advanced immune...

10.31989/ffhd.v15i4.1592 article EN Functional Foods in Health and Disease 2025-04-18

This data article is related to the research entitled "Assessment of structurally modified plant virus as a novel adjuvant in toxicity studies" (Nikitin et al., 2018), devoted safety study - spherical particles (SPs). SPs are generated by thermally denatured tobacco mosaic (TMV) coat protein and act effective for development new vaccine candidates. reports additional results on studies TMV SPs. The weight coefficients laboratory animals internal organs complements subchronic studies. Also...

10.1016/j.dib.2018.10.102 article EN cc-by Data in Brief 2018-10-26

We have developed a fusion system for reliable production of insoluble hydrophobic proteins in soluble stable forms. A carrier is thermophilic minichaperone, GroEL apical domain (GrAD), 15 kDa monomer able to bind diverse protein substrates. The Met-less variant GrAD has been made further convenient use Met-specific CNBr chemical cleavage, if desired. retained stability and solubility the original protein. Target polypeptides can be fused either C-terminus or N-terminus GrAD. tested with two...

10.1093/protein/gzv060 article EN Protein Engineering Design and Selection 2015-11-25

In this review, we discuss the potential of molecular chaperones belonging to GroEL family as applied different practical uses.The GroEL, often referred chaperonin, plays a fundamental role in protein folding cells and is essential for proper number proteins.Early on studying it has been considered, along with other chaperones, an attractive tool assist recombinant their refolding vitro.Several schemes using have difficult-todeal targets, especially those insoluble unstable.Fusion constructs...

10.17756/nwj.2018-053 article EN NanoWorld Journal 2018-01-01

Abstract Hydrophobic recombinant proteins often tend to aggregate upon expression into inclusion bodies and are difficult refold. Producing them in soluble forms constitutes a common bottleneck problem. A fusion system for production of insoluble hydrophobic stable with thermophilic minichaperone, GroEL apical domain (GrAD) as carrier, has recently been developed. To provide the utmost flexibility interactions between carrier various target protein moieties strategy making permutated...

10.1038/s41598-019-51015-0 article EN cc-by Scientific Reports 2019-10-21

Abstract The system is developed for efficient biosynthetic production of difficult-to-express polypeptides. A target polypeptide produced fused into T. thermophilus GroEL chaperonin chain in such a way that it presented inside the cavity near substrate binding surface. Such presentation allows alleviating potential problems instability, toxicity or hydrophobicity peptide. Thermostability thermophilic can be used its one-step separation from host cell proteins by heating. may released any...

10.1038/s41598-020-78094-8 article EN cc-by Scientific Reports 2020-12-03

Synthetic peptides are in high demand as biologically active substances. Solid phase synthesis is the primary method of peptide production. However, it has drawbacks: large amount chemical waste and rapid increase price with length. Biosynthesis intended to bypass these flaws. Direct biosynthesis usually not effective among other approaches for improving quality quantity target product fusion partners widely used. In this study we used a thermostable chaperon-based partner developed by us...

10.1016/j.btre.2022.e00734 article EN cc-by Biotechnology Reports 2022-05-14

Extracts from mistletoe (<i>Viscum album</i> L.) contain three main toxic proteins -the lectins MLI (also known as vls-cumln), MLII and MLIII. A catalytic subu-nlt of the plant lectin MLIII has been cloned expressed In <i>Escherichia coli</i> cells. The structure immunochemical properties recombinant A-subunlt were Investigated using a panel monoclonal antibodies against ML-toxlns. Rlbosome-lnactlvating activity was determined cell-free system exhibiting Inhibition endogenous protein...

10.1055/s-0031-1296966 article EN Arzneimittelforschung 2011-12-25

Large peptide biosynthesis is a valuable alternative to conventional chemical synthesis. Enfuvirtide, the largest therapeutic used in HIV infection treatment, was synthesized our thermostable chaperone-based system and evaluated for quality as well profile of process-related impurities. Host cell proteins (HCPs) BrCN cleavage-modified peptides were by LC-MS intermediate. Cleavage modifications during reaction assessed after maps aligned simple in-house algorithm formylation/oxidation levels...

10.1371/journal.pone.0286752 article EN cc-by PLoS ONE 2023-06-08
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