N. A. Petushkova

ORCID: 0000-0002-4101-4607
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Advanced Proteomics Techniques and Applications
  • Mass Spectrometry Techniques and Applications
  • Metabolomics and Mass Spectrometry Studies
  • Pharmacogenetics and Drug Metabolism
  • Analytical Chemistry and Chromatography
  • Glycosylation and Glycoproteins Research
  • Molecular Biology Techniques and Applications
  • Ubiquitin and proteasome pathways
  • S100 Proteins and Annexins
  • Physiological and biochemical adaptations
  • Carbohydrate Chemistry and Synthesis
  • Neurological Disorders and Treatments
  • Eicosanoids and Hypertension Pharmacology
  • Computational Drug Discovery Methods
  • Drug Transport and Resistance Mechanisms
  • Cannabis and Cannabinoid Research
  • Diet, Metabolism, and Disease
  • Digestive system and related health
  • Heme Oxygenase-1 and Carbon Monoxide
  • Flavonoids in Medical Research
  • Glutathione Transferases and Polymorphisms
  • Pregnancy and preeclampsia studies
  • Axon Guidance and Neuronal Signaling
  • Metal-Catalyzed Oxygenation Mechanisms
  • Skin and Cellular Biology Research

Institute of Biomedical Chemistry
2014-2024

Institute of Protein Research
2023

Academy of Medical Sciences
2008-2014

Russian Academy of Sciences
2008-2014

The University of Texas Southwestern Medical Center
2000

The role of electrostatic interactions in the association P450s with their nicotinamide adenine dinucleotide phosphate- (NADPH) dependent flavoprotein reductases was studied by fluorescence resonance energy transfer. fluorescent probe 7-(ethylamino)-3-(4'-maleimidylphenyl)-4-methylcoumarin maleimide (coumarylphenylmaleimide, CPM) introduced into molecule at a 1:1 molar ratio. interaction P450 2B4 and NADPH−P450 reductase (CPR) from rabbit liver microsomes compared that isolated heme domain...

10.1021/bi992936u article EN Biochemistry 2000-05-01

Liquid chromatography-tandem mass spectrometry was used to analyze plasma proteins of volunteers (control) and patients with glioblastoma multiform (GBM). A database search pre-set a variable post-translational modification (PTM): phosphorylation, acetylation or ubiquitination. There were no significant differences between the control GBM groups regarding number protein identifications, sequence coverage PTMs. However, in plasma, we unambiguously observed decreased fraction...

10.1371/journal.pone.0177427 article EN cc-by PLoS ONE 2017-05-11

Background There are two ways that statistical methods can learn from biomedical data. One way is to classifiers identify diseases and predict outcomes using the training dataset with established diagnosis for each sample. When not available task be mine presence of meaningful groups (clusters) samples explore underlying data structure (unsupervised learning). Results We investigated proteomic profiles cytosolic fraction human liver two-dimensional electrophoresis (2DE). Samples were...

10.1371/journal.pone.0103950 article EN cc-by PLoS ONE 2014-08-01

Abstract Background Using human keratinocyte HaCaT cell line model, we screened for proteins that changed their content due to SDS exposure in non-toxic dose (25 μg/ml, as determined by the MTT assay and microscopic examination) during 48 h. Methods The altered level of from keratinocytes exposed was analyzed LC-MS/MS approach quantified using Progenesis LC software. Results Pathview map 131 upregulated built, enhancement glycolysis/gluconeogenesis found. Conclusions results our study admit...

10.1186/s41702-019-0054-y article EN cc-by Biomedical Dermatology 2020-01-14

The development of commercially available panels for human blood plasma screening via selected reaction monitoring (SRM) offers reliable, cost-efficient and highly-standardized discovery validation protein biomarkers. However, detection by SRM can be hampered interfering peptide fragment ions. To estimate the influence interference on detection, we performed different types sample preparation implemented measurements well-characterized targets approved US Food Drug Administration.We used...

10.1186/s40169-015-0071-4 article EN cc-by Clinical and Translational Medicine 2015-10-15

Sequential thin slicing of one-dimensional electrophoresis gels followed by slice-by-slice mass spectrometry to allow protein identification was used produce a proteomic map for cytochromes P450. Parallel MALDI-TOF-MS and LC-MS/MS analyses were performed. Combination the two MS methods increased quality identification. We have proposed an efficient approach obtain comprehensive profile drug-metabolizing enzymes in liver that can be differentiate between polymorphic variants

10.1021/pr900262z article EN Journal of Proteome Research 2009-09-02

There is no direct evidence supporting that SDS a carcinogen, so to investigate this fact, we used HaCaT keratinocytes as model of human epidermal cells. To reveal the candidate proteins and/or pathways characterizing impact on HaCaT, proposed comparative proteoinformatics pipeline. For protein extraction, performance two sample preparation protocols was assessed: 0.2% SDS-based solubilization combined with 1DE-gel concentration (Protocol 1) and osmotic shock 2). As result, in SDS-exposed...

10.1038/s41598-022-25934-4 article EN cc-by Scientific Reports 2022-12-12

In the present study, we explored technology of liquid chromatography-mass spectrometry (HPLC-MS/MS) for proteome analysis blood plasma patients with early chronic cerebral ischemia. Analysis mass-spectrometer data carried out in automatic mode using software Progenesis LS-MS. As a result this study identified 43 proteins. The differences group compared control 7 It was found that stages ischemia changes affect proteins related to immune system, system maintenance hemostasis and lipid...

10.18097/pbmc20166205599 article EN Biomeditsinskaya Khimiya 2016-01-01

Proteomics often exploits sequential cutting of the SDS-PAGE gel lane into slices with subsequent identification proteins by peptide mass fingerprinting (PMF). In this paper, influence slice thickness on protein was investigated. Following separation human liver microsomal fraction, 37 to 75 kDa range cut 20 or 40 0.5 mm and 0.25 thickness, respectively. Identification after trypsinolysis performed MALDI-TOF spectrometry. A twofold reduction did not number peaks in PMF-spectra. It...

10.4172/jpb.1000211 article EN Journal of Proteomics & Bioinformatics 2012-01-01
Coming Soon ...