Alexey Petrov

ORCID: 0000-0001-7259-4555
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About
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Research Areas
  • RNA and protein synthesis mechanisms
  • RNA modifications and cancer
  • RNA Research and Splicing
  • Viral Infections and Immunology Research
  • Bacterial Genetics and Biotechnology
  • Bacteriophages and microbial interactions
  • Monoclonal and Polyclonal Antibodies Research
  • Cancer-related gene regulation
  • Advanced biosensing and bioanalysis techniques
  • CRISPR and Genetic Engineering
  • Toxin Mechanisms and Immunotoxins
  • Force Microscopy Techniques and Applications
  • DNA and Nucleic Acid Chemistry
  • Plant Virus Research Studies
  • Ion channel regulation and function
  • Molecular Biology Techniques and Applications
  • Advanced Fluorescence Microscopy Techniques
  • Virus-based gene therapy research
  • Mycobacterium research and diagnosis
  • Polyamine Metabolism and Applications
  • Protein purification and stability
  • Geomagnetism and Paleomagnetism Studies
  • Biofield Effects and Biophysics
  • Microbial Inactivation Methods
  • Advanced Electron Microscopy Techniques and Applications

Auburn University
2017-2023

Stanford University
2010-2019

Institute of Theoretical and Experimental Biophysics
2018

Moscow State University
2008

University of Maryland, College Park
2003-2008

University of Maryland, Baltimore
2007-2008

Johnson University
2000-2002

Rutgers, The State University of New Jersey
2001

Significance Zero-mode waveguides (ZMWs) provide a powerful technology for studying single-molecule real-time dynamics of biological systems. However, difficulties in instrumental implementation and ZMW fabrication prevented their widespread use. Here, we modify commercially available ZMW-based DNA sequencer use as multipurpose fluorescence instrument. The instrumentation presented here allows access to ZMWs the general biophysics community high-throughput multiplexed single molecules.

10.1073/pnas.1315735111 article EN Proceedings of the National Academy of Sciences 2013-12-30

Translating mRNA sequences into functional proteins is a fundamental process necessary for the viability of organisms throughout all kingdoms life. The ribosome carries out this with delicate balance between speed and accuracy. This work investigates how structure function are affected by rRNA base modification. prevailing view that modifications serve to fine tune function.To test hypothesis, yeast strains deficient in ribosomal peptidyltransferase center were monitored changes...

10.1371/journal.pone.0000174 article EN cc-by PLoS ONE 2007-01-23

The human cytomegalovirus (HCMV) is a ubiquitous, pathogenic herpesvirus. complete viral genome transcriptionally active during infection; however, large part of its transcriptome has yet to be annotated. In this work, we applied the amplified isoform sequencing technique from Pacific Biosciences characterize lytic HCMV strain Towne varS. We developed pipeline for transcript annotation using long-read data. identified 248 transcriptional start sites, 116 termination sites and 80 splicing...

10.1038/s41598-017-16262-z article EN cc-by Scientific Reports 2017-11-16

10.1016/b978-0-12-420037-1.00017-8 article EN Methods in enzymology on CD-ROM/Methods in enzymology 2013-01-01

Microwave-accelerated proteolysis using acetic acid has been shown to occur specifically on either or both sides of aspartic residues. This chemical cleavage applied ovalbumin and several model peptides test the effect some more common post-translational modifications. No oxidation methionine cysteine was observed; however, hydrolysis phosphate groups proceeds at a detectable rate. Acid also extended yeast ribosome proteome, where it provided information 74% that proteome. Aspartic occurs...

10.1021/pr070502c article EN Journal of Proteome Research 2008-01-12

Significance Protein biosynthesis is most tightly controlled during translation initiation that involves numerous factors and regulatory proteins. This complexity confounds conventional biochemical methods. Single-molecule approaches are ideally suited to address such questions. However, their application hindered by the lack of fluorescently labeled components eukaryotic machinery. Here, we demonstrate an approach label human 40S ribosomal subunits. As extension this approach, used...

10.1073/pnas.1421328111 article EN Proceedings of the National Academy of Sciences 2014-12-16

During termination of translation, the nascent peptide is first released from ribosome, which must be subsequently disassembled into subunits in a process known as ribosome recycling. In bacteria, and recycling are mediated by translation factors RF, RRF, EF-G, IF3, but their precise roles have remained unclear. Here, we use single-molecule fluorescence to track conformation composition real time during Our results show that release RF induces rotated ribosomal conformation. RRF binds this...

10.1016/j.celrep.2017.06.028 article EN cc-by-nc-nd Cell Reports 2017-07-01

Single-molecule Förster resonance energy transfer (smFRET) is a powerful method for studying the conformational dynamics of biomolecule in real-time. However, how interacting ligands correlate with and regulate extremely challenging because availability limited number fluorescent dyes both high quantum yield minimal spectral overlap. Here we report use nonfluorescent quencher (Black Hole Quencher, BHQ) as an acceptor smFRET. Using Cy3/BHQ pair, can accurately follow changes ribosome during...

10.1021/ja2119964 article EN Journal of the American Chemical Society 2012-03-19

The signal recognition particle (SRP) directs ribosome-nascent chain complexes (RNCs) displaying sequences to protein translocation channels in the plasma membrane of prokaryotes and endoplasmic reticulum eukaryotes. It was initially proposed that SRP binds sequence when it emerges from an RNC successful binding becomes impaired as translation extends nascent chain, moving away on ribosomal surface. Later studies drew this simple model into question, proposing is unaffected by length. Here,...

10.1074/jbc.m114.563239 article EN cc-by Journal of Biological Chemistry 2014-05-08

A new class of eukaryotic protein kinases that are not homologous to members the serine/threonine/tyrosine kinase superfamily was recently identified [Futey, L. M., et al. (1995) J. Biol. Chem. 270, 523−529; Ryazanov, A. G., (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 4884−4889]. This includes elongation factor-2 kinase, Dictyostelium myosin heavy chain A, B, and C, several mammalian putative yet fully characterized [Ryazanov, (1999) Curr. 9, R43−R45]. eEF-2 is a ubiquitous phosphorylates...

10.1021/bi0007270 article EN Biochemistry 2000-09-16
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