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Chemistry

D-Index
42
Citations
6333
World Ranking
17544
National Ranking
67

Overview

Roman G. Efremov is affiliated with the Russian Academy of Sciences in the Russian Federation. Their primary area of work falls within Biochemistry, Genetics and Molecular Biology, with extensive research contributions in Molecular Biology as a subfield.

Their research spans several main topics, which include:

  • Lipid Membrane Structure and Behavior
  • Protein Structure and Dynamics
  • Monoclonal and Polyclonal Antibodies Research
  • Ion channel regulation and function
  • Ion Channels and Receptors
  • RNA and protein synthesis mechanisms
  • Nicotinic Acetylcholine Receptors Study

Roman G. Efremov has authored multiple papers, with recent publications including:

  • Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel, 2021, Nature Structural & Molecular Biology
  • Environmental and dynamic effects explain how nisin captures membrane-bound lipid II, 2020, Scientific Reports
  • Protein compactness and interaction valency define the architecture of a biomolecular condensate across scales, 2023, eLife
  • Complex approach for analysis of snake venom α-neurotoxins binding to HAP, the high-affinity peptide, 2020, Scientific Reports
  • Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?, 2020, Frontiers in Oncology

Frequent co-authors in their research efforts include:

  • Nikolay A. Krylov
  • Anton O. Chugunov
  • Anastasia G. Konshina
  • Eduard V. Bocharov
  • Yu. A. Trofimov

Their work has been published often in the following venues:

  • International Journal of Molecular Sciences (14 publications)
  • bioRxiv (Cold Spring Harbor Laboratory) (6 publications)
  • Zenodo (CERN European Organization for Nuclear Research) (5 publications)
  • Biochimica et Biophysica Acta (BBA) - Biomembranes (4 publications)
  • Biophysical Journal (4 publications)

Their contributions also include book publications through the Institute of Biomedical Chemistry, Moscow, Russia eBooks, notably:

  • Abstracts of XXVII Symposium "Bioinformatics and Computer-Aided Drug Discovery", 2021
  • PROCEEDINGS BOOK OF THE XXVIII SYMPOSIUM "BIOINFORMATICS AND COMPUTER-AIDED DRUG DISCOVERY", MOSCOW, 2022

Best Publications

  • Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state.

    Eduard V. Bocharov;Konstantin S. Mineev;Pavel E. Volynsky;Yaroslav S. Ermolyuk

  • PLATINUM: a web tool for analysis of hydrophobic/hydrophilic organization of biomolecular complexes.

    Timothy V. Pyrkov;Anton O. Chugunov;Nikolay A. Krylov;Dmitry E. Nolde

  • Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger.

    Eduard V. Bocharov;Yulia E. Pustovalova;Konstantin V. Pavlov;Pavel E. Volynsky

  • Molecular lipophilicity in protein modeling and drug design

    Roman G. Efremov;Anton O. Chugunov;Timothy V. Pyrkov;John P. Priestle

  • Surface‐enhanced Raman spectroscopy of biomolecules. Part I.—water‐soluble proteins, dipeptides and amino acids

    G. D. Chumanov;R. G. Efremov;I. R. Nabiev

  • Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel.

    Kirill D. Nadezhdin;Arthur Neuberger;Yuri A. Trofimov;Yuri A. Trofimov;Yuri A. Trofimov;Nikolay A. Krylov;Nikolay A. Krylov

  • Spatial Structure and pH-dependent Conformational Diversity of Dimeric Transmembrane Domain of the Receptor Tyrosine Kinase EphA1

    Eduard V. Bocharov;Maxim L. Mayzel;Pavel E. Volynsky;Marina V. Goncharuk

  • Left-handed dimer of EphA2 transmembrane domain: Helix packing diversity among receptor tyrosine kinases.

    Eduard V. Bocharov;Maxim L. Mayzel;Pavel E. Volynsky;Konstantin S. Mineev

  • Helix-helix interactions in membrane domains of bitopic proteins: specificity and role of lipid environment

    Eduard V. Bocharov;Konstantin S. Mineev;Konstantin V. Pavlov;Sergey A. Akimov

  • Surface-enhanced Raman scattering and its application to the study of biological molecules

    I R Nabiev;R G Efremov;G D Chumanov

  • The role of the invariant His-1069 in folding and function of the Wilson's disease protein, the human copper-transporting ATPase ATP7B

    Ruslan Tsivkovskii;Roman G. Efremov;Svetlana Lutsenko;Svetlana Lutsenko

  • PREDDIMER: a web server for prediction of transmembrane helical dimers

    Anton A. Polyansky;Anton O. Chugunov;Pavel E. Volynsky;Nikolay A. Krylov

  • Human copper-transporting ATPase ATP7B (the Wilson's disease protein): biochemical properties and regulation.

    Svetlana Lutsenko;Roman G. Efremov;Ruslan Tsivkovskii;Joel M. Walker

  • Antimicrobial Peptides Induce Growth of Phosphatidylglycerol Domains in a Model Bacterial Membrane

    Anton A. Polyansky;Anton A. Polyansky;Rajesh Ramaswamy;Pavel E. Volynsky;Ivo F. Sbalzarini

  • Structure and Dynamics of Cardiotoxins

    Anastasia G. Konshina;Peter V. Dubovskii;Roman G. Efremov

  • Multistate organization of transmembrane helical protein dimers governed by the host membrane.

    Anton A. Polyansky;Anton A. Polyansky;Pavel E. Volynsky;Roman G. Efremov;Roman G. Efremov

  • The distinct functional properties of the nucleotide-binding domain of ATP7B, the human copper-transporting ATPase: analysis of the Wilson disease mutations E1064A, H1069Q, R1151H, and C1104F.

    Clinton T. Morgan;Ruslan Tsivkovskii;Yuri A. Kosinsky;Roman G. Efremov

  • Lipid-II forms potential “landing terrain” for lantibiotics in simulated bacterial membrane

    Anton Chugunov;Darya Pyrkova;Dmitry Nolde;Anton Polyansky;Anton Polyansky

  • A Solvent Model for Simulations of Peptides in Bilayers. I. Membrane-Promoting α-Helix Formation

    Roman G. Efremov;Dmitry E. Nolde;Gérard Vergoten;Alexander S. Arseniev

  • Interaction of three-finger toxins with phospholipid membranes: comparison of S- and P-type cytotoxins.

    Peter V. Dubovskii;Dmitry M. Lesovoy;Maxim A. Dubinnyi;Anastasiya G. Konshina

  • Pyrenemethyl ara-uridine-2'-carbamate: a strong interstrand excimer in the major groove of a DNA duplex.

    Natalia N. Dioubankova;Andrei D. Malakhov;Dmitry A. Stetsenko;Michael J. Gait

Frequent Co-Authors

Alexander S. Arseniev
Alexander S. Arseniev Russian Academy of Sciences
Igor Nabiev
Igor Nabiev Moscow Engineering Physics Institute
Jan Tytgat
Jan Tytgat KU Leuven
Svetlana Lutsenko
Svetlana Lutsenko Johns Hopkins University
Eugene V. Grishin
Eugene V. Grishin Russian Academy of Sciences
André Capron
André Capron Institut Pasteur
Konstantin A. Lukyanov
Konstantin A. Lukyanov Skolkovo Institute of Science and Technology
Donald D. Newmeyer
Donald D. Newmeyer La Jolla Institute For Allergy & Immunology
Ivo F. Sbalzarini
Ivo F. Sbalzarini Max Planck Institute of Molecular Cell Biology and Genetics
Daniel Bertrand
Daniel Bertrand University of Geneva

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