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Alexander S. Arseniev

Alexander S. Arseniev

D-Index & Metrics

Chemistry

D-Index
67
Citations
12191
World Ranking
7107
National Ranking
18

Overview

Alexander S. Arseniev is affiliated with the Russian Academy of Sciences in the Russian Federation. Their research primarily focuses on biochemistry, genetics, and molecular biology, with significant contributions in molecular biology, cellular and molecular neuroscience, immunology, genetics, and epidemiology subfields.

The scientist's work covers several main topics including:

  • Nicotinic Acetylcholine Receptors Study
  • Ion channel regulation and function
  • Nerve injury and regeneration
  • Lipid Membrane Structure and Behavior
  • Protein Structure and Dynamics
  • Immune Response and Inflammation
  • Venomous Animal Envenomation and Studies

Alexander S. Arseniev has published papers in various scientific journals and venues. Some notable recent publications include:

  • "Apamin structure and pharmacology revisited," 2022, Frontiers in Pharmacology
  • "NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids," 2021, Chemical Science
  • "The architecture of transmembrane and cytoplasmic juxtamembrane regions of Toll-like receptors," 2023, Nature Communications
  • "Spatial Structure and Activity of Synthetic Fragments of Lynx1 and of Nicotinic Receptor Loop C Models," 2020, Biomolecules
  • "Structural Studies Providing Insights into Production and Conformational Behavior of Amyloid-β Peptide Associated with Alzheimer's Disease Development," 2021, Molecules

The most frequent publication venues for Arseniev's work include:

  • Communications Biology
  • Protein Expression and Purification
  • bioRxiv (Cold Spring Harbor Laboratory)
  • International Journal of Molecular Sciences
  • Nature Communications

Alexander S. Arseniev frequently collaborates with several researchers, including:

  • Константин С. Минеев
  • Sergey A. Goncharuk
  • Marina V. Goncharuk
  • Erik F. Kot
  • Eduard V. Bocharov

Best Publications

  • 1H-NMR study of gramicidin A transmembrane ion channel: Head-to-head right-handed, single-stranded helices

    A.S. Arseniev;I.L. Barsukov;V.F. Bystrov;A.L. Lomize

  • Three-dimensional structure of ectatomin from Ectatomma tuberculatum ant venom.

    Dmitry E. Nolde;Alexander G. Sobol;Kirill A. Pluzhnikov;Eugene V. Grishin

  • NMR studies of Brownian tumbling and internal motions in proteins

    D.M. Korzhnev;M. Billeter;A.S. Arseniev;V.Y. Orekhov

  • 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

  • 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

  • The Chemical Basis of Fungal Bioluminescence

    Konstantin V. Purtov;Valentin N. Petushkov;Mikhail S. Baranov;Konstantin S. Mineev

  • Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H-15N NMR spectroscopy.

    Vladislav Yu. Orekhov;Konstantine V. Pervushin;Alexander S. Arseniev

  • Spatial Structure of the Transmembrane Domain Heterodimer of ErbB1 and ErbB2 Receptor Tyrosine Kinases

    Konstantin S. Mineev;Eduard V. Bocharov;Yulia E. Pustovalova;Olga V. Bocharova

  • Cancer cell injury by cytotoxins from cobra venom is mediated through lysosomal damage

    Alexei V. Feofanov;George V. Sharonov;Maria V. Astapova;Dmitriy I. Rodionov

  • Lipid-protein nanodiscs for cell-free production of integral membrane proteins in a soluble and folded state: comparison with detergent micelles, bicelles and liposomes.

    E.N. Lyukmanova;Z.O. Shenkarev;N.F. Khabibullina;N.F. Khabibullina;G.S. Kopeina;G.S. Kopeina

  • Conformation and mode of membrane interaction in cyclotides. Spatial structure of kalata B1 bound to a dodecylphosphocholine micelle.

    Zakhar O. Shenkarev;Kirill D. Nadezhdin;Vladimir A. Sobol;Alexander G. Sobol

  • 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

  • From Structure and Dynamics of Protein L7/L12 to Molecular Switching in Ribosome

    Eduard V. Bocharov;Alexander G. Sobol;Konstantin V. Pavlov;Dmitry M. Korzhnev

  • NMR solution spatial structure of ‘short’ scorpion insectotoxin I5A

    Alexander S. Arseniev;Vladimir I. Kondakov;Vladimir N. Maiorov;Vladimir F. Bystrov

  • 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

  • Disulfide-stabilized Helical Hairpin Structure and Activity of a Novel Antifungal Peptide EcAMP1 from Seeds of Barnyard Grass (Echinochloa crus-galli)

    Svetlana B. Nolde;Alexander A. Vassilevski;Eugene A. Rogozhin;Nikolay A. Barinov

  • Structural insights into the proton pumping by unusual proteorhodopsin from nonmarine bacteria

    Ivan Gushchin;Pavel Chervakov;Pavel Kuzmichev;Alexander N. Popov

  • Three-dimensional structure of (1-71)bacterioopsin solubilized in methanol/chloroform and SDS micelles determined by 15N-1H heteronuclear NMR spectroscopy.

    Konstantine V. Pervushin;Vladislav Yu. Orekhov;Alexander I. Popov;Larisa Yu. Musina

  • NMR Structure and Action on Nicotinic Acetylcholine Receptors of Water-soluble Domain of Human LYNX1

    Ekaterina N. Lyukmanova;Zakhar O. Shenkarev;Mikhail A. Shulepko;Konstantin S. Mineev

Frequent Co-Authors

Roman G. Efremov
Roman G. Efremov Russian Academy of Sciences
Eugene V. Grishin
Eugene V. Grishin Russian Academy of Sciences
Sergey Lukyanov
Sergey Lukyanov Pirogov Russian National Research Medical University
Martin Billeter
Martin Billeter University of Gothenburg
Jan Tytgat
Jan Tytgat KU Leuven
Kazuyuki Akasaka
Kazuyuki Akasaka Kyoto Prefectural University of Medicine
Ferdinand Hucho
Ferdinand Hucho Freie Universität Berlin
Vladimir P. Skulachev
Vladimir P. Skulachev Lomonosov Moscow State University
Horst Kessler
Horst Kessler Technical University of Munich
Jonathan B. Cohen
Jonathan B. Cohen Harvard University

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