A. A. Ivanov

Emory University, Atlanta, Georgia, United States

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Publications (8)4.7 Total impact

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    ABSTRACT: Crystallization of N-[(8R)-2-methoxy-5,6,7,8,9,10-hexahydro-6,9-methanocyclohepta[b]indol-8-yl]acetamide was accompanied by oxidation at the C5a–C10a bond with formation of N-[(5S)-10-methoxy-2,8-dioxo-1,2,3,4,5,6,7,8-octahydro-3,6-methano-1-benzazecin-5-yl]acetamide whose structure was determined by X-ray analysis. Docking of this compound into melatonin-binding pocket of MT1A receptor was simulated by computer-assisted molecular modeling.
    No preview · Article · Apr 2012 · Russian Journal of Organic Chemistry
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    ABSTRACT: 2-(endo-7-Hydroxybicyclo[3.3.1]non-exo-3-ylmethyl)propane-1,3-diol was synthesized in seven steps starting from endo-7-hydroxybicyclo[3.3.1]nonane-exo-3-carboxylic acid. The title compound attracts interest as intermediate product for the synthesis of potential tubulin ligands.
    No preview · Article · Aug 2008 · Russian Journal of Organic Chemistry
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    ABSTRACT: The epiphysis hormone melatonin plays a key role in the regulation of circadian rhythms of mammals, as well as in the functioning of the cardiovascular, immune, and digestive systems and retina [1]. The involvement of melatonin in the regulation of a great number of physiological processes has determined its use as a drug. However, when used as a drug, melatonin has certain disadvantages—a short degradation period and low solubility (which causes difficulties with preparation of the pharmaceutical dosage form), as well as a too broad spectrum of action. In view of this, the search for melatonin analogs that would be deprived of the above-listed disadvantages is very important. For this purpose, it is necessary to study the characteristic features of the structure of melatonin receptors and the main mechanisms of ligand‐receptor interactions. Melatonin receptors belong to the rhodopsin family of G protein-coupled receptors. Because the representatives of this family are located in the lipid bilayer of cell membrane, crystallization of these receptors and experimental study of their structure are hampered. Xray data were obtained for only one representative of this family, rhodopsin [2]. Since all receptors of the rhodopsin family have a similar structure, the most effective way of constructing molecular models of melatonin receptors is modeling based on their homology with rhodopsin. Two subtypes (Mel1a and Mel1b) of human melatonin receptors are known. Similar to other representatives of the rhodopsin family, the melatonin receptor consists of seven transmembrane α -helices, three intracellular and three extracellular hydrophilic loops, as well as an intracellular and an extracellular terminal domains.
    Full-text · Article · Jul 2005 · Doklady Biochemistry and Biophysics
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    ABSTRACT: An improved strategy of quantitative structure-property relationship (QSPR) studies of diverse and inhomogeneous organic datasets has been proposed. A molecular connectivity term was successively corrected for different structural features encoded in fragmental descriptors. The so-called solvation index 1chis (a weighted Randic index) was used as a "leading" variable and standardized molecular fragments were employed as "corrective" class-specific variables. Performance of the new approach was illustrated by modelling a dataset of experimental normal boiling points of 833 organic compounds belonging to 20 structural classes. Firstly, separate QSPR models were derived for each class and for eight groups of structurally similar classes. Finally, a general model formed by combining all the classes together was derived (r2=0.957, s=12.9degreesC). The strategy outlined can find application in QSPR analyses of massive, highly diverse databases of organic compounds.
    No preview · Article · Jul 2005 · SAR and QSAR in Environmental Research
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    Full-text · Article · Jan 2004 · Doklady Biochemistry and Biophysics
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    A A Ivanov · I I Baskin · V A Palyulin · N S Zefirov

    Full-text · Article · Mar 2003 · Doklady Biochemistry and Biophysics
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    A A Ivanov · I I Baskin · V A Palyulin · N S Zefirov
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    ABSTRACT: Adenosine receptors (classified as G-protein-coupled receptors) are present in the majority of human and mammalian cells and tissues and are involved in many key biological processes. Depending on their biochemical and pharmacologic properties, four subtypes of adenosine receptors (A1, A2a, A2b, and A3) are distinguished. All of them contain a typical transmembrane domain formed by seven α helices linked pairwise with three extracellular and three intracellular hydrophilic loops. The ligand-binding site of the receptor is located inside the transmembrane domain [1]. It is known that activation of the A1 and A3 receptors decreases the cAMP level, whereas activation of the A2a and A2b subtypes increases it. In addition, stimulation of A1 receptors causes activation of potassium channels and inhibition of calcium channels [2]. The receptors ligands of adenosine are widely used in pharmacology and medicine for treatment of some psychoneurological and cardiovascular diseases [3]. Although numerous agonists and antagonists of adenosine receptors are currently known [4], the majority of them do not exhibit sufficient selectivity and efficiency. In addition, no model of adenosine receptors containing not only the transmembrane α helices, but also the hydrophilic loops, has been designed thus far. In view of this, a thorough study of the structure of adenosine receptors and the mechanisms of ligand binding to the receptors, as well as the search for new highly selective and efficient ligands of these receptors is now a topical problem. The purpose of this work was to design a molecular model of the human A1 adenosine receptor and to study the mechanisms of selective binding of ligands to this receptor. Adenosine receptors are membrane proteins; they are difficult to crystallize and study by X-ray analysis. For this reason, the structure of these receptors is studied using molecular modeling based on homology with a template protein (usually, rhodopsin) that is also G-protein-coupled and that was studied by X-ray analysis [5]. To identify the amino acids forming each of the seven transmembrane α helices of the A1 receptor, we performed multiple alignment of the amino acid sequences of the four known subtypes of adenosine receptors and rhodopsin: TM1
    Full-text · Article · Sep 2002 · Doklady Biochemistry and Biophysics

  • No preview · Article · Dec 2001 · Doklady Chemistry

Publication Stats

47 Citations
4.70 Total Impact Points


  • 2012
    • Emory University
      Atlanta, Georgia, United States
  • 2008
    • Russian Academy of Sciences
      • Institute of Physiologically Active Substances
      Moskva, Moscow, Russia
  • 2001-2005
    • Moscow State Forest University
      Mytishi, Moskovskaya, Russia