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  1. Article ; Online: The triplet puzzle theory indicates extensive formation of heteromers between opioid and chemokine receptor subtypes.

    Tarakanov, Alexander O / Fuxe, Kjell

    Journal of neural transmission (Vienna, Austria : 1996)

    2015  Volume 122, Issue 11, Page(s) 1509–1514

    Abstract: Biochemical studies had previously demonstrated examples of heteromerization between opioid and chemokine receptors. Based on the triplet puzzle theory, it has been discovered that opioid receptors are structurally more closely related to chemokine ... ...

    Abstract Biochemical studies had previously demonstrated examples of heteromerization between opioid and chemokine receptors. Based on the triplet puzzle theory, it has been discovered that opioid receptors are structurally more closely related to chemokine receptors than to other class A G-protein-coupled receptors. Their similarity is established in terms of the number of triplet homologies Asn-Leu-Ala, Thr-Leu-Pro, and Tyr-Ala-Phe in the amino acid code of extensive numbers of members of these two receptor groups. Such widespread similarities probably mean that many opioid and chemokine receptor subtypes utilize some of these mutual triplets to form heteromers. The findings underline that heteromerization among these two receptor groups can represent a major general mechanism for significant interactions between opioid peptides and chemokines in pain and neuroinflammation within the neural-glial networks of the CNS including immune cells.
    MeSH term(s) Amino Acid Sequence ; Humans ; Models, Molecular ; Receptors, Chemokine/genetics ; Receptors, Chemokine/metabolism ; Receptors, Opioid/genetics ; Receptors, Opioid/metabolism
    Chemical Substances Receptors, Chemokine ; Receptors, Opioid
    Language English
    Publishing date 2015-11
    Publishing country Austria
    Document type Journal Article
    ZDB-ID 184163-4
    ISSN 1435-1463 ; 0300-9564
    ISSN (online) 1435-1463
    ISSN 0300-9564
    DOI 10.1007/s00702-015-1421-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Glutamate heteroreceptor complexes in the brain.

    Borroto-Escuela, Dasiel O / Tarakanov, Alexander O / Brito, Ismel / Fuxe, Kjell

    Pharmacological reports : PR

    2018  Volume 70, Issue 5, Page(s) 936–950

    Abstract: The existence of mGluR, NMDAR, AMPAR and putative KAR heteroreceptor complexes in synaptic and extrasynaptic regions of brain glutamate synapses represents a major integrative mechanism. Our aim in the current article is to analyze if the formation of ... ...

    Abstract The existence of mGluR, NMDAR, AMPAR and putative KAR heteroreceptor complexes in synaptic and extrasynaptic regions of brain glutamate synapses represents a major integrative mechanism. Our aim in the current article is to analyze if the formation of the different types glutamate hetereceptor complexes involves the contribution of triplet amino acid homologies (protriplets) in a postulated receptor interface based on the triplet puzzle theory. Seven main sets (lists) of receptor pairs in databases were used containing various sets (lists) of human receptor heteromers and nonheteromers obtained from the available scientific publications including the publically available GPCR-hetnet database. Brain mGluR1-mGluR5 and mGluR2-mGluR4 isoreceptor complexes were demonstrated with a predominant extrasynaptic localization at a post- and prejunctional localization. The existence of putative mGluR4-mGluR7 heteroreceptor complexes in the basal ganglia is proposed. Metabotropic glutamate receptor subtypes also participated in the formation of a large number of heteroreceptor complexes like mGluR1-A1R, mGluR5-A2AR, mGluR5-D2R and D2R-A2AR-mGluR5, located in relation to glutamate synapses, especially in the basal ganglia. A putative mGluR1-GABAB1/2 heterocomplex may also exist. NMDAR heteroreceptor complexes were also demonstrated as a fundamental integrative mechanism in the glutamate synapse and its extrasynaptic membranes. It represented fundamental work on inter alia NMDAR-mGluR5, NMDAR-D1R and NMDAR-D2R heteroreceptor complexes involving both antagonistic and facilitatory allosteric receptor-receptor interactions. As to AMPA receptors, a heterocomplex was found for the interaction between IFNgR1 and the AMPAR mediated via the subunit GluA1 which may be of relevance for neuroinflammation. AMPAR-D2R heteroreceptor complexes were also demonstrated. Besides glutamate heteroreceptor complexes and their allosteric receptor-receptor interactions, a significant mechanism for the functional crosstalk can also be phosphorylation and/or reorganization of adapter proteins with dynamic binding to the two receptors modulating the allosteric receptor mechanism.
    MeSH term(s) Animals ; Brain/metabolism ; Humans ; Multiprotein Complexes/metabolism ; Protein Isoforms/metabolism ; Receptors, Glutamate/metabolism ; Sequence Homology, Amino Acid
    Chemical Substances Multiprotein Complexes ; Protein Isoforms ; Receptors, Glutamate
    Language English
    Publishing date 2018-04-11
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 2186248-5
    ISSN 1734-1140
    ISSN 1734-1140
    DOI 10.1016/j.pharep.2018.04.002
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  3. Article: IL1R2, CCR2, and CXCR4 May Form Heteroreceptor Complexes with NMDAR and D2R: Relevance for Schizophrenia.

    Borroto-Escuela, Dasiel O / Tarakanov, Alexander O / Bechter, Karl / Fuxe, Kjell

    Frontiers in psychiatry

    2017  Volume 8, Page(s) 24

    Abstract: The mild neuroinflammation hypothesis of schizophrenia was introduced by Bechter in 2001. It has been hypothesized that a hypofunction of glutamatergic ... ...

    Abstract The mild neuroinflammation hypothesis of schizophrenia was introduced by Bechter in 2001. It has been hypothesized that a hypofunction of glutamatergic signaling
    Language English
    Publishing date 2017-02-15
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2564218-2
    ISSN 1664-0640
    ISSN 1664-0640
    DOI 10.3389/fpsyt.2017.00024
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: FGFR1-5-HT1A Heteroreceptor Complexes: Implications for Understanding and Treating Major Depression.

    Borroto-Escuela, Dasiel O / Tarakanov, Alexander O / Fuxe, Kjell

    Trends in neurosciences

    2016  Volume 39, Issue 1, Page(s) 5–15

    Abstract: The serotonin and neurotrophic factor hypotheses of depression are well known. The discovery of brain fibroblast growth factor receptor 1 (FGFR1)-5 hydroxytryptamine receptor 1A (5-HT1A) heteroreceptor complexes, and their enhancement of neuroplasticity, ...

    Abstract The serotonin and neurotrophic factor hypotheses of depression are well known. The discovery of brain fibroblast growth factor receptor 1 (FGFR1)-5 hydroxytryptamine receptor 1A (5-HT1A) heteroreceptor complexes, and their enhancement of neuroplasticity, offers an integration of these hypotheses at the molecular level. They were first described in the hippocampus and later in midbrain 5-HT neurons, where these heterocomplexes are enriched in 5-HT1A autoreceptors. Combined FGF2 and 5-HT1A agonist treatment increased the formation of these heterocomplexes and the facilitatory allosteric receptor-receptor interactions within them led to the enhancement of FGFR1 signaling and was associated with the development of antidepressant effects. We discuss these findings with regard to a theory of motifs critically involved in these interactions and suggest that these complexes represent novel targets for antidepressants.
    MeSH term(s) Animals ; Depressive Disorder, Major/drug therapy ; Depressive Disorder, Major/metabolism ; Humans ; Neurosciences/trends ; Receptor, Fibroblast Growth Factor, Type 1/metabolism ; Receptor, Serotonin, 5-HT1A/metabolism
    Chemical Substances Receptor, Serotonin, 5-HT1A (112692-38-3) ; Receptor, Fibroblast Growth Factor, Type 1 (EC 2.7.10.1)
    Language English
    Publishing date 2016-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 282488-7
    ISSN 1878-108X ; 0378-5912 ; 0166-2236
    ISSN (online) 1878-108X
    ISSN 0378-5912 ; 0166-2236
    DOI 10.1016/j.tins.2015.11.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Integrin triplets of marine sponges in the murine and human MHCI-CD8 interface and in the interface of human neural receptor heteromers and subunits.

    Tarakanov, Alexander O / Fuxe, Kjell G

    SpringerPlus

    2013  Volume 2, Issue 1, Page(s) 128

    Abstract: Based on our theory, main triplets of amino acid residues have been discovered in cell-adhesion receptors (integrins) of marine sponges, which participate as homologies in the interface between two major immune molecules, MHC class I (MHCI) and CD8αβ. ... ...

    Abstract Based on our theory, main triplets of amino acid residues have been discovered in cell-adhesion receptors (integrins) of marine sponges, which participate as homologies in the interface between two major immune molecules, MHC class I (MHCI) and CD8αβ. They appear as homologies also in several human neural receptor heteromers and subunits. The obtained results probably mean that neural and immune receptors also utilize these structural integrin triplets to form heteromers and ion channels, which are required for a tuned and integrated intracellular and intercellular communication and a communication between cells and the extracellular matrix with an origin in sponges, the oldest multicellular animals.
    Language English
    Publishing date 2013-03-22
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2661116-8
    ISSN 2193-1801
    ISSN 2193-1801
    DOI 10.1186/2193-1801-2-128
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The triplet puzzle of homologies in receptor heteromers exists also in other types of protein-protein interactions.

    Tarakanov, Alexander O / Fuxe, Kjell G

    Journal of molecular neuroscience : MN

    2011  Volume 44, Issue 3, Page(s) 173–177

    Abstract: Based on our theory, we point out main triplets of amino acid residues in the GABAB1 receptor, found in the central and peripheral nervous system, which seem to be critical for both receptor heterodimerization and chemokine binding. The obtained results ... ...

    Abstract Based on our theory, we point out main triplets of amino acid residues in the GABAB1 receptor, found in the central and peripheral nervous system, which seem to be critical for both receptor heterodimerization and chemokine binding. The obtained results suggest that these triplets may "guide-and-clasp" protein-protein interactions playing a role, e.g., in neuroinflammation disorders.
    MeSH term(s) Amino Acid Motifs ; Animals ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Interaction Domains and Motifs/genetics ; Protein Isoforms/chemistry ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Multimerization ; Receptors, GABA-B/chemistry ; Receptors, GABA-B/genetics ; Receptors, GABA-B/metabolism ; Sequence Alignment
    Chemical Substances Protein Isoforms ; Receptors, GABA-B
    Language English
    Publishing date 2011-03-18
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1043392-2
    ISSN 1559-1166 ; 0895-8696
    ISSN (online) 1559-1166
    ISSN 0895-8696
    DOI 10.1007/s12031-011-9511-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Carbon nanotubes towards medicinal biochips.

    Tarakanov, Alexander O / Goncharova, Larisa B / Tarakanov, Yury A

    Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology

    2010  Volume 2, Issue 1, Page(s) 1–10

    Abstract: This overview focuses on the recent advances in carbon nanotube (CNT)-based biochips and tries to clarify their potential for modern molecular medicine. ...

    Abstract This overview focuses on the recent advances in carbon nanotube (CNT)-based biochips and tries to clarify their potential for modern molecular medicine.
    MeSH term(s) Animals ; Biomedical Technology/methods ; Drug Delivery Systems/methods ; Humans ; Microchip Analytical Procedures/methods ; Nanotubes, Carbon
    Chemical Substances Nanotubes, Carbon
    Language English
    Publishing date 2010-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2502698-7
    ISSN 1939-0041 ; 1939-5116
    ISSN (online) 1939-0041
    ISSN 1939-5116
    DOI 10.1002/wnan.69
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  8. Article ; Online: Passive microwave radiometry in biomedical studies.

    Goryanin, Igor / Karbainov, Sergey / Shevelev, Oleg / Tarakanov, Alexander / Redpath, Keith / Vesnin, Sergey / Ivanov, Yuri

    Drug discovery today

    2020  Volume 25, Issue 4, Page(s) 757–763

    Abstract: Passive microwave radiometry (MWR) measures natural emissions in the range 1-10GHz from proteins, cells, organs and the whole human body. The intensity of intrinsic emission is determined by biochemical and biophysical processes. The nature of this ... ...

    Abstract Passive microwave radiometry (MWR) measures natural emissions in the range 1-10GHz from proteins, cells, organs and the whole human body. The intensity of intrinsic emission is determined by biochemical and biophysical processes. The nature of this process is still not very well known. Infrared thermography (IRT) can detect emission several microns deep (skin temperature), whereas MWR allows detection of thermal abnormalities down to several centimeters (internal or deep temperature). MWR is noninvasive and inexpensive. It requires neither fluorescent nor radioactive labels, nor ionizing or other radiation. MWR can be used in early drug discovery as well as preclinical and clinical studies.
    MeSH term(s) Animals ; Body Temperature/physiology ; Clinical Trials as Topic/methods ; Drug Discovery/methods ; Drug Evaluation, Preclinical/methods ; Humans ; Microwaves ; Radiometry/methods ; Thermography/methods
    Language English
    Publishing date 2020-01-28
    Publishing country England
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1324988-5
    ISSN 1878-5832 ; 1359-6446
    ISSN (online) 1878-5832
    ISSN 1359-6446
    DOI 10.1016/j.drudis.2020.01.016
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Cell-cell nanotubes: Tunneling through several types of synapses.

    Tarakanov, Alexander O / Goncharova, Larisa B

    Communicative & integrative biology

    2009  Volume 2, Issue 4, Page(s) 359–361

    Abstract: Nanotube can be generally seen as a nanoscale cylindrical structure. Membrane (or tunneling) nanotube (TNT) is a cytoplasmic tunnel between two cells. Such direct cell-cell channel is used for a physical transport of biochemical cargo, whereas ... ...

    Abstract Nanotube can be generally seen as a nanoscale cylindrical structure. Membrane (or tunneling) nanotube (TNT) is a cytoplasmic tunnel between two cells. Such direct cell-cell channel is used for a physical transport of biochemical cargo, whereas nanotubular networks between cells may be a novel principle of communicative and integrative biology. Recently, TNTs and their networks were discovered in plant cells and then they were reported also in animal cells. Just the reverse, a notion of plant synapse has been also proposed only recently, long after the corresponding notion of neuronal synapse in animals. However, both TNTs and synapses seem to be closely related and evolutionary conserved structures through different types of cells. Accordingly, this mini-review aims to demonstrate that TNTs may represent one of the deep functional similarities between neuronal, immune, viral and plant synapses.
    Language English
    Publishing date 2009-08-26
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2451097-X
    ISSN 1942-0889 ; 1942-0889
    ISSN (online) 1942-0889
    ISSN 1942-0889
    DOI 10.4161/cib.2.4.8289
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  10. Article ; Online: Triplet puzzle: homologies of receptor heteromers.

    Tarakanov, Alexander O / Fuxe, Kjell G

    Journal of molecular neuroscience : MN

    2009  Volume 41, Issue 2, Page(s) 294–303

    Abstract: Based on a mathematical approach, we deduce a set of triplet homologies that may be responsible for receptor-receptor interactions. We show how such triplets of amino acid residues and their 'teams' may be utilized to construct a kind of code that ... ...

    Abstract Based on a mathematical approach, we deduce a set of triplet homologies that may be responsible for receptor-receptor interactions. We show how such triplets of amino acid residues and their 'teams' may be utilized to construct a kind of code that determines (and/or predicts) which receptors should or should not form heterodimers. Based on the obtained results, we propose a 'guide-and-clasp' manner for receptor-receptor interactions where 'adhesive guides' might be the triplet homologies. We also demonstrate their relevance to protein-protein interactions and mention possible implications for novel pharmacological targets and strategies for treatment of diseases, e.g. neuroinflammatory diseases.
    MeSH term(s) Amino Acid Sequence ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Models, Molecular ; Models, Theoretical ; Molecular Sequence Data ; Protein Multimerization ; Protein Structure, Quaternary
    Chemical Substances Membrane Proteins
    Language English
    Publishing date 2009-12-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1043392-2
    ISSN 1559-1166 ; 0895-8696
    ISSN (online) 1559-1166
    ISSN 0895-8696
    DOI 10.1007/s12031-009-9313-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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