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    <timestamp>20261015053117953</timestamp>
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        <full_title>Molecular Sciences and Applications</full_title>
        <issn media_type="print">2944-9138</issn>
        <issn media_type="electronic">2732-9992</issn>
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      <journal_issue>
        <publication_date media_type="online">
          <month>05</month>
          <day>14</day>
          <year>2026</year>
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          <month>05</month>
          <day>14</day>
          <year>2026</year>
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          <volume>6</volume>
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        <titles>
          <title>A Multiphysics Model of Magnetically Enhanced ATP Hydrolysis in Ferromagnetic Nanosystems</title>
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        <contributors>
          <person_name sequence="first" contributor_role="author">
            <given_name>Paata J.</given_name>
            <surname>Kervalishvili</surname>
            <affiliations>
              <institution>
                <institution_name>Department of Physical Sciences, Tbilisi, GEORGIA</institution_name>
              </institution>
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        <jats:abstract xml:lang="en"><jats:p>This study develops a multiphysics framework for evaluating whether alternating magnetic fields (AMF) applied to Fe₃O₄ and MnFe₂O₄ nanoparticles can modify ATP hydrolysis through thermal, mechanical, and ion-mediated pathways. Rather than assigning a single phenomenological magnetic activation-energy reduction to all effects, the model starts from Arrhenius/Eyring kinetics and derives the observed rate change as the sum of a temperature-dependent contribution and explicitly defined non-thermal perturbations. The thermal term is constrained by the measured temperature history and nanoparticle specific absorption rate (SAR); the mechanical term is related to magnetic torque, hydrodynamic damping, and experimentally measurable particle motion; and the catalytic term is expressed through independently measurable Fe²⁺/Mn²⁺ concentrations and dose-response parameters. The available experimental observations reported in the original manuscript—2.5–3-fold enhancement of non-enzymatic hydrolysis under nanoparticle/AMF conditions, approximately 40% enhancement of Na⁺/K⁺-ATPase activity under stated isothermal conditions, and Raman/FTIR changes in phosphate-associated bands—are retained, but their interpretation is deliberately narrowed. In particular, the present data support rate enhancement under specified conditions and are consistent with multiple mechanisms; they do not, by themselves, establish a unique mechanical mechanism, nanoscale temperature gradients, or synergistic coupling. A mechanism-separation experimental matrix is therefore defined, together with quantitative spectroscopic observables and statistical requirements.</jats:p></jats:abstract>
        <publication_date media_type="online">
          <month>10</month>
          <day>15</day>
          <year>2026</year>
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        <publication_date media_type="print">
          <month>10</month>
          <day>15</day>
          <year>2026</year>
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        <pages>
          <first_page>114</first_page>
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          <item_number item_number_type="article_number">10</item_number>
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          <doi>10.37394/232023.2026.6.10</doi>
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