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In silico analysis of the γ-carbonic anhydrase EcoCAγ from Enterobacteria: assessing the role of the 72-residue N-terminal extension.

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Title: In silico analysis of the γ-carbonic anhydrase EcoCAγ from Enterobacteria: assessing the role of the 72-residue N-terminal extension.
Authors: Stoliarskaia MY; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation.; Institute of Cyber Intelligence Systems, National Research Nuclear University MEPhI, Moscow, Russian Federation., Nikonov OS; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation., Borisevich SS; Institute of Cyber Intelligence Systems, National Research Nuclear University MEPhI, Moscow, Russian Federation.; Ufa Institute of Chemistry, Ufa Federal Research Centre, Russian Academy of Sciences, Ufa, Russian Federation.
Source: Journal of biomolecular structure & dynamics [J Biomol Struct Dyn] 2026 May; Vol. 44 (8), pp. 4057-4071. Date of Electronic Publication: 2025 Nov 14.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
Journal Info: Publisher: Taylor & Francis Country of Publication: England NLM ID: 8404176 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1538-0254 (Electronic) Linking ISSN: 07391102 NLM ISO Abbreviation: J Biomol Struct Dyn Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: In silico analysis of the γ-carbonic anhydrase EcoCAγ from Enterobacteria: assessing the role of the 72-residue N-terminal extension.
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  Data: <searchLink fieldCode="AU" term="%22Stoliarskaia+MY%22">Stoliarskaia MY</searchLink>; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation.; Institute of Cyber Intelligence Systems, National Research Nuclear University MEPhI, Moscow, Russian Federation.<br /><searchLink fieldCode="AU" term="%22Nikonov+OS%22">Nikonov OS</searchLink>; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation.<br /><searchLink fieldCode="AU" term="%22Borisevich+SS%22">Borisevich SS</searchLink>; Institute of Cyber Intelligence Systems, National Research Nuclear University MEPhI, Moscow, Russian Federation.; Ufa Institute of Chemistry, Ufa Federal Research Centre, Russian Academy of Sciences, Ufa, Russian Federation.
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  Data: <searchLink fieldCode="JN" term="%228404176%22">Journal of biomolecular structure & dynamics</searchLink> [J Biomol Struct Dyn] 2026 May; Vol. 44 (8), pp. 4057-4071. <i>Date of Electronic Publication: </i>2025 Nov 14.
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  Data: Journal Article; Research Support, Non-U.S. Gov't
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Taylor+%26+Francis%22">Taylor & Francis </searchLink><i>Country of Publication: </i>England <i>NLM ID: </i>8404176 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1538-0254 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2207391102%22">07391102 </searchLink><i>NLM ISO Abbreviation: </i>J Biomol Struct Dyn <i>Subsets: </i>MEDLINE
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      – Type: doi
        Value: 10.1080/07391102.2025.2586041
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      – Code: eng
        Text: English
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      Pagination:
        StartPage: 4057
    Titles:
      – TitleFull: In silico analysis of the γ-carbonic anhydrase EcoCAγ from Enterobacteria: assessing the role of the 72-residue N-terminal extension.
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            NameFull: Stoliarskaia MY
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            NameFull: Nikonov OS
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            – D: 01
              M: 05
              Text: 2026 May
              Type: published
              Y: 2026
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              Value: 44
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