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Cooperativity in septin polymerization is tunable by ionic strength and membrane adsorption.

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Title: Cooperativity in septin polymerization is tunable by ionic strength and membrane adsorption.
Authors: Vogt EJD; Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina; Department of Cell Biology, Duke University Medical School, Durham, North Carolina., Seim I; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany., Snead WT; Department of Cell Biology, Duke University Medical School, Durham, North Carolina., Curtis BN; Department of Cell Biology, Duke University Medical School, Durham, North Carolina; Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina., Gladfelter AS; Department of Cell Biology, Duke University Medical School, Durham, North Carolina. Electronic address: asg3@duke.edu.
Source: Biophysical journal [Biophys J] 2026 Jun 16; Vol. 125 (12), pp. 2964-2977. Date of Electronic Publication: 2025 Aug 07.
Publication Type: Journal Article
Journal Info: Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1542-0086 (Electronic) Linking ISSN: 00063495 NLM ISO Abbreviation: Biophys J Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: Cooperativity in septin polymerization is tunable by ionic strength and membrane adsorption.
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  Data: <searchLink fieldCode="AU" term="%22Vogt+EJD%22">Vogt EJD</searchLink>; Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina; Department of Cell Biology, Duke University Medical School, Durham, North Carolina.<br /><searchLink fieldCode="AU" term="%22Seim+I%22">Seim I</searchLink>; Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany.<br /><searchLink fieldCode="AU" term="%22Snead+WT%22">Snead WT</searchLink>; Department of Cell Biology, Duke University Medical School, Durham, North Carolina.<br /><searchLink fieldCode="AU" term="%22Curtis+BN%22">Curtis BN</searchLink>; Department of Cell Biology, Duke University Medical School, Durham, North Carolina; Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.<br /><searchLink fieldCode="AU" term="%22Gladfelter+AS%22">Gladfelter AS</searchLink>; Department of Cell Biology, Duke University Medical School, Durham, North Carolina. Electronic address: asg3@duke.edu.
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  Data: <searchLink fieldCode="JN" term="%220370626%22">Biophysical journal</searchLink> [Biophys J] 2026 Jun 16; Vol. 125 (12), pp. 2964-2977. <i>Date of Electronic Publication: </i>2025 Aug 07.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Cell+Press%22">Cell Press </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>0370626 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1542-0086 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200063495%22">00063495 </searchLink><i>NLM ISO Abbreviation: </i>Biophys J <i>Subsets: </i>MEDLINE
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        Value: 10.1016/j.bpj.2025.08.005
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      – Code: eng
        Text: English
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      – TitleFull: Cooperativity in septin polymerization is tunable by ionic strength and membrane adsorption.
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              Text: 2026 Jun 16
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