Academic Journal
Isolation and characterization of plant plasma membrane P-type H+-ATPase dimers.
| Τίτλος: | Isolation and characterization of plant plasma membrane P-type H+-ATPase dimers. |
|---|---|
| Συγγραφείς: | Malysenko E; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany., Günther Pomorski T; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany.; Department of Plant and Environmental Sciences, University of Copenhagen, 1871, Frederiksberg, Denmark., Justesen BH; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany. bo.justesen@ruhr-uni-bochum.de. |
| Πηγή: | Scientific reports [Sci Rep] 2026 Sep 15; Vol. 16 (1). Date of Electronic Publication: 2026 Sep 15. |
| Τύπος έκδοσης: | Journal Article; Research Support, Non-U.S. Gov't |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN: 2045-2322 (Electronic) Linking ISSN: 20452322 NLM ISO Abbreviation: Sci Rep Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: London : Nature Publishing Group, copyright 2011- |
| Ιατρικοί όροι (MeSH): | Proton-Translocating ATPases*/chemistry , Proton-Translocating ATPases*/isolation & purification , Proton-Translocating ATPases*/metabolism , Cell Membrane*/enzymology , Arabidopsis Proteins*/chemistry , Arabidopsis Proteins*/metabolism , Arabidopsis Proteins*/isolation & purification , Arabidopsis*/enzymology , Protein Multimerization*, Liposomes/metabolism ; Chromatography, Gel |
| Περίληψη: | Plant H⁺-ATPases are activated through tightly regulated hexameric assembly, relieving autoinhibition via displacement of a regulatory domain during the oligomerization process. Sub-hexameric assembly states also exist but their role in activity regulation remains elusive. To characterize sub-hexameric plant H⁺-ATPases, we isolated homo-oligomers of the H⁺-ATPases AHA2 and determined their sizes with size exclusion chromatography multi-angle light scattering. AHA2 predominantly presented as a monomer but also assembled into stable dimers and larger complexes. Activity assays on solubilized and liposome-reconstituted AHA2 monomers and dimers revealed that dimerization did not affect enzymatic activity, suggesting that AHA2 dimerization does not represent a separate regulatory pathway. Instead, AHA2 dimers may serve as reservoirs for rapid hexamer assembly, facilitating the dynamic regulation of protein activity. (© 2026. The Author(s).) |
| Competing Interests: | Declarations. Competing interests: The authors declare no competing interests. |
| References: | Annu Rev Plant Physiol Plant Mol Biol. 2001 Jun;52:817-845. (PMID: 11337417) Methods. 2008 Oct;46(2):73-82. (PMID: 18625320) Int J Mol Sci. 2023 Aug 23;24(17):. (PMID: 37685912) Annu Rev Biophys. 2011;40:243-66. (PMID: 21351879) J Biol Chem. 1982 Aug 25;257(16):9365-71. (PMID: 6213606) J Biol Chem. 1991 Dec 25;266(36):24439-45. (PMID: 1837022) Sci Adv. 2021 Nov 12;7(46):eabj5255. (PMID: 34757782) J Cell Sci. 2011 Aug 1;124(Pt 15):2515-9. (PMID: 21768325) J Biol Chem. 2002 Feb 22;277(8):6353-8. (PMID: 11744700) J Vis Exp. 2009 Aug 03;(30):. (PMID: 19684561) Methods Mol Biol. 2016;1377:105-9. (PMID: 26695026) FEBS Lett. 2025 Feb;599(4):545-558. (PMID: 39627950) J Biol Chem. 2000 Dec 15;275(50):39167-73. (PMID: 10995773) Protein Expr Purif. 1998 Feb;12(1):29-37. (PMID: 9473454) Curr Genet. 1987;12(2):105-10. (PMID: 2966684) Nature. 1953 Apr 25;171(4356):720-4. (PMID: 13054689) Front Physiol. 2017 Apr 11;8:202. (PMID: 28443028) Biochemistry. 1999 Jun 1;38(22):7227-34. (PMID: 10353834) J Biol Chem. 1998 Nov 6;273(45):30018-23. (PMID: 9792723) FEBS Lett. 1989 Apr 24;247(2):381-5. (PMID: 2523820) Mol Cell. 2007 Feb 9;25(3):427-40. (PMID: 17289589) Cold Spring Harb Perspect Biol. 2011 Jun 01;3(6):. (PMID: 21536707) J Biol Chem. 2013 Sep 13;288(37):26419-29. (PMID: 23836891) Biochim Biophys Acta. 1998 Jul 17;1372(2):261-71. (PMID: 9675306) Yeast. 1986 Sep;2(3):163-7. (PMID: 3333305) J Mol Biol. 2001 Jun 1;309(2):465-76. (PMID: 11371165) PLoS Genet. 2024 Jan 16;20(1):e1011121. (PMID: 38227612) Nature. 1954 May 1;173(4409):821-2. (PMID: 13165653) J Biol Chem. 1999 Dec 17;274(51):36774-80. (PMID: 10593986) Curr Protoc Protein Sci. 2014 Aug 01;77:29.10.1-29.10.30. (PMID: 25081744) J Biol Chem. 2015 Jun 26;290(26):16281-91. (PMID: 25971968) Science. 2016 Mar 25;351(6280):1469-73. (PMID: 27013734) Curr Res Struct Biol. 2021 Mar 16;3:85-94. (PMID: 34235488) Annu Rev Biochem. 2020 Jun 20;89:583-603. (PMID: 31874046) J Biol Chem. 2000 Jun 9;275(23):17762-70. (PMID: 10748153) J Biol Chem. 2001 Aug 10;276(32):29613-6. (PMID: 11404364) Nat Commun. 2021 Nov 8;12(1):6439. (PMID: 34750373) J Phys Condens Matter. 2018 Oct 31;30(43):435101. (PMID: 30280702) J Biol Chem. 2003 Oct 24;278(43):42266-72. (PMID: 12888557) Nature. 2007 Dec 13;450(7172):1111-4. (PMID: 18075595) Mol Membr Biol. 2011 Apr;28(3):171-81. (PMID: 21314479) Biochem Biophys Rep. 2018 Oct 30;16:122-129. (PMID: 30417130) Crystals (Basel). 2020 Feb;10(2):. (PMID: 32494365) J Biol Chem. 2010 Mar 5;285(10):7344-50. (PMID: 20068040) FEMS Yeast Res. 2015 Aug;15(5):fov030. (PMID: 26019146) Nat Protoc. 2018 May;13(5):1106-1120. (PMID: 29700483) Biochemistry. 2020 Jun 23;59(24):2210-2225. (PMID: 32459472) J Biol Chem. 2018 Nov 2;293(44):17095-17106. (PMID: 30217814) Pflugers Arch. 2009 Jan;457(3):645-55. (PMID: 18228034) Plant J. 1998 Mar;13(5):661-71. (PMID: 9681008) Sci Rep. 2014 Jun 06;4:5195. (PMID: 24903231) Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11675-80. (PMID: 16081536) Biophys J. 2011 May 4;100(9):2309-17. (PMID: 21539801) Plant J. 2010 Apr;62(2):291-301. (PMID: 20128881) Biochim Biophys Acta Mol Cell Res. 2024 Jan;1871(1):119600. (PMID: 37741574) |
| Contributed Indexing: | Keywords: Dimers; H+-ATPase; Membrane reconstitution; Oligomers; Proton pumping; SEC-MALS |
| Substance Nomenclature: | EC 3.6.3.14 (Proton-Translocating ATPases) 0 (Arabidopsis Proteins) 0 (Liposomes) EC 7.1.2.1 (AHA2 protein, Arabidopsis) |
| Entry Date(s): | Date Created: 20260916 Date Completed: 20260916 Latest Revision: 20260918 |
| Update Code: | 20260918 |
| PubMed Central ID: | PMC13578685 |
| DOI: | 10.1038/s41598-026-70970-z |
| PMID: | 42744987 |
| Βάση Δεδομένων: | MEDLINE |
| FullText | Links: – Type: other Url: https://resolver.ebsco.com:443/public/rma-ftfapi/ejs/direct?AccessToken=4DE9AD7B544D5E98B1DF&Show=Object Text: Availability: 0 CustomLinks: – Url: https://dx.doi.org/doi:10.1038/s41598-026-70970-z Name: EDS - Springer Nature Journals (s7799221) Category: fullText Text: View record at Springer |
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| Header | DbId: cmedm DbLabel: MEDLINE An: 42744987 AccessLevel: 3 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
| IllustrationInfo | |
| Items | – Name: Title Label: Title Group: Ti Data: Isolation and characterization of plant plasma membrane P-type H<superscript>+</superscript>-ATPase dimers. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AU" term="%22Malysenko+E%22">Malysenko E</searchLink>; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany.<br /><searchLink fieldCode="AU" term="%22Günther+Pomorski+T%22">Günther Pomorski T</searchLink>; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany.; Department of Plant and Environmental Sciences, University of Copenhagen, 1871, Frederiksberg, Denmark.<br /><searchLink fieldCode="AU" term="%22Justesen+BH%22">Justesen BH</searchLink>; Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, 44780, Bochum, Germany. bo.justesen@ruhr-uni-bochum.de. – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22101563288%22">Scientific reports</searchLink> [Sci Rep] 2026 Sep 15; Vol. 16 (1). <i>Date of Electronic Publication: </i>2026 Sep 15. – Name: TypePub Label: Publication Type Group: TypPub Data: Journal Article; Research Support, Non-U.S. Gov't – Name: Language Label: Language Group: Lang Data: English – Name: TitleSource Label: Journal Info Group: Src Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Nature+Publishing+Group%22">Nature Publishing Group </searchLink><i>Country of Publication: </i>England <i>NLM ID: </i>101563288 <i>Publication Model: </i>Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>2045-2322 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2220452322%22">20452322 </searchLink><i>NLM ISO Abbreviation: </i>Sci Rep <i>Subsets: </i>MEDLINE – Name: PublisherInfo Label: Imprint Name(s) Group: PubInfo Data: <i>Original Publication</i>: London : Nature Publishing Group, copyright 2011- – Name: SubjectMESH Label: MeSH Terms Group: Su Data: <searchLink fieldCode="MM" term="%22Proton-Translocating+ATPases%22">Proton-Translocating ATPases*</searchLink>/<searchLink fieldCode="MM" term="%22Proton-Translocating+ATPases+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Proton-Translocating+ATPases%22">Proton-Translocating ATPases*</searchLink>/<searchLink fieldCode="MM" term="%22Proton-Translocating+ATPases+isolation+%26+purification%22">isolation & purification</searchLink> <br /><searchLink fieldCode="MM" term="%22Proton-Translocating+ATPases%22">Proton-Translocating ATPases*</searchLink>/<searchLink fieldCode="MM" term="%22Proton-Translocating+ATPases+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Cell+Membrane%22">Cell Membrane*</searchLink>/<searchLink fieldCode="MM" term="%22Cell+Membrane+enzymology%22">enzymology</searchLink> <br /><searchLink fieldCode="MM" term="%22Arabidopsis+Proteins%22">Arabidopsis Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Arabidopsis+Proteins+chemistry%22">chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Arabidopsis+Proteins%22">Arabidopsis Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Arabidopsis+Proteins+metabolism%22">metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Arabidopsis+Proteins%22">Arabidopsis Proteins*</searchLink>/<searchLink fieldCode="MM" term="%22Arabidopsis+Proteins+isolation+%26+purification%22">isolation & purification</searchLink> <br /><searchLink fieldCode="MM" term="%22Arabidopsis%22">Arabidopsis*</searchLink>/<searchLink fieldCode="MM" term="%22Arabidopsis+enzymology%22">enzymology</searchLink> <br /><searchLink fieldCode="MM" term="%22Protein+Multimerization%22">Protein Multimerization*</searchLink><br /><searchLink fieldCode="MH" term="%22Liposomes%22">Liposomes</searchLink>/<searchLink fieldCode="MH" term="%22Liposomes+metabolism%22">metabolism</searchLink> ; <searchLink fieldCode="MH" term="%22Chromatography%2C+Gel%22">Chromatography, Gel</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Plant H⁺-ATPases are activated through tightly regulated hexameric assembly, relieving autoinhibition via displacement of a regulatory domain during the oligomerization process. Sub-hexameric assembly states also exist but their role in activity regulation remains elusive. To characterize sub-hexameric plant H⁺-ATPases, we isolated homo-oligomers of the H⁺-ATPases AHA2 and determined their sizes with size exclusion chromatography multi-angle light scattering. AHA2 predominantly presented as a monomer but also assembled into stable dimers and larger complexes. Activity assays on solubilized and liposome-reconstituted AHA2 monomers and dimers revealed that dimerization did not affect enzymatic activity, suggesting that AHA2 dimerization does not represent a separate regulatory pathway. Instead, AHA2 dimers may serve as reservoirs for rapid hexamer assembly, facilitating the dynamic regulation of protein activity.<br /> (© 2026. The Author(s).) – Name: Abstract Label: Competing Interests Group: Ab Data: Declarations. Competing interests: The authors declare no competing interests. – Name: Ref Label: References Group: RefInfo Data: Annu Rev Plant Physiol Plant Mol Biol. 2001 Jun;52:817-845. (PMID: <searchLink fieldCode="PM" term="%2211337417%22">11337417)</searchLink><br />Methods. 2008 Oct;46(2):73-82. (PMID: <searchLink fieldCode="PM" term="%2218625320%22">18625320)</searchLink><br />Int J Mol Sci. 2023 Aug 23;24(17):. (PMID: <searchLink fieldCode="PM" term="%2237685912%22">37685912)</searchLink><br />Annu Rev Biophys. 2011;40:243-66. (PMID: <searchLink fieldCode="PM" term="%2221351879%22">21351879)</searchLink><br />J Biol Chem. 1982 Aug 25;257(16):9365-71. (PMID: <searchLink fieldCode="PM" term="%226213606%22">6213606)</searchLink><br />J Biol Chem. 1991 Dec 25;266(36):24439-45. (PMID: <searchLink fieldCode="PM" term="%221837022%22">1837022)</searchLink><br />Sci Adv. 2021 Nov 12;7(46):eabj5255. (PMID: <searchLink fieldCode="PM" term="%2234757782%22">34757782)</searchLink><br />J Cell Sci. 2011 Aug 1;124(Pt 15):2515-9. (PMID: <searchLink fieldCode="PM" term="%2221768325%22">21768325)</searchLink><br />J Biol Chem. 2002 Feb 22;277(8):6353-8. (PMID: <searchLink fieldCode="PM" term="%2211744700%22">11744700)</searchLink><br />J Vis Exp. 2009 Aug 03;(30):. (PMID: <searchLink fieldCode="PM" term="%2219684561%22">19684561)</searchLink><br />Methods Mol Biol. 2016;1377:105-9. (PMID: <searchLink fieldCode="PM" term="%2226695026%22">26695026)</searchLink><br />FEBS Lett. 2025 Feb;599(4):545-558. (PMID: <searchLink fieldCode="PM" term="%2239627950%22">39627950)</searchLink><br />J Biol Chem. 2000 Dec 15;275(50):39167-73. (PMID: <searchLink fieldCode="PM" term="%2210995773%22">10995773)</searchLink><br />Protein Expr Purif. 1998 Feb;12(1):29-37. (PMID: <searchLink fieldCode="PM" term="%229473454%22">9473454)</searchLink><br />Curr Genet. 1987;12(2):105-10. (PMID: <searchLink fieldCode="PM" term="%222966684%22">2966684)</searchLink><br />Nature. 1953 Apr 25;171(4356):720-4. (PMID: <searchLink fieldCode="PM" term="%2213054689%22">13054689)</searchLink><br />Front Physiol. 2017 Apr 11;8:202. (PMID: <searchLink fieldCode="PM" term="%2228443028%22">28443028)</searchLink><br />Biochemistry. 1999 Jun 1;38(22):7227-34. (PMID: <searchLink fieldCode="PM" term="%2210353834%22">10353834)</searchLink><br />J Biol Chem. 1998 Nov 6;273(45):30018-23. (PMID: <searchLink fieldCode="PM" term="%229792723%22">9792723)</searchLink><br />FEBS Lett. 1989 Apr 24;247(2):381-5. (PMID: <searchLink fieldCode="PM" term="%222523820%22">2523820)</searchLink><br />Mol Cell. 2007 Feb 9;25(3):427-40. (PMID: <searchLink fieldCode="PM" term="%2217289589%22">17289589)</searchLink><br />Cold Spring Harb Perspect Biol. 2011 Jun 01;3(6):. (PMID: <searchLink fieldCode="PM" term="%2221536707%22">21536707)</searchLink><br />J Biol Chem. 2013 Sep 13;288(37):26419-29. (PMID: <searchLink fieldCode="PM" term="%2223836891%22">23836891)</searchLink><br />Biochim Biophys Acta. 1998 Jul 17;1372(2):261-71. (PMID: <searchLink fieldCode="PM" term="%229675306%22">9675306)</searchLink><br />Yeast. 1986 Sep;2(3):163-7. (PMID: <searchLink fieldCode="PM" term="%223333305%22">3333305)</searchLink><br />J Mol Biol. 2001 Jun 1;309(2):465-76. (PMID: <searchLink fieldCode="PM" term="%2211371165%22">11371165)</searchLink><br />PLoS Genet. 2024 Jan 16;20(1):e1011121. (PMID: <searchLink fieldCode="PM" term="%2238227612%22">38227612)</searchLink><br />Nature. 1954 May 1;173(4409):821-2. (PMID: <searchLink fieldCode="PM" term="%2213165653%22">13165653)</searchLink><br />J Biol Chem. 1999 Dec 17;274(51):36774-80. (PMID: <searchLink fieldCode="PM" term="%2210593986%22">10593986)</searchLink><br />Curr Protoc Protein Sci. 2014 Aug 01;77:29.10.1-29.10.30. (PMID: <searchLink fieldCode="PM" term="%2225081744%22">25081744)</searchLink><br />J Biol Chem. 2015 Jun 26;290(26):16281-91. (PMID: <searchLink fieldCode="PM" term="%2225971968%22">25971968)</searchLink><br />Science. 2016 Mar 25;351(6280):1469-73. (PMID: <searchLink fieldCode="PM" term="%2227013734%22">27013734)</searchLink><br />Curr Res Struct Biol. 2021 Mar 16;3:85-94. (PMID: <searchLink fieldCode="PM" term="%2234235488%22">34235488)</searchLink><br />Annu Rev Biochem. 2020 Jun 20;89:583-603. (PMID: <searchLink fieldCode="PM" term="%2231874046%22">31874046)</searchLink><br />J Biol Chem. 2000 Jun 9;275(23):17762-70. (PMID: <searchLink fieldCode="PM" term="%2210748153%22">10748153)</searchLink><br />J Biol Chem. 2001 Aug 10;276(32):29613-6. (PMID: <searchLink fieldCode="PM" term="%2211404364%22">11404364)</searchLink><br />Nat Commun. 2021 Nov 8;12(1):6439. (PMID: <searchLink fieldCode="PM" term="%2234750373%22">34750373)</searchLink><br />J Phys Condens Matter. 2018 Oct 31;30(43):435101. (PMID: <searchLink fieldCode="PM" term="%2230280702%22">30280702)</searchLink><br />J Biol Chem. 2003 Oct 24;278(43):42266-72. (PMID: <searchLink fieldCode="PM" term="%2212888557%22">12888557)</searchLink><br />Nature. 2007 Dec 13;450(7172):1111-4. (PMID: <searchLink fieldCode="PM" term="%2218075595%22">18075595)</searchLink><br />Mol Membr Biol. 2011 Apr;28(3):171-81. (PMID: <searchLink fieldCode="PM" term="%2221314479%22">21314479)</searchLink><br />Biochem Biophys Rep. 2018 Oct 30;16:122-129. (PMID: <searchLink fieldCode="PM" term="%2230417130%22">30417130)</searchLink><br />Crystals (Basel). 2020 Feb;10(2):. (PMID: <searchLink fieldCode="PM" term="%2232494365%22">32494365)</searchLink><br />J Biol Chem. 2010 Mar 5;285(10):7344-50. (PMID: <searchLink fieldCode="PM" term="%2220068040%22">20068040)</searchLink><br />FEMS Yeast Res. 2015 Aug;15(5):fov030. (PMID: <searchLink fieldCode="PM" term="%2226019146%22">26019146)</searchLink><br />Nat Protoc. 2018 May;13(5):1106-1120. (PMID: <searchLink fieldCode="PM" term="%2229700483%22">29700483)</searchLink><br />Biochemistry. 2020 Jun 23;59(24):2210-2225. (PMID: <searchLink fieldCode="PM" term="%2232459472%22">32459472)</searchLink><br />J Biol Chem. 2018 Nov 2;293(44):17095-17106. (PMID: <searchLink fieldCode="PM" term="%2230217814%22">30217814)</searchLink><br />Pflugers Arch. 2009 Jan;457(3):645-55. (PMID: <searchLink fieldCode="PM" term="%2218228034%22">18228034)</searchLink><br />Plant J. 1998 Mar;13(5):661-71. (PMID: <searchLink fieldCode="PM" term="%229681008%22">9681008)</searchLink><br />Sci Rep. 2014 Jun 06;4:5195. (PMID: <searchLink fieldCode="PM" term="%2224903231%22">24903231)</searchLink><br />Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11675-80. (PMID: <searchLink fieldCode="PM" term="%2216081536%22">16081536)</searchLink><br />Biophys J. 2011 May 4;100(9):2309-17. (PMID: <searchLink fieldCode="PM" term="%2221539801%22">21539801)</searchLink><br />Plant J. 2010 Apr;62(2):291-301. (PMID: <searchLink fieldCode="PM" term="%2220128881%22">20128881)</searchLink><br />Biochim Biophys Acta Mol Cell Res. 2024 Jan;1871(1):119600. (PMID: <searchLink fieldCode="PM" term="%2237741574%22">37741574)</searchLink> – Name: SubjectMinor Label: Contributed Indexing Group: Data: <i>Keywords: </i>Dimers; H+-ATPase; Membrane reconstitution; Oligomers; Proton pumping; SEC-MALS – Name: NumberCAS Label: Substance Nomenclature Group: ID Data: EC 3.6.3.14 (Proton-Translocating ATPases)<br />0 (Arabidopsis Proteins)<br />0 (Liposomes)<br />EC 7.1.2.1 (AHA2 protein, Arabidopsis) – Name: DateEntry Label: Entry Date(s) Group: Date Data: <i>Date Created: </i>20260916 <i>Date Completed: </i>20260916 <i>Latest Revision: </i>20260918 – Name: DateUpdate Label: Update Code Group: Date Data: 20260918 – Name: PubmedCentralID Label: PubMed Central ID Group: ID Data: PMC13578685 – Name: DOI Label: DOI Group: ID Data: 10.1038/s41598-026-70970-z – Name: AN Label: PMID Group: ID Data: 42744987 |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1038/s41598-026-70970-z Languages: – Code: eng Text: English Subjects: – SubjectFull: Liposomes metabolism Type: general – SubjectFull: Chromatography, Gel Type: general – SubjectFull: Proton-Translocating ATPases chemistry Type: general – SubjectFull: Proton-Translocating ATPases isolation & purification Type: general – SubjectFull: Proton-Translocating ATPases metabolism Type: general – SubjectFull: Cell Membrane enzymology Type: general – SubjectFull: Arabidopsis Proteins chemistry Type: general – SubjectFull: Arabidopsis Proteins metabolism Type: general – SubjectFull: Arabidopsis Proteins isolation & purification Type: general – SubjectFull: Arabidopsis enzymology Type: general – SubjectFull: Protein Multimerization Type: general Titles: – TitleFull: Isolation and characterization of plant plasma membrane P-type H+-ATPase dimers. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Malysenko E – PersonEntity: Name: NameFull: Günther Pomorski T – PersonEntity: Name: NameFull: Justesen BH IsPartOfRelationships: – BibEntity: Dates: – D: 15 M: 09 Text: 2026 Sep 15 Type: published Y: 2026 Identifiers: – Type: issn-electronic Value: 2045-2322 Numbering: – Type: volume Value: 16 – Type: issue Value: 1 Titles: – TitleFull: Scientific reports Type: main |
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