ATP synthase F1 subunits recruited to centromeres by CENP-A are required for male meiosis
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2041-1723
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
-
online resource.
- Bibliographic citation
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ATP synthase F1 subunits recruited to centromeres by CENP-A are required for male meiosis ; volume:9 ; number:1 ; day:13 ; month:7 ; year:2018 ; pages:1-11 ; date:12.2018
Nature Communications ; 9, Heft 1 (13.7.2018), 1-11, 12.2018
- Classification
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Biowissenschaften, Biologie
- Creator
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Collins, Caitríona M.
- Contributor
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Malacrida, Beatrice
Burke, Colin
Kiely, Patrick A.
Dunleavy, Elaine M.
SpringerLink (Online service)
- DOI
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10.1038/s41467-018-05093-9
- URN
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urn:nbn:de:101:1-2018091320410929280654
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:28 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Collins, Caitríona M.
- Malacrida, Beatrice
- Burke, Colin
- Kiely, Patrick A.
- Dunleavy, Elaine M.
- SpringerLink (Online service)
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Role of Kir6.2 subunits of ATP-sensitive potassium channels in endotoxemia-induced cardiac dysfunction
Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
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Meiosis through three centuries
Expression of the cyanobacterial FoF1 ATP synthase regulator AtpΘ depends on small DNA-binding proteins and differential mRNA stability : = Expression of the cyanobacterial FoF1 ATP synthase regulator Atp[Theta] depends on small DNA-binding proteins and differential mRNA stability
Structural and functional studies of the central stalk subunits of the ATP synthase from Escherichia coli
F1
F1
Meiosis
Chromosome behavior during meiosis in pollen mother cells from Saccharum officinarum × Erianthus arundinaceus F1 hybrids
ATP-Synthase und F1-ATPase [F-ATPase] des thermoacidophilen Archaebakteriums Sulfolobus acidocaldarius
Role of Kir6.2 subunits of ATP-sensitive potassium channels in endotoxemia-induced cardiac dysfunction
Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
Struktur- und Funktionsuntersuchungen an den Membranproteinen Bacteriorhodopsin und Chloroplasten-FoF1-ATP-Synthase
Testis-specific ATP synthase peripheral stalk subunits required for tissue-specific mitochondrial morphogenesis in Drosophila
Meiosis through three centuries
Expression of the cyanobacterial FoF1 ATP synthase regulator AtpΘ depends on small DNA-binding proteins and differential mRNA stability : = Expression of the cyanobacterial FoF1 ATP synthase regulator Atp[Theta] depends on small DNA-binding proteins and differential mRNA stability
Structural and functional studies of the central stalk subunits of the ATP synthase from Escherichia coli
F1
F1
Meiosis
Chromosome behavior during meiosis in pollen mother cells from Saccharum officinarum × Erianthus arundinaceus F1 hybrids
ATP-Synthase und F1-ATPase [F-ATPase] des thermoacidophilen Archaebakteriums Sulfolobus acidocaldarius
Role of Kir6.2 subunits of ATP-sensitive potassium channels in endotoxemia-induced cardiac dysfunction
Peptides induce ATP hydrolysis at both subunits of the transporter associated with antigen processing
Struktur- und Funktionsuntersuchungen an den Membranproteinen Bacteriorhodopsin und Chloroplasten-FoF1-ATP-Synthase
Testis-specific ATP synthase peripheral stalk subunits required for tissue-specific mitochondrial morphogenesis in Drosophila
Meiosis through three centuries
Expression of the cyanobacterial FoF1 ATP synthase regulator AtpΘ depends on small DNA-binding proteins and differential mRNA stability : = Expression of the cyanobacterial FoF1 ATP synthase regulator Atp[Theta] depends on small DNA-binding proteins and differential mRNA stability
Structural and functional studies of the central stalk subunits of the ATP synthase from Escherichia coli
F1