AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2045-2322
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules ; volume:8 ; number:1 ; day:19 ; month:10 ; year:2018 ; pages:1-10 ; date:12.2018
Scientific reports ; 8, Heft 1 (19.10.2018), 1-10, 12.2018
- Classification
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Biowissenschaften, Biologie
- Creator
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Yano, Tomoki
- Contributor
-
Torisawa, Takayuki
Oiwa, Kazuhiro
Tsukita, Sachiko
SpringerLink (Online service)
- DOI
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10.1038/s41598-018-33418-7
- URN
-
urn:nbn:de:101:1-2018112100370970082172
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 11:02 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
- Yano, Tomoki
- Torisawa, Takayuki
- Oiwa, Kazuhiro
- Tsukita, Sachiko
- SpringerLink (Online service)
Other Objects (12)
Publisher Correction: AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules
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Crosslinking of microtubules and actin filaments by S100A8/S100A9
Author Correction: CryoET reveals actin filaments within platelet microtubules
Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau
Dynamizing nuclear actin filaments
Distinct functions of microtubules and actin filaments in the transportation of the male germ unit in pollen
The roles and regulation of the actin cytoskeleton, intermediate filaments and microtubules in smooth muscle cell migration
Contribution of actin filaments and microtubules to cell elongation and alignment depends on the grating depth of microgratings
On the depolymerization of actin filaments
On the depolymerization of actin filaments
Actin filaments and bundles in flow
Publisher Correction: AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules
CryoET reveals actin filaments within platelet microtubules
Crosslinking of microtubules and actin filaments by S100A8/S100A9
Author Correction: CryoET reveals actin filaments within platelet microtubules
Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau
Dynamizing nuclear actin filaments
Distinct functions of microtubules and actin filaments in the transportation of the male germ unit in pollen
The roles and regulation of the actin cytoskeleton, intermediate filaments and microtubules in smooth muscle cell migration
Contribution of actin filaments and microtubules to cell elongation and alignment depends on the grating depth of microgratings
On the depolymerization of actin filaments
On the depolymerization of actin filaments
Actin filaments and bundles in flow
Publisher Correction: AMPK-dependent phosphorylation of cingulin reversibly regulates its binding to actin filaments and microtubules
CryoET reveals actin filaments within platelet microtubules
Crosslinking of microtubules and actin filaments by S100A8/S100A9
Author Correction: CryoET reveals actin filaments within platelet microtubules
Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau
Dynamizing nuclear actin filaments
Distinct functions of microtubules and actin filaments in the transportation of the male germ unit in pollen
The roles and regulation of the actin cytoskeleton, intermediate filaments and microtubules in smooth muscle cell migration
Contribution of actin filaments and microtubules to cell elongation and alignment depends on the grating depth of microgratings
On the depolymerization of actin filaments
On the depolymerization of actin filaments