Microscopic studies on severing properties of actin-binding protein: its potential use in therapeutic treatment of actin-rich inclusions
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2093-3371
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Microscopic studies on severing properties of actin-binding protein: its potential use in therapeutic treatment of actin-rich inclusions ; volume:12 ; number:1 ; day:28 ; month:10 ; year:2021 ; pages:1-6 ; date:12.2021
Journal of analytical science and technology ; 12, Heft 1 (28.10.2021), 1-6, 12.2021
- Creator
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Kim, Han-ul
Bharda, Anahita Vispi
Moon, Jeong Chan
Jeoung, Dooil
Chung, Jeong Min
Jung, Hyun Suk
- Contributor
-
SpringerLink (Online service)
- DOI
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10.1186/s40543-021-00305-2
- URN
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urn:nbn:de:101:1-2022010806133419642107
- Rights
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Open Access; 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
- Kim, Han-ul
- Bharda, Anahita Vispi
- Moon, Jeong Chan
- Jeoung, Dooil
- Chung, Jeong Min
- Jung, Hyun Suk
- SpringerLink (Online service)
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Molekulare Charakterisierung eines menschlichen γ-Actin-Pseudogens [Gamma-Actin-Pseudogens]
Cytokinetic abscission requires actin-dependent microtubule severing
Molecular interactions of actin : actin structure and actin binding proteins
Molecular interactions of actin : actin-myosin interaction and actin based regulation
Actin Waves
Oligomerization of Lrrk controls actin severing and α-synuclein neurotoxicity in vivo
Mathematical methods for the quantification of Actin-filaments in microscopic images
Mathematical Methods for the Quantification of Actin-Filaments in Microscopic Images
Cysteine-rich protein 1 (CRP1) regulates actin filament bundling
Visualizing polymerizable actin
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