The giant protein titin regulates the length of the striated muscle thick filament
- 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
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online resource.
- Bibliographic citation
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The giant protein titin regulates the length of the striated muscle thick filament ; volume:8 ; number:1 ; day:19 ; month:10 ; year:2017 ; pages:1-11 ; date:12.2017
Nature Communications ; 8, Heft 1 (19.10.2017), 1-11, 12.2017
- Creator
-
Tonino, Paola
Kiss, Balazs
Strom, Josh
Methawasin, Mei
Smith, John E.
Kolb, Justin
Labeit, Siegfried
Granzier, Henk
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s41467-017-01144-9
- URN
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urn:nbn:de:101:1-2019061421041292210779
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:54 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Tonino, Paola
- Kiss, Balazs
- Strom, Josh
- Methawasin, Mei
- Smith, John E.
- Kolb, Justin
- Labeit, Siegfried
- Granzier, Henk
- SpringerLink (Online service)
Other Objects (12)
Identification and characterization of novel vertebrate striated muscle proteins interacting with the giant titin and nebulin filament systems
The giant titin: how to evaluate its role in cardiomyopathies
Functional and Mutational Analysis of Kinase Domain of the Giant Protein Titin
F-actin architecture determines constraints on myosin thick filament motion
Elucidating the role of Titin mutations and the Titin-Nexilin interaction on the pathogenesis of dilated cardiomyopathy in zebrafish
Digenic inheritance involving a muscle-specific protein kinase and the giant titin protein causes a skeletal muscle myopathy
The Frank–Starling Law: a jigsaw of titin proportions
Lanyon Quoit & The Giant's Table & The Giant's Quoit
Dynamics of active filament systems : the role of filament polymerization and depolymerization
Mid the thick Arrows, Vol. 1
Mid the thick Arrows, Vol. 2
The N2A region of titin has a unique structural configuration
Identification and characterization of novel vertebrate striated muscle proteins interacting with the giant titin and nebulin filament systems
The giant titin: how to evaluate its role in cardiomyopathies
Functional and Mutational Analysis of Kinase Domain of the Giant Protein Titin
F-actin architecture determines constraints on myosin thick filament motion
Elucidating the role of Titin mutations and the Titin-Nexilin interaction on the pathogenesis of dilated cardiomyopathy in zebrafish
Digenic inheritance involving a muscle-specific protein kinase and the giant titin protein causes a skeletal muscle myopathy
The Frank–Starling Law: a jigsaw of titin proportions
Lanyon Quoit & The Giant's Table & The Giant's Quoit
Dynamics of active filament systems : the role of filament polymerization and depolymerization
Mid the thick Arrows, Vol. 1
Mid the thick Arrows, Vol. 2
The N2A region of titin has a unique structural configuration
Identification and characterization of novel vertebrate striated muscle proteins interacting with the giant titin and nebulin filament systems
The giant titin: how to evaluate its role in cardiomyopathies
Functional and Mutational Analysis of Kinase Domain of the Giant Protein Titin
F-actin architecture determines constraints on myosin thick filament motion
Elucidating the role of Titin mutations and the Titin-Nexilin interaction on the pathogenesis of dilated cardiomyopathy in zebrafish
Digenic inheritance involving a muscle-specific protein kinase and the giant titin protein causes a skeletal muscle myopathy
The Frank–Starling Law: a jigsaw of titin proportions
Lanyon Quoit & The Giant's Table & The Giant's Quoit
Dynamics of active filament systems : the role of filament polymerization and depolymerization
Mid the thick Arrows, Vol. 1
Mid the thick Arrows, Vol. 2