- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
-
Englisch
- Bibliographic citation
-
Interaction of the Zika virus with the cytoplasmic dynein-1 ; volume:20 ; number:1 ; day:6 ; month:3 ; year:2023 ; pages:1-11 ; date:12.2023
Virology journal ; 20, Heft 1 (6.3.2023), 1-11, 12.2023
- Creator
-
Zavala-Vargas, Dan Israel
Visoso-Carbajal, Giovani
Cedillo-Barrón, Leticia
Filisola-Villaseñor, Jessica Georgina
Rosales-Ramirez, Romel
Ludert, Juan E.
Morales-Ríos, Edgar
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1186/s12985-023-01992-6
- URN
-
urn:nbn:de:101:1-2408252133409.155958400998
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:21 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
- Zavala-Vargas, Dan Israel
- Visoso-Carbajal, Giovani
- Cedillo-Barrón, Leticia
- Filisola-Villaseñor, Jessica Georgina
- Rosales-Ramirez, Romel
- Ludert, Juan E.
- Morales-Ríos, Edgar
- SpringerLink (Online service)
Other Objects (12)
The force generation of cytoplasmic dynein is load dependent
Evolution of the eukaryotic dynactin complex, the activator of cytoplasmic dynein
The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein
Characterization of the Dynein-Dynactin Interaction
Kinesin and dynein respond differently to cytoplasmic drag
Two switches turn cytoplasmic dynein into an universal motor
Cargo specificity, regulation, and therapeutic potential of cytoplasmic dynein
Cytoplasmic dynein: a key player in neurodegenerative and neurodevelopmental diseases
A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity
Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge
Cytoplasmic dynein regulates the subcellular localization of sphingosine kinase 2 to elicit tumor-suppressive functions in glioblastoma
Step Sizes and Rate Constants of Single-headed Cytoplasmic Dynein Measured with Optical Tweezers
The force generation of cytoplasmic dynein is load dependent
Evolution of the eukaryotic dynactin complex, the activator of cytoplasmic dynein
The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein
Characterization of the Dynein-Dynactin Interaction
Kinesin and dynein respond differently to cytoplasmic drag
Two switches turn cytoplasmic dynein into an universal motor
Cargo specificity, regulation, and therapeutic potential of cytoplasmic dynein
Cytoplasmic dynein: a key player in neurodegenerative and neurodevelopmental diseases
A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity
Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge
Cytoplasmic dynein regulates the subcellular localization of sphingosine kinase 2 to elicit tumor-suppressive functions in glioblastoma
Step Sizes and Rate Constants of Single-headed Cytoplasmic Dynein Measured with Optical Tweezers
The force generation of cytoplasmic dynein is load dependent
Evolution of the eukaryotic dynactin complex, the activator of cytoplasmic dynein
The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein
Characterization of the Dynein-Dynactin Interaction
Kinesin and dynein respond differently to cytoplasmic drag
Two switches turn cytoplasmic dynein into an universal motor
Cargo specificity, regulation, and therapeutic potential of cytoplasmic dynein
Cytoplasmic dynein: a key player in neurodegenerative and neurodevelopmental diseases
A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity
Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge
Cytoplasmic dynein regulates the subcellular localization of sphingosine kinase 2 to elicit tumor-suppressive functions in glioblastoma