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A new model for the interaction of dystrophin with F-actin
Inna N. Rybakova
, Kurt J. Amann
,
James M. Ervasti
Biochemistry, Molecular Biology, and Biophysics (TMED)
Research output
:
Contribution to journal
›
Article
›
peer-review
202
Scopus citations
Overview
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Dive into the research topics of 'A new model for the interaction of dystrophin with F-actin'. Together they form a unique fingerprint.
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Keyphrases
Dystrophin
100%
Filamentous Actin (F-actin)
100%
Actin
17%
Binding Site
11%
Co-sedimentation
11%
F-actin Binding
11%
Actin Cross-linking
11%
Electron Microscopy
5%
Amino Acids
5%
Skeletal muscle
5%
Recombinant
5%
High Capacity
5%
Low Affinity
5%
Calpain
5%
Binding Protein
5%
Actin Filaments
5%
Actinin
5%
Sequence Homology
5%
Complexity Bounds
5%
Depolymerization
5%
Low Speed
5%
Viscometry
5%
Actin Binding
5%
Falling Ball
5%
Glycoprotein Complex
5%
Microcapillary
5%
Rod Domain
5%
Biochemistry, Genetics and Molecular Biology
Dystrophin
100%
Actin
100%
Glycoprotein
47%
Cross-Link
23%
Binding Site
11%
Electron Microscopy
5%
Amino Acids
5%
Binding Protein
5%
Depolymerization
5%
Skeletal Muscle
5%
Actinin
5%
Sequence Homology
5%
Microcirculation
5%
Calpain
5%
Neuroscience
Dystrophin
100%
Actin
100%
Glycoprotein
47%
Binding Site
11%
Monomer
11%
Actin Filament
5%
Electron Microscopy
5%
Calpain
5%
Skeletal Muscle
5%
Amino Acid
5%
Protein Binding
5%
Sequence Homology
5%
Actinin
5%