Ervasti, James M. - Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota

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Ervasti, James M. - Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota

Disease-causing missense mutations in actin binding domain 1 of dystrophin induce thermodynamic
Comp. by: RMervin Date:9/1/08 Time:16:57:02 Stage:1st Revises File Path:// pchns1301/WOMAT/Production/PRODENV/0000000001/0000005969/
Developmental Cell 11, 111, September, 2006 2006 Elsevier Inc. DOI 10.1016/j.devcel.2006.07.001 Cytoplasmic g-Actin Is Not Required for
Skeletal Muscle-Specific Ablation of ccyto-Actin Does Not Exacerbate the mdx Phenotype
The FASEB Journal Research Communication Context-dependent functional substitution of -skeletal
-Actin is required for cytoskeletal maintenance but not development
Dystrophin and Utrophin Bind Actin through Distinct Modes of Contact*
Delayed Embryonic Development and Impaired Cell Growth and Survival in Actg1 Null Mice
Functional Substitution by TAT-Utrophin in Dystrophin-Deficient Mice
Cytoplasmic -actin contributes to a compensatory remodeling response in dystrophin-deficient muscle
Dystrophin and utrophin have distinct effects on the structural dynamics of actin
Destabilization of the Dystrophin-Glycoprotein Complex without Functional Deficits in a-Dystrobrevin Null
The Rockefeller University Press $30.00 J. Cell Biol. Vol. 186 No. 3 363369
Dystrophin, its interactions with other proteins, and implications for muscular dystrophy