The effect of skeletal myosin light chain kinase gene ablation on the fatigability of mouse fast muscle
β Scribed by William Gittings; Jiang Huang; Ian C. Smith; Joe Quadrilatero; Rene Vandenboom
- Book ID
- 106449456
- Publisher
- Springer Netherlands
- Year
- 2011
- Tongue
- English
- Weight
- 480 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0142-4319
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π SIMILAR VOLUMES
## Abstract The binding of calmodulin (CaM) to four synthetic peptide analogues of the skeletal muscle myosin light chain kinase (skβMLCK) target sequence has been studied using 1HβNMR. The 18βresidue peptide WFF is anchored to CaM via the interaction of the Trp 4 side chain with the Cβdomain and t
A DNA probe derived from a mouse intronless pseudogene including coding regions for the myosin fast skeletal muscle alkali light chains, MLC1F/MLC3F (suggested HGM symbol, MYL1), was tested on a panel of 25 independent man-rodent somatic cell hybrids in order to assign the human MLC1F/MLC3F gene to