No alteration in gene expression of components of the ubiquitin proteasome proteolytic pathway in dystrophin-deficient muscles
- 16 September 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 393 (2-3), 292-296
- https://doi.org/10.1016/0014-5793(96)00910-6
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Coordinate activation of lysosomal, Ca2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscleBiochemical Journal, 1996
- Muscle wasting in a rat model of long-lasting sepsis results from the activation of lysosomal, Ca2+ -activated, and ubiquitin-proteasome proteolytic pathways.JCI Insight, 1996
- Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes.JCI Insight, 1994
- Calpains (intracellular calcium-activated cysteine proteinases): Structure-activity relationships and involvement in normal and abnormal cellular metabolismInternational Journal of Biochemistry, 1990
- Increased protein degradation results from elevated free calcium levels found in muscle from mdx miceNature, 1988
- Duchenne muscular dystrophy: Deficiency of dystrophin at the muscle cell surfaceCell, 1988
- Immunolocalization of cathepsins B, H and L in skeletal muscle of X-linked muscular dystrophy (mdx) mouseActa Neuropathologica, 1988
- Dystrophin: The protein product of the duchenne muscular dystrophy locusCell, 1987
- Skeletal muscle and liver contain a soluble ATP + ubiquitin-dependent proteolytic systemBiochemical Journal, 1987
- Duchenne muscular dystrophy: Pathogenetic aspects and genetic preventionHuman Genetics, 1984