Asatoor, A. M. & Armstrong, M. D. (1967). 3-Methylhistidine, a component of actin. Biochemical and Biophysical Research Communications 26, 168–174.
Ciechanover, A. (2006). The ubiquitin proteolytic system: from a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology 66 (Suppl. 1), S7–S19.
De Boever, S., Vangestel, C., De Backer, P., Croubels, S. & Sys, S. U. (2008). Identification and validation of housekeeping genes as internal control for gene expression in an intravenous LPS inflammation model in chickens. Veterinary Immunology and Immunopathology 122, 312–317.
Du, J., Wang, X., Miereles, C., Bailey, J. L., Debigare, R., Zheng, B., Price, S. R. & Mitch, W. E. (2004). Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. Journal of Clinical Investigation 113, 115–123.
Franch, H. A. & Price, S. R. (2005). Molecular signaling pathways regulating muscle proteolysis during atrophy. Current Opinion in Clinical Nutrition and Metabolic Care 8, 271–275.
Glass, D. J. (2005). Skeletal muscle hypertrophy and atrophy signaling pathways. International Journal of Biochemistry and Cell Biology 37, 1974–1984.
Goll, D. E., Thompson, V. F., Li, H., Wei, W. & Cong, J. (2003). The calpain system. Physiological Reviews 83, 731–801.
Goll, D. E., Neti, G., Mares, S. W. & Thompson, V. F. (2008). Myofibrillar protein turnover: the proteasome and the calpains. Journal of Animal Science 86 (Suppl.), E19–E35.
Hayashi, K., Maeda, Y., Toyomizu, M. & Tomita, Y. (1987). High-performance liquid chromatographic method for the analysis of Nτ-methylhistidine in food, chicken excreta, and rat urine. Journal of Nutritional Science and Vitaminology 33, 151–156.
Johnson, P., Harris, C. I. & Perry, S. V. (1967). 3-Methylhistidine in actin and other muscle proteins. Biochemical Journal 105, 361–370.
Kamizono, T., Nakashima, K., Ohtsuka, A. & Hayashi, K. (2010). Effects of feeding hexane-extracts of a shochu distillery by-product on skeletal muscle protein degradation in broiler chicken. Bioscience, Biotechnology, and Biochemistry 74, 92–95.
Kamizono, T., Ohtsuka, A., Hashimoto, F. & Hayashi, K. (2013). Dibutoxybutane suppresses protein degradation and promotes growth in cultured chicken muscle cells. Journal of Poultry Science 50, 37–43.
Mahfudz, L. D., Hayashi, K., Ikeda, M., Hamada, K., Ohtsuka, A. & Tomita, Y. (1996 a). The effective use of shochu distillery by-product as a source of broiler feed. Japanese Poultry Science 33, 1–7.
Mahfudz, L. D., Hayashi, K., Otsuji, Y., Ohtsuka, A. & Tomita, Y. (1996 b). Separation of growth promoting factor of broiler chicken from shochu distillery by-product. Japanese Poultry Science 33, 96–103.
Mahfudz, L. D., Nakashima, K., Ohtsuka, A. & Hayashi, K. (1997). Growth factors for a primary chick muscle cell culture from shochu distillery by-products. Bioscience, Biotechnology, and Biochemistry 61, 1844–1847.
Mujahid, A., Akiba, Y., Warden, C. H. & Toyomizu, M. (2007). Sequential changes in superoxide production, anion carriers and substrate oxidation in skeletal muscle mitochondria of heat-stressed chickens. FEBS Letters 581, 3461–3467.
Nakashima, K., Komatsu, T., Yamazaki, M. & Abe, H. (2005). Effects of fasting and refeeding on expression of proteolytic-related genes in skeletal muscle of chicks. Journal of Nutritional Science and Vitaminology 51, 248–253.
Nakashima, K., Ishida, A. & Katsumata, M. (2009). Comparison of proteolytic-related gene expression in the skeletal muscles of layer and broiler chickens. Bioscience, Biotechnology, and Biochemistry 73, 1869–1871.
Ohtsuka, A., Kawatomi, N., Nakashima, K., Araki, T. & Hayashi, K. (2011). Gene expression of muscle-specific ubiquitin ligase, atrogin-1/MAFbx, positively correlates with skeletal muscle proteolysis in food-deprived broiler chickens. Journal of Poultry Science 48, 92–96.
Saleh, A. A., Eid, Y. Z., Ebeid, T. A., Ohtsuka, A., Yamamoto, M. & Hayashi, K. (2012). Feeding Aspergillus awamori reduces skeletal muscle protein breakdown and stimulates growth in broilers. Animal Science Journal 83, 594–598.
Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989). Molecular Cloning: a Laboratory Manual, 2nd edn. New York: Cold Spring Harbor Laboratory Press.
Sorimachi, H., Hata, S. & Ono, Y. (2011). Impact of genetic insights into calpain biology. Journal of Biochemistry 150, 23–37.
Sultana, M. S., Kamizono, T., Furusono, K. & Hayashi, K. (2011). Shochu distillery by-product loses growth promoting activity during preservation. Journal of Warm Regional Society of Animal Science, Japan 54, 99–105.
Szewczyk, N. J. & Jacobson, L. A. (2005). Signal-transduction networks and the regulation of muscle protein degradation. International Journal of Biochemistry and Cell Biology 37, 1997–2011.
Tesseraud, S., Bouvarel, I., Collin, A., Audouin, E., Crochet, S., Seiliez, I. & Leterrier, C. (2009). Daily variations in dietary lysine content alter the expression of genes related to proteolysis in chicken pectoralis major muscle. Journal of Nutrition 139, 38–43.
Young, V. R., Alexis, S. D., Baliga, B. S., Munro, H. N. & Muecke, W. (1972). Metabolism of administered 3-methylhistidine. Lack of muscle transfer ribonucleic acid charging and quantitative excretion as 3-methylhistidine and its N-acetyl derivative. Journal of Biological Chemistry 247, 3592–3600.