Atrogin-1

Questa voce sull'argomento proteine è solo un abbozzo.

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Atrogin-1 è una proteina che regola i meccanismi di autofagia cellulare attraverso il proteasoma. La carenza di questa proteina, in modelli animali, è implicata nella cardiomiopatia ipertrofica restrittiva.^[1]

• T. Zaglia, G. Milan; A. Ruhs; M. Franzoso; E. Bertaggia; N. Pianca; A. Carpi; P. Carullo; P. Pesce; D. Sacerdoti; C. Sarais, Atrogin-1 deficiency promotes cardiomyopathy and premature death via impaired autophagy., in J Clin Invest, maggio 2014, DOI:10.1172/JCI66339, PMID 24789905.
• LM. Baehr, M. Tunzi; SC. Bodine, Muscle hypertrophy is associated with increases in proteasome activity that is independent of MuRF1 and MAFbx expression., in Front Physiol, vol. 5, 2014, p. 69, DOI:10.3389/fphys.2014.00069, PMID 24600408.
• T. Sato, Y. Ito; T. Nagasawa, Regulation of skeletal muscle protein degradation and synthesis by oral administration of lysine in rats., in J Nutr Sci Vitaminol (Tokyo), vol. 59, n. 5, 2013, pp. 412-9, PMID 24418875.
• A. Suryawan, TA. Davis, Regulation of protein degradation pathways by amino acids and insulin in skeletal muscle of neonatal pigs., in J Anim Sci Biotechnol, vol. 5, n. 1, 2014, p. 8, DOI:10.1186/2049-1891-5-8, PMID 24438646.
• K. Nakashima, A. Ishida; M. Katsumata, Comparison of atrogin-1/MAFbx mRNA expression in the gizzards of egg- and meat-type chickens., in Biosci Biotechnol Biochem, vol. 77, n. 11, 2013, pp. 2319-21, PMID 24200787.
• K. Nakashima, A. Ishida; M. Katsumata, Atrogin-1/MAFbx, a muscle-specific ubiquitin ligase, is highly expressed in the smooth muscle of the chicken gizzard., in Biosci Biotechnol Biochem, vol. 77, n. 5, 2013, pp. 1092-5, PMID 23649234.

• SS. Thomas, WE. Mitch, Mechanisms stimulating muscle wasting in chronic kidney disease: the roles of the ubiquitin-proteasome system and myostatin., in Clin Exp Nephrol, vol. 17, n. 2, Apr 2013, pp. 174-82, DOI:10.1007/s10157-012-0729-9, PMID 23292175.
• XH. Wang, WE. Mitch, Muscle wasting from kidney failure-a model for catabolic conditions., in Int J Biochem Cell Biol, vol. 45, n. 10, Oct 2013, pp. 2230-8, DOI:10.1016/j.biocel.2013.06.027, PMID 23872437.
• H. Kohsaka, [Mechanism, diagnosis, and treatment of steroid myopathy]., in Brain Nerve, vol. 65, n. 11, Nov 2013, pp. 1375-80, PMID 24200615.
• JP. Gumucio, CL. Mendias, Atrogin-1, MuRF-1, and sarcopenia., in Endocrine, vol. 43, n. 1, Feb 2013, pp. 12-21, DOI:10.1007/s12020-012-9751-7, PMID 22815045.
• M. Zungu, JC. Schisler; MF. Essop; C. McCudden; C. Patterson; MS. Willis, Regulation of AMPK by the ubiquitin proteasome system., in Am J Pathol, vol. 178, n. 1, Jan 2011, pp. 4-11, DOI:10.1016/j.ajpath.2010.11.030, PMID 21224036.
• VC. Foletta, LJ. White; AE. Larsen; B. Léger; AP. Russell, The role and regulation of MAFbx/atrogin-1 and MuRF1 in skeletal muscle atrophy., in Pflugers Arch, vol. 461, n. 3, Mar 2011, pp. 325-35, DOI:10.1007/s00424-010-0919-9, PMID 21221630.
• DJ. Glass, PI3 kinase regulation of skeletal muscle hypertrophy and atrophy., in Curr Top Microbiol Immunol, vol. 346, 2010, pp. 267-78, DOI:10.1007/82_2010_78, PMID 20593312.
• MJ. Tisdale, Cancer cachexia., in Curr Opin Gastroenterol, vol. 26, n. 2, Mar 2010, pp. 146-51, DOI:10.1097/MOG.0b013e3283347e77, PMID 19918173.
• K. Sakuma, A. Yamaguchi, Molecular mechanisms in aging and current strategies to counteract sarcopenia., in Curr Aging Sci, vol. 3, n. 2, Jul 2010, pp. 90-101, PMID 20158492.

• Statine

• KLF15

• FBXO32

• RBX1

• EIF3A

• WikiGenes – Collaborative Publishing, WikiGenes - Fbxo32 - F-box protein 32, su wikigenes.org, MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine (archiviato dall'url originale il 5 maggio 2014).

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