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Showing 13 to 24 of 221 entries
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T-tubule biogenesis and triad formation in skeletal muscle and implication in human diseases.

Skeletal muscle

Al-Qusairi L, Laporte J.
PMID: 21797990
Skelet Muscle. 2011 Jul 13;1(1):26. doi: 10.1186/2044-5040-1-26.

In skeletal muscle, the excitation-contraction (EC) coupling machinery mediates the translation of the action potential transmitted by the nerve into intracellular calcium release and muscle contraction. EC coupling requires a highly specialized membranous structure, the triad, composed of a...

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Al-Qusairi L, Laporte J. T-tubule biogenesis and triad formation in skeletal muscle and implication in human diseases. Skelet Muscle. 2011;1(1):26doi: 10.1186/2044-5040-1-26.
Al-Qusairi, L., & Laporte, J. (2011). T-tubule biogenesis and triad formation in skeletal muscle and implication in human diseases. Skeletal muscle, 1(1), 26. https://doi.org/10.1186/2044-5040-1-26
Al-Qusairi, Lama, and Laporte, Jocelyn. "T-tubule biogenesis and triad formation in skeletal muscle and implication in human diseases." Skeletal muscle vol. 1,1 (2011): 26. doi: https://doi.org/10.1186/2044-5040-1-26
Al-Qusairi L, Laporte J. T-tubule biogenesis and triad formation in skeletal muscle and implication in human diseases. Skelet Muscle. 2011 Jul 13;1(1):26. doi: 10.1186/2044-5040-1-26. PMID: 21797990; PMCID: PMC3156648.
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Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models.

Skeletal muscle

Schiaffino S, Mammucari C.
PMID: 21798082
Skelet Muscle. 2011 Jan 24;1(1):4. doi: 10.1186/2044-5040-1-4.

A highly conserved signaling pathway involving insulin-like growth factor 1 (IGF1), and a cascade of intracellular components that mediate its effects, plays a major role in the regulation of skeletal muscle growth. A central component in this cascade is...

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Schiaffino S, Mammucari C. Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models. Skelet Muscle. 2011;1(1):4doi: 10.1186/2044-5040-1-4.
Schiaffino, S., & Mammucari, C. (2011). Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models. Skeletal muscle, 1(1), 4. https://doi.org/10.1186/2044-5040-1-4
Schiaffino, Stefano, and Mammucari, Cristina. "Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models." Skeletal muscle vol. 1,1 (2011): 4. doi: https://doi.org/10.1186/2044-5040-1-4
Schiaffino S, Mammucari C. Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models. Skelet Muscle. 2011 Jan 24;1(1):4. doi: 10.1186/2044-5040-1-4. PMID: 21798082; PMCID: PMC3143906.
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IIb or not IIb? Regulation of myosin heavy chain gene expression in mice and men.

Skeletal muscle

Harrison BC, Allen DL, Leinwand LA.
PMID: 21798083
Skelet Muscle. 2011 Feb 01;1(1):5. doi: 10.1186/2044-5040-1-5.

BACKGROUND: While the myosin heavy chain IIb isoform (MyHC-IIb) is the predominant motor protein in most skeletal muscles of rats and mice, the messenger RNA (mRNA) for this isoform is only expressed in a very small subset of specialized...

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Harrison BC, Allen DL, Leinwand LA. IIb or not IIb? Regulation of myosin heavy chain gene expression in mice and men. Skelet Muscle. 2011;1(1):5doi: 10.1186/2044-5040-1-5.
Harrison, B. C., Allen, D. L., & Leinwand, L. A. (2011). IIb or not IIb? Regulation of myosin heavy chain gene expression in mice and men. Skeletal muscle, 1(1), 5. https://doi.org/10.1186/2044-5040-1-5
Harrison, Brooke C, et al. "IIb or not IIb? Regulation of myosin heavy chain gene expression in mice and men." Skeletal muscle vol. 1,1 (2011): 5. doi: https://doi.org/10.1186/2044-5040-1-5
Harrison BC, Allen DL, Leinwand LA. IIb or not IIb? Regulation of myosin heavy chain gene expression in mice and men. Skelet Muscle. 2011 Feb 01;1(1):5. doi: 10.1186/2044-5040-1-5. PMID: 21798083; PMCID: PMC3143903.
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Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques.

Skeletal muscle

Ohlendieck K.
PMID: 21798084
Skelet Muscle. 2011 Feb 01;1(1):6. doi: 10.1186/2044-5040-1-6.

BACKGROUND: Skeletal muscle fibres represent one of the most abundant cell types in mammals. Their highly specialised contractile and metabolic functions depend on a large number of membrane-associated proteins with very high molecular masses, proteins with extensive posttranslational modifications...

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Ohlendieck K. Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques. Skelet Muscle. 2011;1(1):6doi: 10.1186/2044-5040-1-6.
Ohlendieck, K. (2011). Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques. Skeletal muscle, 1(1), 6. https://doi.org/10.1186/2044-5040-1-6
Ohlendieck, Kay. "Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques." Skeletal muscle vol. 1,1 (2011): 6. doi: https://doi.org/10.1186/2044-5040-1-6
Ohlendieck K. Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques. Skelet Muscle. 2011 Feb 01;1(1):6. doi: 10.1186/2044-5040-1-6. PMID: 21798084; PMCID: PMC3143904.
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Ryanodine receptors.

Skeletal muscle

Capes EM, Loaiza R, Valdivia HH.
PMID: 21798098
Skelet Muscle. 2011 May 04;1(1):18. doi: 10.1186/2044-5040-1-18.

Excitation-contraction coupling involves the faithful conversion of electrical stimuli to mechanical shortening in striated muscle cells, enabled by the ubiquitous second messenger, calcium. Crucial to this process are ryanodine receptors (RyRs), the sentinels of massive intracellular calcium stores contained...

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Capes EM, Loaiza R, Valdivia HH. Ryanodine receptors. Skelet Muscle. 2011;1(1):18doi: 10.1186/2044-5040-1-18.
Capes, E. M., Loaiza, R., & Valdivia, H. H. (2011). Ryanodine receptors. Skeletal muscle, 1(1), 18. https://doi.org/10.1186/2044-5040-1-18
Capes, E Michelle, et al. "Ryanodine receptors." Skeletal muscle vol. 1,1 (2011): 18. doi: https://doi.org/10.1186/2044-5040-1-18
Capes EM, Loaiza R, Valdivia HH. Ryanodine receptors. Skelet Muscle. 2011 May 04;1(1):18. doi: 10.1186/2044-5040-1-18. PMID: 21798098; PMCID: PMC3156641.
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Sarcospan: a small protein with large potential for Duchenne muscular dystrophy.

Skeletal muscle

Marshall JL, Crosbie-Watson RH.
PMID: 23282144
Skelet Muscle. 2013 Jan 03;3(1):1. doi: 10.1186/2044-5040-3-1.

Purification of the proteins associated with dystrophin, the gene product responsible for Duchenne muscular dystrophy, led to the discovery of the dystrophin-glycoprotein complex. Sarcospan, a 25-kDa transmembrane protein, was the last component to be identified and its function in...

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Marshall JL, Crosbie-Watson RH. Sarcospan: a small protein with large potential for Duchenne muscular dystrophy. Skelet Muscle. 2013;3(1):1doi: 10.1186/2044-5040-3-1.
Marshall, J. L., & Crosbie-Watson, R. H. (2013). Sarcospan: a small protein with large potential for Duchenne muscular dystrophy. Skeletal muscle, 3(1), 1. https://doi.org/10.1186/2044-5040-3-1
Marshall, Jamie L, and Crosbie-Watson, Rachelle H. "Sarcospan: a small protein with large potential for Duchenne muscular dystrophy." Skeletal muscle vol. 3,1 (2013): 1. doi: https://doi.org/10.1186/2044-5040-3-1
Marshall JL, Crosbie-Watson RH. Sarcospan: a small protein with large potential for Duchenne muscular dystrophy. Skelet Muscle. 2013 Jan 03;3(1):1. doi: 10.1186/2044-5040-3-1. PMID: 23282144; PMCID: PMC3599653.
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Satellite cell therapy - from mice to men.

Skeletal muscle

Bareja A, Billin AN.
PMID: 23369649
Skelet Muscle. 2013 Jan 31;3(1):2. doi: 10.1186/2044-5040-3-2.

Satellite cells are rare mononuclear skeletal muscle-resident cells that are the chief contributors to regenerative myogenesis following muscle injury. Although first identified more than 50 years ago, it is only recently that the murine satellite cell has become molecularly...

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Bareja A, Billin AN. Satellite cell therapy - from mice to men. Skelet Muscle. 2013;3(1):2doi: 10.1186/2044-5040-3-2.
Bareja, A., & Billin, A. N. (2013). Satellite cell therapy - from mice to men. Skeletal muscle, 3(1), 2. https://doi.org/10.1186/2044-5040-3-2
Bareja, Akshay, and Billin, Andrew N. "Satellite cell therapy - from mice to men." Skeletal muscle vol. 3,1 (2013): 2. doi: https://doi.org/10.1186/2044-5040-3-2
Bareja A, Billin AN. Satellite cell therapy - from mice to men. Skelet Muscle. 2013 Jan 31;3(1):2. doi: 10.1186/2044-5040-3-2. PMID: 23369649; PMCID: PMC3579761.
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Measuring microRNA reporter activity in skeletal muscle using hydrodynamic limb vein injection of plasmid DNA combined with in vivo imaging.

Skeletal muscle

Guess MG, Barthel KK, Pugach EK, Leinwand LA.
PMID: 23915674
Skelet Muscle. 2013 Aug 01;3(1):19. doi: 10.1186/2044-5040-3-19.

BACKGROUND: microRNA regulation plays an important role in the remodeling that occurs in response to pathologic and physiologic stimuli in skeletal muscle. In response to stress, microRNAs are dynamically regulated, resulting in a widespread "fine-tuning" of gene expression. An...

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Guess MG, Barthel KK, Pugach EK, et al. Measuring microRNA reporter activity in skeletal muscle using hydrodynamic limb vein injection of plasmid DNA combined with in vivo imaging. Skelet Muscle. 2013;3(1):19doi: 10.1186/2044-5040-3-19.
Guess, M. G., Barthel, K. K., Pugach, E. K., & Leinwand, L. A. (2013). Measuring microRNA reporter activity in skeletal muscle using hydrodynamic limb vein injection of plasmid DNA combined with in vivo imaging. Skeletal muscle, 3(1), 19. https://doi.org/10.1186/2044-5040-3-19
Guess, Martin G, et al. "Measuring microRNA reporter activity in skeletal muscle using hydrodynamic limb vein injection of plasmid DNA combined with in vivo imaging." Skeletal muscle vol. 3,1 (2013): 19. doi: https://doi.org/10.1186/2044-5040-3-19
Guess MG, Barthel KK, Pugach EK, Leinwand LA. Measuring microRNA reporter activity in skeletal muscle using hydrodynamic limb vein injection of plasmid DNA combined with in vivo imaging. Skelet Muscle. 2013 Aug 01;3(1):19. doi: 10.1186/2044-5040-3-19. PMID: 23915674; PMCID: PMC3750807.
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A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome.

Skeletal muscle

Blandin G, Marchand S, Charton K, Danièle N, Gicquel E, Boucheteil JB, Bentaib A, Barrault L, Stockholm D, Bartoli M, Richard I.
PMID: 23414517
Skelet Muscle. 2013 Feb 15;3(1):3. doi: 10.1186/2044-5040-3-3.

BACKGROUND: The complexity of the skeletal muscle and the identification of numerous human disease-causing mutations in its constitutive proteins make it an interesting tissue for proteomic studies aimed at understanding functional relationships of interacting proteins in both health and...

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Blandin G, Marchand S, Charton K, et al. A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome. Skelet Muscle. 2013;3(1):3doi: 10.1186/2044-5040-3-3.
Blandin, G., Marchand, S., Charton, K., Danièle, N., Gicquel, E., Boucheteil, J. B., Bentaib, A., Barrault, L., Stockholm, D., Bartoli, M., & Richard, I. (2013). A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome. Skeletal muscle, 3(1), 3. https://doi.org/10.1186/2044-5040-3-3
Blandin, Gaëlle, et al. "A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome." Skeletal muscle vol. 3,1 (2013): 3. doi: https://doi.org/10.1186/2044-5040-3-3
Blandin G, Marchand S, Charton K, Danièle N, Gicquel E, Boucheteil JB, Bentaib A, Barrault L, Stockholm D, Bartoli M, Richard I. A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome. Skelet Muscle. 2013 Feb 15;3(1):3. doi: 10.1186/2044-5040-3-3. PMID: 23414517; PMCID: PMC3610214.
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Sphingosine kinase/sphingosine 1-phosphate axis: a new player for insulin-like growth factor-1-induced myoblast differentiation.

Skeletal muscle

Bernacchioni C, Cencetti F, Blescia S, Donati C, Bruni P.
PMID: 22788716
Skelet Muscle. 2012 Jul 12;2(1):15. doi: 10.1186/2044-5040-2-15.

BACKGROUND: Insulin-like growth factor-1 (IGF-1) is the most important physiological regulator of skeletal muscle progenitor cells, which are responsible for adult skeletal muscle regeneration. The ability of IGF-1 to affect multiple aspects of skeletal muscle cell biology such as...

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Bernacchioni C, Cencetti F, Blescia S, et al. Sphingosine kinase/sphingosine 1-phosphate axis: a new player for insulin-like growth factor-1-induced myoblast differentiation. Skelet Muscle. 2012;2(1):15doi: 10.1186/2044-5040-2-15.
Bernacchioni, C., Cencetti, F., Blescia, S., Donati, C., & Bruni, P. (2012). Sphingosine kinase/sphingosine 1-phosphate axis: a new player for insulin-like growth factor-1-induced myoblast differentiation. Skeletal muscle, 2(1), 15. https://doi.org/10.1186/2044-5040-2-15
Bernacchioni, Caterina, et al. "Sphingosine kinase/sphingosine 1-phosphate axis: a new player for insulin-like growth factor-1-induced myoblast differentiation." Skeletal muscle vol. 2,1 (2012): 15. doi: https://doi.org/10.1186/2044-5040-2-15
Bernacchioni C, Cencetti F, Blescia S, Donati C, Bruni P. Sphingosine kinase/sphingosine 1-phosphate axis: a new player for insulin-like growth factor-1-induced myoblast differentiation. Skelet Muscle. 2012 Jul 12;2(1):15. doi: 10.1186/2044-5040-2-15. PMID: 22788716; PMCID: PMC3439699.
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Early onset muscle weakness and disruption of muscle proteins in mouse models of spinal muscular atrophy.

Skeletal muscle

Boyer JG, Murray LM, Scott K, De Repentigny Y, Renaud JM, Kothary R.
PMID: 24119341
Skelet Muscle. 2013 Oct 11;3(1):24. doi: 10.1186/2044-5040-3-24.

BACKGROUND: The childhood neuromuscular disease spinal muscular atrophy (SMA) is caused by mutations or deletions of the survival motor neuron (SMN1) gene. Although SMA has traditionally been considered a motor neuron disease, the muscle-specific requirement for SMN has never...

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Boyer JG, Murray LM, Scott K, et al. Early onset muscle weakness and disruption of muscle proteins in mouse models of spinal muscular atrophy. Skelet Muscle. 2013;3(1):24doi: 10.1186/2044-5040-3-24.
Boyer, J. G., Murray, L. M., Scott, K., De Repentigny, Y., Renaud, J. M., & Kothary, R. (2013). Early onset muscle weakness and disruption of muscle proteins in mouse models of spinal muscular atrophy. Skeletal muscle, 3(1), 24. https://doi.org/10.1186/2044-5040-3-24
Boyer, Justin G, et al. "Early onset muscle weakness and disruption of muscle proteins in mouse models of spinal muscular atrophy." Skeletal muscle vol. 3,1 (2013): 24. doi: https://doi.org/10.1186/2044-5040-3-24
Boyer JG, Murray LM, Scott K, De Repentigny Y, Renaud JM, Kothary R. Early onset muscle weakness and disruption of muscle proteins in mouse models of spinal muscular atrophy. Skelet Muscle. 2013 Oct 11;3(1):24. doi: 10.1186/2044-5040-3-24. PMID: 24119341; PMCID: PMC3852932.
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Andrographolide attenuates skeletal muscle dystrophy in mdx mice and increases efficiency of cell therapy by reducing fibrosis.

Skeletal muscle

Cabrera D, Gutiérrez J, Cabello-Verrugio C, Morales MG, Mezzano S, Fadic R, Casar JC, Hancke JL, Brandan E.
PMID: 24655808
Skelet Muscle. 2014 Mar 21;4:6. doi: 10.1186/2044-5040-4-6. eCollection 2014.

BACKGROUND: Duchenne muscular dystrophy (DMD) is characterized by the absence of the cytoskeletal protein dystrophin, muscle wasting, increased transforming growth factor type beta (TGF-β) signaling, and fibrosis. At the present time, the only clinically validated treatments for DMD are...

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Cabrera D, Gutiérrez J, Cabello-Verrugio C, et al. Andrographolide attenuates skeletal muscle dystrophy in mdx mice and increases efficiency of cell therapy by reducing fibrosis. Skelet Muscle. 2014;4:6doi: 10.1186/2044-5040-4-6.
Cabrera, D., Gutiérrez, J., Cabello-Verrugio, C., Morales, M. G., Mezzano, S., Fadic, R., Casar, J. C., Hancke, J. L., & Brandan, E. (2014). Andrographolide attenuates skeletal muscle dystrophy in mdx mice and increases efficiency of cell therapy by reducing fibrosis. Skeletal muscle, 46. https://doi.org/10.1186/2044-5040-4-6
Cabrera, Daniel, et al. "Andrographolide attenuates skeletal muscle dystrophy in mdx mice and increases efficiency of cell therapy by reducing fibrosis." Skeletal muscle vol. 4 (2014): 6. doi: https://doi.org/10.1186/2044-5040-4-6
Cabrera D, Gutiérrez J, Cabello-Verrugio C, Morales MG, Mezzano S, Fadic R, Casar JC, Hancke JL, Brandan E. Andrographolide attenuates skeletal muscle dystrophy in mdx mice and increases efficiency of cell therapy by reducing fibrosis. Skelet Muscle. 2014 Mar 21;4:6. doi: 10.1186/2044-5040-4-6. eCollection 2014. PMID: 24655808; PMCID: PMC4021597.
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Showing 13 to 24 of 221 entries