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How β2-adrenergic agonists induce skeletal muscle hypertrophy?
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/cbf.2848openalex-snapshot
IGF and myostatin pathways are respectively induced during the earlier and the later stages of skeletal muscle hypertrophy induced by clenbuterol, a β2‐adrenergic agonist
inferredcites →https://doi.org/10.1002/mus.21950openalex-snapshot
The muscle‐hypertrophic effect of clenbuterol is additive to the hypertrophic effect of myostatin suppression
inferredcites →https://doi.org/10.1006/dbio.2000.9682openalex-snapshot
MyoD−/− Satellite Cells in Single-Fiber Culture Are Differentiation Defective and MRF4 Deficient
inferredcites →https://doi.org/10.1016/j.archoralbio.2006.01.003openalex-snapshot
The expressions of insulin-like growth factors, their receptors, and binding proteins are related to the mechanism regulating masseter muscle mass in the rat
inferredcites →https://doi.org/10.1016/j.biocel.2009.03.002openalex-snapshot
MicroRNAs 1, 133, and 206: Critical factors of skeletal and cardiac muscle development, function, and disease
inferredcites →https://doi.org/10.1016/j.biocel.2013.06.025openalex-snapshot
β2-Adrenergic agonists and the treatment of skeletal muscle wasting disorders
inferredcites →https://doi.org/10.1016/j.biocel.2013.07.019openalex-snapshot
Regulation of Akt-mTOR, ubiquitin-proteasome and autophagy-lysosome pathways in response to formoterol administration in rat skeletal muscle
inferredcites →https://doi.org/10.1016/j.ceb.2009.01.029openalex-snapshot
MicroRNA control of muscle development and disease
inferredcites →https://doi.org/10.1016/j.cmet.2007.11.004openalex-snapshot
FoxO3 Coordinately Activates Protein Degradation by the Autophagic/Lysosomal and Proteasomal Pathways in Atrophying Muscle Cells
inferredcites →https://doi.org/10.1016/j.cmet.2009.10.008openalex-snapshot
Autophagy Is Required to Maintain Muscle Mass
inferredcites →https://doi.org/10.1016/j.tig.2008.01.007openalex-snapshot
MicroRNAs flex their muscles
inferredcites →https://doi.org/10.1016/j.ydbio.2004.01.046openalex-snapshot
Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis
inferredcites →https://doi.org/10.1016/j.yexcr.2010.04.009openalex-snapshot
Signalling and the control of skeletal muscle size
inferredcites →https://doi.org/10.1016/s0092-8674(04)00400-3openalex-snapshot
Foxo Transcription Factors Induce the Atrophy-Related Ubiquitin Ligase Atrogin-1 and Cause Skeletal Muscle Atrophy
inferredcites →https://doi.org/10.1016/s1534-5807(04)00107-8openalex-snapshot
Deacetylase Inhibitors Increase Muscle Cell Size by Promoting Myoblast Recruitment and Fusion through Induction of Follistatin
inferredcites →https://doi.org/10.1038/45230openalex-snapshot
Ghrelin is a growth-hormone-releasing acylated peptide from stomach
inferredcites →https://doi.org/10.1038/ncb1101-1009openalex-snapshot
Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways
inferredcites →https://doi.org/10.1038/ncb1101-1014openalex-snapshot
Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
inferredcites →https://doi.org/10.1038/ncb2404openalex-snapshot
Wnt7a–Fzd7 signalling directly activates the Akt/mTOR anabolic growth pathway in skeletal muscle
inferredcites →https://doi.org/10.1038/ng1810openalex-snapshot
A mutation creating a potential illegitimate microRNA target site in the myostatin gene affects muscularity in sheep
inferredcites →https://doi.org/10.1038/sj.bjp.0706669openalex-snapshot
Systemic administration of β2‐adrenoceptor agonists, formoterol and salmeterol, elicit skeletal muscle hypertrophy in rats at micromolar doses
inferredcites →https://doi.org/10.1073/pnas.0501076102openalex-snapshot
Genome-wide analysis of cAMP-response element binding protein occupancy, phosphorylation, and target gene activation in human tissues
inferredcites →https://doi.org/10.1079/bjn19880134openalex-snapshot
The relation between dietary restriction or clenbuterol (a selective β2 agonist) treatment on muscle growth and calpain proteinase (EC3.4.22.17) and calpastatin activities in lambs
inferredcites →https://doi.org/10.1083/jcb.200207056openalex-snapshot
Myostatin negatively regulates satellite cell activation and self-renewal
inferredcites →https://doi.org/10.1083/jcb.200912093openalex-snapshot
Mammalian target of rapamycin regulates miRNA-1 and follistatin in skeletal myogenesis
inferredcites →https://doi.org/10.1083/jcb.9.2.493openalex-snapshot
SATELLITE CELL OF SKELETAL MUSCLE FIBERS
inferredcites →https://doi.org/10.1096/fj.05-5125fjeopenalex-snapshot
Transcriptional profiling of myostatin‐knockout mice implicates Wnt signaling in postnatal skeletal muscle growth and hypertrophy
inferredcites →https://doi.org/10.1097/00005768-200202000-00014openalex-snapshot
Inhibited longitudinal growth of bones in young male rats by clenbuterol
inferredcites →https://doi.org/10.1113/jphysiol.2010.196725openalex-snapshot
Cellular mechanisms underlying temporal changes in skeletal muscle protein synthesis and breakdown during chronic β-adrenoceptor stimulation in mice
inferredcites →https://doi.org/10.1126/science.1065874openalex-snapshot
Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy
inferredcites →https://doi.org/10.1128/mcb.23.8.2893-2906.2003openalex-snapshot
MyoD Stimulates RB Promoter Activity via the CREB/p300 Nuclear Transduction Pathway
inferredcites →https://doi.org/10.1139/y10-114openalex-snapshot
Time course in calpain activity and autolysis in slow and fast skeletal muscle during clenbuterol treatment
inferredcites →https://doi.org/10.1152/ajpendo.00188.2011openalex-snapshot
Clenbuterol suppresses proteasomal and lysosomal proteolysis and atrophy-related genes in denervated rat soleus muscles independently of Akt
inferredcites →https://doi.org/10.1152/ajpendo.00193.2009openalex-snapshot
Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin
inferredcites →https://doi.org/10.1152/ajpendo.00555.2011openalex-snapshot
cAMP signaling in skeletal muscle adaptation: hypertrophy, metabolism, and regeneration
inferredcites →https://doi.org/10.1152/ajpendo.2000.279.1.e188openalex-snapshot
Amelioration of denervation-induced atrophy by clenbuterol is associated with increased PKC-α activity
inferredcites →https://doi.org/10.1152/ajpendo.2001.281.3.e449openalex-snapshot
Catecholamines inhibit Ca2+-dependent proteolysis in rat skeletal muscle through β2-adrenoceptors and cAMP
inferredcites →https://doi.org/10.1152/ajpendo.2001.281.4.e676openalex-snapshot
Elevated IGF-II mRNA and phosphorylation of 4E-BP1 and p70S6kin muscle showing clenbuterol-induced anabolism
inferredcites →https://doi.org/10.1152/ajpendo.2002.282.1.e31openalex-snapshot
Role of IGF-I and IGFBPs in the changes of mass and phenotype induced in rat soleus muscle by clenbuterol
inferredcites →https://doi.org/10.1152/japplphysiol.00873.2006openalex-snapshot
Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol
inferredcites →https://doi.org/10.1152/physrev.00028.2007openalex-snapshot
Role of β-Adrenoceptor Signaling in Skeletal Muscle: Implications for Muscle Wasting and Disease
inferredcites →https://doi.org/10.1161/01.cir.92.9.483openalex-snapshot
Clenbuterol Induces Hypertrophy of the Latissimus Dorsi Muscle and Heart in the Rat With Molecular and Phenotypic Changes
inferredcites →https://doi.org/10.1172/jci117929openalex-snapshot
Muscle protein waste in tumor-bearing rats is effectively antagonized by a beta 2-adrenergic agonist (clenbuterol). Role of the ATP-ubiquitin-dependent proteolytic pathway.
inferredcites →https://doi.org/10.1186/1471-2164-7-320openalex-snapshot
Changes in skeletal muscle gene expression following clenbuterol administration
inferredcites →https://doi.org/10.1210/en.2009-0428openalex-snapshot
Mechanisms Involved in 3′,5′-Cyclic Adenosine Monophosphate-Mediated Inhibition of the Ubiquitin-Proteasome System in Skeletal Muscle
inferredcites →https://doi.org/10.1210/en.2011-1687openalex-snapshot
The Type 1 Insulin-Like Growth Factor Receptor (IGF-IR) Pathway Is Mandatory for the Follistatin-Induced Skeletal Muscle Hypertrophy
inferredcites →https://doi.org/10.1247/csf.08022openalex-snapshot
MicroRNA-206 Is Highly Expressed in Newly Formed Muscle Fibers: Implications Regarding Potential for Muscle Regeneration and Maturation in Muscular Dystrophy
inferredcites →https://doi.org/10.1254/jphs.08097fpopenalex-snapshot
Effects of the β2-Agonist Clenbuterol on β1- and β2-Adrenoceptor mRNA Expressions of Rat Skeletal and Left Ventricle Muscles
inferredcites →https://doi.org/10.2141/jpsa.0120120openalex-snapshot
In vivo Administration of β2-agonist Clenbuterol and Subsequent Increase in Skeletal Muscle Mass in Neonatal Chicks
inferredcites →https://doi.org/10.2527/jas.2012-5737openalex-snapshot
The effects of Capn1 gene inactivation on skeletal muscle growth, development, and atrophy, and the compensatory role of other proteolytic systems1
inferredcites →https://doi.org/10.2527/jas1987.6561514xopenalex-snapshot
Cimaterol-Induced Muscle Hypertrophy and Altered Endocrine Status in Lambs
inferredcites →https://doi.org/10.4161/cc.10.3.14710openalex-snapshot
MicroRNAs in skeletal myogenesis
inferredcites →https://doi.org/10.7600/jpfsm.1.139openalex-snapshot
Effects of β2-agonists and exercise on β2-adrenergic receptor signaling in skeletal muscles
inferredcites →https://doi.org/10.7600/jpfsm.1.83openalex-snapshot
Roles played by protein metabolism and myogenic progenitor cells in exercise-induced muscle hypertrophy and their relation to resistance training regimens
inferredcites →https://doi.org/10.7600/jpfsm.2.101openalex-snapshot
Growth factor-dependent and independent regulation of skeletal muscle mass - Is IGF-1 necessary for skeletal muscle hypertrophy? -
inferredcites →https://doi.org/10.7600/jpfsm.2.179openalex-snapshot
Molecular basis of muscle hypertrophy and atrophy: Potential therapy for muscular dystrophy
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.4792708openalex-extracted
Development of an Immunoaffinity Chromatographic Adsorbent Using a Moderate Affinity, Anti-Salbutamol Chicken Scfv for High Sensitivity Lc-Ms/Ms Detection of Salbutamol in Porcine Urine
inferred← citeshttps://doi.org/10.1016/j.microc.2024.111246openalex-snapshot
Development of an immunoaffinity chromatographic adsorbent using a moderate affinity, anti-salbutamol chicken scFv for high sensitivity LC-MS/MS detection of salbutamol in porcine urine
inferred← citeshttps://doi.org/10.17650/2222-8721-2024-14-1-51-62openalex-snapshot
Stages of research and development of therapeutic approaches for Duchenne myodystrophy. Part I: the period before etiotropic approaches introduction
inferred← citeshttps://doi.org/10.3177/jnsv.64.68openalex-snapshot
Identification of Functional Food Factors as β2-Adrenergic Receptor Agonists and Their Potential Roles in Skeletal Muscle
inferred← citeshttps://doi.org/10.3389/fphar.2018.00896openalex-snapshot
Wogonin Attenuates Isoprenaline-Induced Myocardial Hypertrophy in Mice by Suppressing the PI3K/Akt Pathway
inferred← citeshttps://doi.org/10.3390/nu13062042openalex-snapshot
Egg White Protein Feeding Facilitates Skeletal Muscle Gain in Young Rats with/without Clenbuterol Treatment
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