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Polyomavirus Large T Antigen Induces Alterations in Cytoplasmic Signalling Pathways Involving Shc Activation

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LncR-133a Suppresses Myoblast Differentiation by Sponging miR-133a-3p to Activate the FGFR1/ERK1/2 Signaling Pathway in Goats

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DA-Raf, a dominant-negative regulator of the Ras–ERK pathway, is essential for skeletal myocyte differentiation including myoblast fusion and apoptosis

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Phosphoproteomics Profiling Defines a Target Landscape of the Basophilic Protein Kinases AKT, S6K, and RSK in Skeletal Myotubes

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A Phosphoproteomic Screen Identifies a Guanine Nucleotide Exchange Factor for Rab3A Protein as a Mitogen-activated Protein (MAP) Kinase Phosphatase-5-regulated MAP Kinase Target in Interleukin 6 (IL-6) Secretion and Myogenesis

Lee, H., Min, K., Yi, J.-S., Shi, H., Chang, W., Jackson, L. V., & Bennett, A. M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.769208 · Cited by 8

In vitrocellular response to oxidized collagen-PLLA hybrid scaffolds designed for the repair of muscular tissue defects and complex incisional hernias

Pu, F., Rhodes, N. P., Bayon, Y., & Hunt, J. A. (2013) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.1837 · Cited by 8

Glial cell-induced endothelial morphogenesis is inhibited by interfering with extracellular signal-regulated kinase signaling.

Chandrasekar, N., Mohanam, S., Lakka, S. S., Dinh, D. H., Olivero, W. C., Gujrati, M., & Rao, J. S. (2003) · PubMed · Cited by 8

Role of farnesyltransferase inhibitors in hematologic malignancies

Santos, E. S., Rosenblatt, J. D., & Goodman, M. S. (2004) · Expert Review of Anticancer Therapy · doi:10.1586/14737140.4.5.843 · Cited by 8

How to MEK Muscle

Penn, B. H., Berkes, C. A., Bergstrom, D. A., & Tapscott, S. J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00331-8 · Cited by 8

Elevated expression of NF-κB and Bcl-2 proteins in C2C12 myocytes during myogenesis is affected by PD98059, LY294002 and SB203580

Kwiecinska, P., ROSZKIEWICZ, B., Łokociejewska, M., & Orzechowski, A. (2005) · Cell Biology International · doi:10.1016/j.cellbi.2004.12.013 · Cited by 8

Role of MAP Kinases p42erk-2/p44erk-1 in Cementum-derived Attachment-protein-mediated Cell Attachment

Komaki, M., Kang, M.-H., & Narayanan, A. S. (2000) · Journal of Dental Research · doi:10.1177/00220345000790101001 · Cited by 8

Senescent cells inhibit mouse myoblast differentiation via the SASP-lipid 15d-PGJ2 mediated modification and control of HRas

Pundlik, S. S., Barik, A., Venkateshvaran, A., Sahoo, S. S., Jaysingh, M. A., Math, R. G. H., Lal, H., Hashmi, M. A., & Ramanathan, A. (2024) · eLife · doi:10.7554/elife.95229 · Cited by 12

Global transcriptomic analysis reveals Lnc-ADAMTS9 exerting an essential role in myogenesis through modulating the ERK signaling pathway

Wang, L., He, T., Zhang, X., Wang, Y., Qiu, K., Jiao, N., He, L., & Yin, J. (2021) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-020-00524-4 · Cited by 7

FGGY carbohydrate kinase domain containing is expressed and alternatively spliced in skeletal muscle and attenuates MAP kinase and Akt signaling

Smith, A. L., Gjoka, E., Izhar, M., Novo, K., Mason, B. C., Casas, A. D. L., & Waddell, D. S. (2021) · Gene · doi:10.1016/j.gene.2021.145836 · Cited by 7

The Role of Signal Transduction Pathways in Drug and Radiation Resistance

Grant, S., Fisher, P. B., & Dent, P. (2002) · Cancer treatment and research · doi:10.1007/978-1-4615-1173-1_5 · Cited by 7

Cracking the code: Understanding ESWT's role in bone fracture healing

Jing, N., Hou, Y.-C., Zhang, J.-C., Xu, G., Lei, M., Tang, X., Chen, W. R., Ni, H., & Zhang, F. (2025) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2024.11.006 · Cited by 6

Recombinant adenoviral microRNA-206 induces myogenesis in C2C12 cells

Zhang, W., Wang, T., Su, Y., Li, W., Frame, L. T., & Ai, G. (2011) · Medical Science Monitor · doi:10.12659/msm.882122 · Cited by 6

Muscle-derived TRAIL negatively regulates myogenic differentiation

Kim, D., Singh, N., Waldemer, R. J., Yoon, M., & Chen, J. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112165 · Cited by 6

Mitogen-Activated Protein Kinases and Mitogen-Activated Protein Kinase Phosphatases in Regenerative Myogenesis and Muscular Dystrophy

Shi, H., & Gil-Antón, M. (2012) · InTech eBooks · doi:10.5772/30307 · Cited by 5

Selenium and Skeletal Muscle Health in Sports Nutrition

Wang, Q., Huang, J., Zhu, K., & Zuo, W. (2025) · Nutrients · doi:10.3390/nu17111902 · Cited by 8

Data-Modeling Identifies Conflicting Signaling Axes Governing Myoblast Proliferation and Differentiation Responses to Diverse Ligand Stimuli

Loiben, A. M., Soueid‐Baumgarten, S., Kopyto, R. F., Bhattacharya, D., Kim, J. C., & Cosgrove, B. D. (2017) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-017-0508-5 · Cited by 6

Lrrc75b is a novel negative regulator of C2C12 myogenic differentiation

Zhong, Y.-C., Zou, L., Wang, Z., Pan, Y., Dai, Z., Liu, X., Cui, L., & Zuo, C. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2016.2738 · Cited by 5

Analysis of the role of extracellular signal regulated kinase (ERK5) in the differentiation of muscle cells

Dinev, D. (2001) · Online Publication Service of Würzburg University (Würzburg University)

MEK1 plays contrary stage-specific roles in skeletal myogenic differentiation

Jo, C., Jang, B. G., & Jo, S. A. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.08.008 · Cited by 30

Mitogen-activated Protein Kinase Pathway Is Involved in the Differentiation of Muscle Cells

Gredinger, E., Gerber, A. N., Tamir, Y., Tapscott, S. J., & Bengal, E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.17.10436 · Cited by 210

Extracellular signal regulated kinase 5 (ERK5) is required for the differentiation of muscle cells

Dinev, D., Jordan, B. W. M., Neufeld, B., Lee, J., Lindemann, D., Rapp, U. R., & Ludwig, S. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve177 · Cited by 110

p38 Mitogen-activated Protein Kinase Pathway Promotes Skeletal Muscle Differentiation

Zetser, A., Gredinger, E., & Bengal, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.5193 · Cited by 461