Publication: Tissue Transglutaminase 2 has higher affinity for relaxed than for stretched fibronectin fibers
Tissue Transglutaminase 2 has higher affinity for relaxed than for stretched fibronectin fibers
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Selcuk, K., Leitner, A., Braun, L., Le Blanc, F., Pacak, P., Pot, S., & Vogel, V. (2024). Tissue Transglutaminase 2 has higher affinity for relaxed than for stretched fibronectin fibers. Matrix Biology, 125, 113–132. https://doi.org/10.1016/j.matbio.2023.12.006
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Tissue transglutaminase 2 (TG2) plays a vital role in stabilizing extracellular matrix (ECM) proteins through enzymatic crosslinking during tissue growth, repair, and inflammation. TG2 also binds non-covalently to fibronectin (FN), an essential component of the ECM, facilitating cell adhesion, migration, proliferation, and survival. However, the interaction between TG2 and fibrillar FN remains poorly understood, as most studies have focused on soluble or surface-adsorbed FN or FN fragments, which differ in their conformations from ins
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Selcuk, K., Leitner, A., Braun, L., Le Blanc, F., Pacak, P., Pot, S., & Vogel, V. (2024). Tissue Transglutaminase 2 has higher affinity for relaxed than for stretched fibronectin fibers. Matrix Biology, 125, 113–132. https://doi.org/10.1016/j.matbio.2023.12.006