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tgf-β1 (1968) 1968
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Journal of Cellular Physiology, ISSN 0021-9541, 06/2019, Volume 234, Issue 6, pp. 8834 - 8845
Purpose During myocardial infarction (MI), cardiac fibroblasts (CFs) transform into myofibroblast (CMT). This study aimed to investigate the crosstalk of... 
TGF‐β1 | cardiac fibroblasts | myofibroblast | Notch1 | myocardial fibrosis | TGF-β1 | Heart | Myocardial infarction | Phosphorylation | Phenotypes | Transformation | Collagen (type I) | Deactivation | Secretion | Transforming growth factor | Crosstalk | Markers | Smad3 protein | Inactivation | Signaling | Antagonism | Fibrosis | Fibroblasts | Infarction | Inhibition | Growth factors
Journal Article
Journal Article
Cellular Signalling, ISSN 0898-6568, 03/2018, Volume 43, pp. 1 - 10
Fibrotic disorders of the renal, pulmonary, cardiac, and hepatic systems are associated with significant morbidity and mortality. Effective therapies to... 
TGF-β1 | Plasminogen activator Inhibitor-1 | Kidney | Fibrosis | p53 | Plasminogen Activator Inhibitor-1
Journal Article
PLoS ONE, ISSN 1932-6203, 05/2013, Volume 8, Issue 5, p. e63896
The hormone relaxin (RLX) is produced by the heart and has beneficial actions on the cardiovascular system. We previously demonstrated that RLX stimulates... 
FIBROSIS | ACTIVATION | REGENERATION | MULTIDISCIPLINARY SCIENCES | NOTCH | TISSUE INHIBITOR | MICE | DIFFERENTIATION | INDUCTION | METALLOPROTEINASES | EXPRESSION | Animals, Newborn | NIH 3T3 Cells | Collagen Type I - metabolism | Receptors, G-Protein-Coupled - metabolism | Receptors, Notch - metabolism | Humans | Actins - metabolism | Smad3 Protein - metabolism | Down-Regulation - drug effects | Myofibroblasts - drug effects | Myocardium - cytology | Relaxin - pharmacology | Myofibroblasts - cytology | Myofibroblasts - metabolism | Transforming Growth Factor beta - pharmacology | Animals | Signal Transduction - drug effects | Cytoskeleton - metabolism | Mice | Transforming Growth Factor beta - metabolism | Cytoskeleton - drug effects | Receptors, Peptide - metabolism | Heart | Neonates | Tissue inhibitor of metalloproteinases | Collagen (type I) | Phosphorylation | Histogenesis | Smooth muscle | Smad3 protein | Activation | Biochemistry | Signal transduction | Actin | Rodents | Fibroblasts | Extracellular matrix | Experimentation | Metalloproteinase | Inhibition | Heart diseases | Cardiovascular system | Muscles | Cultures | Histology | Pharmacology | Relaxin | Gelatinase B | Medicine | Regeneration | Musculoskeletal system | Signaling | Molecular modelling | Inhibitors | Stromal cells | Collagen | Fibrosis | Ligands | Notch protein | Clinical medicine | Receptor mechanisms | Laboratory animals | Secretase | Phenylglycine
Journal Article
Journal Article
中国药理学报:英文版, ISSN 1671-4083, 2016, Volume 37, Issue 6, pp. 783 - 793
Journal Article
Journal Article
Journal Article