| Endothelial POFUT1 controls injury-induced liver fibrosis by repressing fibrinogen synthesis. | Endothelial POFUT1 controls injury-induced liver fibrosis by repressing fibrinogen synthesis.
He S, Luo Y, Ma W, Wang X, Yan C, Hao W, Fang Y, Su H, Lai B, Liu J, Xiong Y, Bai T, Ren X, Liu E, Han H, Wu Y, Yuan Z, Wang Y. | 07/10/2024 |
| EOGT enables residual Notch signaling in mouse intestinal cells lacking POFUT1. | EOGT enables residual Notch signaling in mouse intestinal cells lacking POFUT1.
Nauman M, Varshney S, Choi J, Augenlicht LH, Stanley P., Free PMC Article | 10/25/2023 |
| Role of poFUT1 and O-fucosylation in placental angiogenesisdagger. | Role of poFUT1 and O-fucosylation in placental angiogenesis†.
Liang C, Li Y, Qin H, Ramzan MN, Wang H, Liu S, Yan Q. | 04/19/2023 |
| Epiregulin and poFUT1 may be suggested as the potential diagnostic biomarkers and useful treatment targets for abortion. | Epiregulin promotes trophoblast epithelial-mesenchymal transition through poFUT1 and O-fucosylation by poFUT1 on uPA.
Cui X, Wang H, Li Y, Chen T, Liu S, Yan Q., Free PMC Article | 03/7/2020 |
| POFUT1 could be a new controller of myotube growth during myogenesis, especially through NFATc2/IL-4 signaling pathway. | Downregulation of POFUT1 Impairs Secondary Myogenic Fusion Through a Reduced NFATc2/IL-4 Signaling Pathway.
Der Vartanian A, Chabanais J, Carrion C, Maftah A, Germot A., Free PMC Article | 02/8/2020 |
| POFUT1 inactivation disrupts angiogenic signaling events and results in excessive angiogenic cell proliferation and plexus formation, leading to anomalous coronary arteries, myocardial infarction and heart failure. | Uncontrolled angiogenic precursor expansion causes coronary artery anomalies in mice lacking Pofut1.
Wang Y, Wu B, Lu P, Zhang D, Wu B, Varshney S, Del Monte-Nieto G, Zhuang Z, Charafeddine R, Kramer AH, Sibinga NE, Frangogiannis NG, Kitsis RN, Adams RH, Alitalo K, Sharp DJ, Harvey RP, Stanley P, Zhou B., Free PMC Article | 12/23/2017 |
| both wild-type and mutant Pofut1 proteins were degraded through lysosome dependent machinery. Pofut1 protein loss in the point mutant embryos caused the same phenotypes as those observed in Pofut1 null embryos | Pofut1 point-mutations that disrupt O-fucosyltransferase activity destabilize the protein and abolish Notch1 signaling during mouse somitogenesis.
Ajima R, Suzuki E, Saga Y., Free PMC Article | 12/9/2017 |
| The POFUT1 binds EGF-like domains of the hEGF type and that the highly correlated presence of POFUT1 and fucosylatable hEGFs has accompanied animal evolution. | Recognition of EGF-like domains by the Notch-modifying O-fucosyltransferase POFUT1.
Li Z, Han K, Pak JE, Satkunarajah M, Zhou D, Rini JM. | 09/9/2017 |
| Loss of Pofut1 expression is associated with Muscle Aging-Related Phenotypes. | Deletion of Pofut1 in Mouse Skeletal Myofibers Induces Muscle Aging-Related Phenotypes in cis and in trans.
Zygmunt DA, Singhal N, Kim ML, Cramer ML, Crowe KE, Xu R, Jia Y, Adair J, Martinez-Pena Y Valenzuela I, Akaaboune M, White P, Janssen PM, Martin PT., Free PMC Article | 09/9/2017 |
| results demonstrated that POFUT1-mediated O-fucosylation of NOTCH receptors regulates myogenic cell differentiation and affects postnatal muscle growth in mice | Reduced Notch signalling leads to postnatal skeletal muscle hypertrophy in Pofut1cax/cax mice.
Al Jaam B, Heu K, Pennarubia F, Segelle A, Magnol L, Germot A, Legardinier S, Blanquet V, Maftah A., Free PMC Article | 06/10/2017 |
| results establish the critical role of Pofut1 on Notch pathway activation during myogenic differentiation | Protein O-fucosyltransferase 1 expression impacts myogenic C2C12 cell commitment via the Notch signaling pathway.
Der Vartanian A, Audfray A, Al Jaam B, Janot M, Legardinier S, Maftah A, Germot A., Free PMC Article | 03/21/2015 |
| mDLL1 O-fucosylation by POFUT1 is dispensable for ligand function | O-fucosylation of the notch ligand mDLL1 by POFUT1 is dispensable for ligand function.
MĂĽller J, Rana NA, Serth K, Kakuda S, Haltiwanger RS, Gossler A., Free PMC Article | 01/10/2015 |
| Loss of Pofut1 is associated with myeloid hyperplasia and impaired lymphopoiesis. | Protein O-fucosyltransferase 1 (Pofut1) regulates lymphoid and myeloid homeostasis through modulation of Notch receptor ligand interactions.
Yao D, Huang Y, Huang X, Wang W, Yan Q, Wei L, Xin W, Gerson S, Stanley P, Lowe JB, Zhou L., Free PMC Article | 08/27/2011 |
| Reduced POFUT1 levels might affect Notch trafficking or overall O-fucosylation. | Notch signalling in the paraxial mesoderm is most sensitive to reduced Pofut1 levels during early mouse development.
Schuster-Gossler K, Harris B, Johnson KR, Serth J, Gossler A., Free PMC Article | 01/21/2010 |
| These data are consistent with a role for Pofut1 in AChR aggregation during synaptogenesis via the regulation of the synaptogenic activity of muscle agrin. | O-fucosylation of muscle agrin determines its ability to cluster acetylcholine receptors.
Kim ML, Chandrasekharan K, Glass M, Shi S, Stahl MC, Kaspar B, Stanley P, Martin PT., Free PMC Article | 01/21/2010 |
| Pofut1 is required for Notch signaling upstream of NICD1. | Pofut1 is required for the proper localization of the Notch receptor during mouse development.
Okamura Y, Saga Y. | 01/21/2010 |
| Pofut1 and O-fucose have roles in mammalian Notch signaling | Roles of Pofut1 and O-fucose in mammalian Notch signaling.
Stahl M, Uemura K, Ge C, Shi S, Tashima Y, Stanley P., Free PMC Article | 01/21/2010 |