| Stimulating VAPB-PTPIP51 ER-mitochondria tethering corrects FTD/ALS mutant TDP43 linked Ca[2+] and synaptic defects. | Stimulating VAPB-PTPIP51 ER-mitochondria tethering corrects FTD/ALS mutant TDP43 linked Ca(2+) and synaptic defects.
Markovinovic A, Martín-Guerrero SM, Mórotz GM, Salam S, Gomez-Suaga P, Paillusson S, Greig J, Lee Y, Mitchell JC, Noble W, Miller CCJ., Free PMC Article | 03/8/2024 |
| PTPIP51 inhibits non-small-cell lung cancer by promoting PTEN-mediated EGFR degradation. | PTPIP51 inhibits non-small-cell lung cancer by promoting PTEN-mediated EGFR degradation.
He M, Wang X, Chen W, Zhang J, Xiong Y, Cao L, Zhang L, Zhao N, Yang Y, Wang L. | 04/16/2022 |
| Phospholipid transfer function of PTPIP51 at mitochondria-associated ER membranes. | Phospholipid transfer function of PTPIP51 at mitochondria-associated ER membranes.
Yeo HK, Park TH, Kim HY, Jang H, Lee J, Hwang GS, Ryu SE, Park SH, Song HK, Ban HS, Yoon HJ, Lee BI., Free PMC Article | 08/21/2021 |
| Disruption of endoplasmic reticulum-mitochondria tethering proteins in post-mortem Alzheimer's disease brain. | Disruption of endoplasmic reticulum-mitochondria tethering proteins in post-mortem Alzheimer's disease brain.
Lau DHW, Paillusson S, Hartopp N, Rupawala H, Mórotz GM, Gomez-Suaga P, Greig J, Troakes C, Noble W, Miller CCJ., Free PMC Article | 08/7/2021 |
| Study shows that the VAPB-PTPIP51 tethers regulate autophagy and demonstrates that overexpression of VAPB or PTPIP51 to tighten endoplasmic reticulum-mitochondria contacts impairs, whereas small interfering RNA-mediated loss of VAPB or PTPIP51 to loosen contacts stimulates, autophagosome formation. | The ER-Mitochondria Tethering Complex VAPB-PTPIP51 Regulates Autophagy.
Gomez-Suaga P, Paillusson S, Stoica R, Noble W, Hanger DP, Miller CCJ., Free PMC Article | 07/7/2018 |
| the latest findings concerning PTPIP51 protein function, regulation and protein complex formation with regard to the involved signaling pathways and subcellular compartments (review) | Orchestrating cellular signaling pathways-the cellular "conductor" protein tyrosine phosphatase interacting protein 51 (PTPIP51).
Brobeil A, Dietel E, Gattenlöhner S, Wimmer M. | 02/17/2018 |
| High PTPIP51 expression is associated with glioblastoma. | PTPIP51 levels in glioblastoma cells depend on inhibition of the EGF-receptor.
Petri MK, Brobeil A, Planz J, Bräuninger A, Gattenlöhner S, Nestler U, Stenzinger A, Paradowska A, Wimmer M. | 09/24/2016 |
| PTPIP51 is regulated by its phosphorylation status combined with a thereby induced subcellular redistribution. | The known interactome of PTPIP51 in HaCaT cells—inhibition of kinases and receptors.
Brobeil A, Koch P, Eiber M, Tag C, Wimmer M. | 11/8/2014 |
| The presented data confirms a tyrosine phosphorylation-dependent interaction of PTPIP51 with 14-3-3beta and Raf-1 in vivo and a tyrosine-dependent interaction profile with DAGKalpha and PKA. | PTPIP51 in protein interactions: regulation and in situ interacting partners.
Brobeil A, Bobrich M, Tag C, Wimmer M. | 10/20/2012 |
| In glioblastoma PTPIP51 expression increases with the grade of malignancy and PTPIP51 interacts in situ with 14-3-3ss and PTP1B. | PTPIP51, a positive modulator of the MAPK/Erk pathway, is upregulated in glioblastoma and interacts with 14-3-3β and PTP1B in situ.
Petri MK, Koch P, Stenzinger A, Kuchelmeister K, Nestler U, Paradowska A, Steger K, Brobeil A, Viard M, Wimmer M. | 02/4/2012 |
| PTPIP51 is phosphorylated by Lyn and c-Src kinases lacking dephosphorylation by PTP1B in acute myeloid leukemia. | PTPIP51 is phosphorylated by Lyn and c-Src kinases lacking dephosphorylation by PTP1B in acute myeloid leukemia.
Brobeil A, Bobrich M, Graf M, Kruchten A, Blau W, Rummel M, Oeschger S, Steger K, Wimmer M. | 11/26/2011 |
| PTPIP51 expression was restricted to myeloid precursor cells undergoing differentiation. In blood cells therefore, PTPIP51 expression is restricted to differentiating and mature neutrophil granulocytes. | PTPIP51-a myeloid lineage specific protein interacts with PTP1B in neutrophil granulocytes.
Brobeil A, Graf M, Oeschger S, Steger K, Wimmer M. | 12/11/2010 |
| The promoter methylation status of PTPIP51 seems to influence the expression of PTPIP51, which was seen as elevated in the prostate carcinoma. | PTPIP51 mRNA and protein expression in tissue microarrays and promoter methylation of benign prostate hyperplasia and prostate carcinoma.
Koch P, Petri M, Paradowska A, Stenzinger A, Sturm K, Steger K, Wimmer M. | 01/21/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | See all PubMed (2) articlesGenetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ. Association between genetic variants in VEGF, ERCC3 and occupational benzene haematotoxicity.
Hosgood HD 3rd, Zhang L, Shen M, Berndt SI, Vermeulen R, Li G, Yin S, Yeager M, Yuenger J, Rothman N, Chanock S, Smith M, Lan Q. | 12/2/2009 |
| The results clearly point toward a strong association between PTPIP51 expression and differentiation in human muscle cells. | Differentiation-dependent PTPIP51 expression in human skeletal muscle cell culture.
Barop J, Sauer H, Steger K, Wimmer M., Free PMC Article | 01/21/2010 |
| FAM82A2 is expressed in keratinocyte carcinoma and their surrounding stroma. | The novel protein PTPIP51 is expressed in human keratinocyte carcinomas and their surrounding stroma.
Koch P, Stenzinger A, Viard M, Märker D, Mayser P, Nilles M, Schreiner D, Steger K, Wimmer M., Free PMC Article | 01/21/2010 |
| PTPIP51 and PTP1B, play a role in differentiation and apoptosis of the cytotrophoblast and syncytiotrophoblast, respectively. Moreover, PTPIP51 may also serve as a cellular signaling partner in angiogenesis and vascular remodeling. | Protein tyrosine phosphatase interacting protein 51 (PTPIP51) mRNA expression and localization and its in vitro interacting partner protein tyrosine phosphatase 1B (PTP1B) in human placenta of the first, second, and third trimester.
Stenzinger A, Märker D, Koch P, Hoffmann J, Baal N, Steger K, Wimmer M., Free PMC Article | 01/21/2010 |
| PTPIP51 is a mitochondrial protein with apoptosis-inducing function and that the N-terminal TM domain is required for both the correct targeting of the protein to mitochondria and its apoptotic functions. | Protein tyrosine phosphatase interacting protein 51 (PTPIP51) is a novel mitochondria protein with an N-terminal mitochondrial targeting sequence and induces apoptosis.
Lv BF, Yu CF, Chen YY, Lu Y, Guo JH, Song QS, Ma DL, Shi TP, Wang L. | 01/21/2010 |
| PTPIP51 might be involved in the regulation of cellular processes associated with differentiation, movement, or cytoskeletal organization | The novel protein PTPIP51 exhibits tissue- and cell-specific expression.
Stenzinger A, Kajosch T, Tag C, Porsche A, Welte I, Hofer HW, Steger K, Wimmer M. | 01/21/2010 |