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Статті в журналах з теми "PTPN14"
Hatterschide, Joshua, Amelia E. Bohidar, Miranda Grace, Tara J. Nulton, Hee Won Kim, Brad Windle, Iain M. Morgan, Karl Munger, and Elizabeth A. White. "PTPN14 degradation by high-risk human papillomavirus E7 limits keratinocyte differentiation and contributes to HPV-mediated oncogenesis." Proceedings of the National Academy of Sciences 116, no. 14 (March 20, 2019): 7033–42. http://dx.doi.org/10.1073/pnas.1819534116.
Повний текст джерелаPo’uha, Sela T., Marion Le Grand, Miriam B. Brandl, Andrew J. Gifford, Gregory J. Goodall, Yeesim Khew-Goodall, and Maria Kavallaris. "Stathmin levels alter PTPN14 expression and impact neuroblastoma cell migration." British Journal of Cancer 122, no. 3 (December 6, 2019): 434–44. http://dx.doi.org/10.1038/s41416-019-0669-1.
Повний текст джерелаLEHRER, STEVEN, and PETER H. RHEINSTEIN. "PTPN14 Mutations and Cervical Cancer." Cancer Diagnosis & Prognosis 1, no. 4 (September 3, 2021): 275–77. http://dx.doi.org/10.21873/cdp.10035.
Повний текст джерелаBottini, Angel, Dennis J. Wu, Rizi Ai, Michelle Le Roux, Beatrix Bartok, Michele Bombardieri, Karen M. Doody та ін. "PTPN14 phosphatase and YAP promote TGFβ signalling in rheumatoid synoviocytes". Annals of the Rheumatic Diseases 78, № 5 (26 лютого 2019): 600–609. http://dx.doi.org/10.1136/annrheumdis-2018-213799.
Повний текст джерелаFu, Panfeng, Ramaswamy Ramchandran, Mark Shaaya, Longshuang Huang, David L. Ebenezer, Ying Jiang, Yulia Komarova, et al. "Phospholipase D2 restores endothelial barrier function by promoting PTPN14-mediated VE-cadherin dephosphorylation." Journal of Biological Chemistry 295, no. 22 (April 23, 2020): 7669–85. http://dx.doi.org/10.1074/jbc.ra119.011801.
Повний текст джерелаLu, Yingzhi, Zhenxin Wang, Ling Zhou, Zhaoming Ma, Jianguo Zhang, Yan Wu, Yan Shao, and Yunyun Yang. "FAT1 and PTPN14 Regulate the Malignant Progression and Chemotherapy Resistance of Esophageal Cancer through the Hippo Signaling Pathway." Analytical Cellular Pathology 2021 (October 19, 2021): 1–9. http://dx.doi.org/10.1155/2021/9290372.
Повний текст джерелаShi, Wenting, and Fang Wang. "circ_AKT3 knockdown suppresses cisplatin resistance in gastric cancer." Open Medicine 17, no. 1 (January 1, 2022): 280–91. http://dx.doi.org/10.1515/med-2021-0355.
Повний текст джерелаYoon, Sun-Young, Jinsoo Kim, Bum Soo Lee, Su Cheol Baek, Sang J. Chung, and Ki Hyun Kim. "Terminalin from African Mango (Irvingia gabonensis) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine Phosphatases." Biomolecules 12, no. 2 (February 17, 2022): 321. http://dx.doi.org/10.3390/biom12020321.
Повний текст джерелаChoi, Jaewoo, Anita Saraf, Laurence Florens, Michael P. Washburn, and Luca Busino. "PTPN14 regulates Roquin2 stability by tyrosine dephosphorylation." Cell Cycle 17, no. 18 (September 17, 2018): 2243–55. http://dx.doi.org/10.1080/15384101.2018.1522912.
Повний текст джерелаWang, W., J. Huang, X. Wang, J. Yuan, X. Li, L. Feng, J. I. Park, and J. Chen. "PTPN14 is required for the density-dependent control of YAP1." Genes & Development 26, no. 17 (September 1, 2012): 1959–71. http://dx.doi.org/10.1101/gad.192955.112.
Повний текст джерелаДисертації з теми "PTPN14"
Hamyeh, Mohamed. "Régulation de l'agressivité tumorale mammaire par la protéine tyrosine phosphatase PTPL1/PTPN13." Thesis, Montpellier, 2016. http://www.theses.fr/2016MONTT015/document.
Повний текст джерелаThe regulation of breast tumor aggressiveness by Protein Tyrosine Phosphatase PTPL1/ PTPN13Breast cancer is a major problem for public health of which the incidence continues to increase. Its mortality is often linked to metastasis formation. Studies on PTPL1, the largest protein tyrosine phosphatase, have shown that it presents the characteristics of a tumor suppressor gene. PTPL1 is mutated in several types of cancers and its expression is associated with good prognostic in prostate and breast cancers. My team has shown that PTPL1 mediates the pro apoptotic effect of anti-estrogen in hormone-sensitive tumor cells by dephosphorylating IRS1, Insulin growth factor-1 receptor substrate, thus blocking PI3K/Akt pathway. In addition, PTPL1 regulates the growth, the invasion, and the adhesion of low aggressive breast tumor cells MCF-7.Our team established an isogenic cellular model capable of expressing PTPL1 or its mutants (phosphatase-dead and substrate-trapping mutants) in an inducible fashion in invasive cells. We showed that functional PTPL1 expression has a negative impact on cell aggressive phenotypes. Interestingly, the phosphatase-dead mutant exhibits the same behavior as the transfection control. This evidences that PTPL1 activity is crucial for the inhibition of aggressiveness. We are currently testing the clones tumorigenicity in athyemic mice.Furthermore, we conducted a comparative proteomic (SILAC) in order to study the global tyrosine phosphatome in MCF-7 and MDA-MB-231 cells with or without PTPL1. Our findings suggest that PTPL1 regulates the phosphorylation of proteins involved in different signaling pathways already described in the literature to be impacted by PTPL1. Remarkably, the quarter of proteins identified belong to cell junction structure or regulation. We then studied the impact of this phosphatase on cell junctions and showed that PTPL1 overexpression enhances cell aggregate formation in 3D culture, increases cell contact stability, relocates desmoglein to the cell junctions, and induces E-cadherin re-expression at the level of cell-cell contacts in MDA-MB-231 cells.Cell junctions and polarity are very important in oncology and particularly in the invasive process which is the first step in the metastatic dissemination. Our ongoing work focuses on identifying direct substrates for PTPL1 in order to elucidate the underlying PTPL1 signal leading to cell junctions and consequently propose a novel therapeutic targets
Dromard, Mathilde. "Rôles et mécanismes d'action de la protéine tyrosine phosphatase PTPL1/ptpn13 dans les cancers mammaires et ovariens." Montpellier 2, 2008. http://www.theses.fr/2008MON20040.
Повний текст джерелаRecent clinical studies have suggested an anti-oncogenic role for the Protein Tyrosine Phosphatase (PTP) PTPL1/ptpn13. Analysis of the inhibitory effect of 4-hydroxytamoxifen (OH-Tam) on growth factor action has allowed to identify the key role played by a new class of enzymes, PTPs, and more specially PTPL1 on the control of cell proliferation. The first part of my PhD studies, has demonstrated that PTPL1 inhibits activation of the Insulin Receptor Substrate-1 (IRS-1)/PI3K/Akt pathway induced by Insulin like Growth Factor 1 (IGF1), through the dephosphorylation of IRS-1, and that PTPL1 is sufficient to inhibit the IGF1 effect on cell survival and to induce apoptosis. Moreover, we have clarified the mechanisms by which the anti-estrogen OH-Tam inhibits Nerve Growth Factor (NGF)-induced breast cancer cells growth through PTPL1. PTPL1 is able to induce dephosphorylation of the NGF receptor, p140TrkA, which is necessary for activation of the MAPK (Mitogen Activated Protein Kinase) pathway and regulation of cell growth. Finally, in agreement with our retrospective studies showing the prognostic value of PTPL1 expression in ovarian tumors, we have also showed an inhibitory effect of PTPL1 on invasion, mobility and proliferation of ovarian cancer cells. Altogether, these results are consistent with the anti-oncogenic role played by this PTP. The identification of PTPL1 molecular targets and our understanding of the mechanisms that regulate its expression, its location and its activities, should allow consideration of new therapeutic approaches to regulate the expression or activity of this anti-oncogene
Tchankouo, Nguetcheu Stéphane. "Rôle des kinases LAMMER et des phosphatases PTP1B/PTP61F dans la régulation des voies de signalisation médiées par l'insuline." Thesis, Paris 11, 2012. http://www.theses.fr/2012PA11T067/document.
Повний текст джерелаType 2 diabetes and cancer represent the major public health problems. One important therapeutic target for these pathologies is the protein tyrosin phosphatase PTP1B. The phosphatase is known to negatively regulates the insulin signaling pathway by dephosphorylating the insulin receptor, IR or the insulin receptor substrate, IRS. However,PTP1B functions and its regulation mechanism remain poorly known. Two studies has notably described opposite effects of PTP1B activity following phosphorylation of its Ser50 residue either by CLK1/CLK2, LAMMER kinases or by AKT. Furthermore, AKT, a main insulin signaling pathway component, has been shown to phosphorylate the LAMMER kinaseCLK1 following insulin stimulation. In addition, the role of PTP1B in the regulation of the RAS/MAPK signaling pathway and hence in cancer is a very controversial subject. The first objective of this work was to analyse, the role of Ptp61F (the Drosophila ortholog of human PTP1B) in the Drosophila insulin pathway, the interaction between the phosphatase and the Drosophila LAMMER kinase gene, Doa, the role of Ptp61F in the RAS/MAPK signaling pathway. To achieve these, we took advantage of the genetic powerful of Drosophila to generate a Ptp61F gene mutant which has been characterized and its role in signaling pathways has been studied. This study showed that Ptp61F interacts with IR like PTP1B in mammals. It shows that Ptp61F regulates key components of insulin signaling pathway Pi3K/Akt. It also shows that Ptp61F is able to regulate the Drosophila LAMMER kinase gene, Doa. Finally, we noted that Ptp61F interacts by inhibiting the activity of severalcomponent of the RAS/MAPK signaling pathway of Drosophila (Egfr, Ras, rl (human ERK)) and conclude that Rl coud be a direct substrate of PTP61F. The data showing that Ptp61F interacts with Akt and the Drosophila LAMMER kinase gene, Doa, were the basis for the second study in order to show the role that the mammal LAMMER kinase CLK2 (Cdc-like kinase 2) could play in the insulin signaling pathway at molecular level using the human neuroblastoma cell line SH-SY5Y. From this second study, we show that CLK2 play an important role in insulin signaling. CLK2 is induced by insulin and its expression increases with time. PTP1B interacts in vivo and in vitro with CLK2. Overexpression of CLK2 impairs AKT phosphorylation by a mechanism which could involved PTP1B, since in vitro, CLK2 phosphorylates PTP1B and the latter interacts withAKT in vivo. It is the Ser50 residue of PTP1B being phosphorylated by CLK2 and this phosphorylation event represses PTP1B activity in vitro. AKT cannot phosphorylates PTP1B in vitro, suggesting that the phosphorylation of PTP1B by AKT could be cellular environment dependant
Cheyssac, Claire. "Etude de deux gènes candidats du DT2 : EIF4A2 : candidat positionnel au locus 3Q27 et PTPN1/PTP1B : cible pharmacologique dans la sensibilité à l'insuline." Lille 2, 2006. http://www.theses.fr/2006LIL2S009.
Повний текст джерелаType 2 diabetes (T2D) is the most common form of diabetes affecting more than 170 million people worldwide. The T2D pathophysiological mechanisms are characterized by defects of insulin secretion and insulin action leading to chronic hyperglycaemia determined by interactions between genetic and environmental risk factors. Although many genes responsible for monogenic forms of diabetes were identified, genetic determinants influencing T2D predisposition are still largely unknown. To identify new susceptibility variants, we used two approaches : - a familial association study of positional candidate gene variants at the 3q27 locus in falilies showing linkage to T2D with onset before 45 years ; and the exploration of a physiological candidate gene, PTPN1, through case-control analyses in different groups of subjects with type 2 diabetes or obesity. The analysis of the 3q27 locus in French families with strong T2D aggregation (432 diabetes subjects and 129 normoglycaemic subjects) confirmed of a genetic linkage with T2D age-of-onset. Two genes were investigated : KNG1, coding for kininogen, the bradykinin precursor, and EIF4A2 coding for the Eukaryotic Translation Initiation Factor 4 alpha 2, a translation initiation factor involved in protein synthesis which is down-regulated by glucose in rat pancreatic beta cells (INS832/13). A variant (rs266714), located upstream of the EIF4A2 gene showed association with T2D and T2D age-of-onset in the families. Affected sib-pairs sharing at least one at risk T allele showed a LOD-score of 5. 24 which could explain the T2D linkage. Moreover, this variant partly explains the age-of-onset linkage. The rs266714 SNP could modify the expression level of the eIF4A2 factor which modulates mRNA translation and protein synthesis rates in pancreatic beta cells. The PTPN1 gene codes for the protein tyrosine phosphatase 1B, a negative regulator of the insulin and leptin signalling pathways. An association with T2D and moderate obesity is observed for a variant at the PTPN1 gene locus. In 736 normoglycaemic non obese subjects, 2 intronic SNPs associate with variations of quantitative traits of glucose and lipid metabolism : increased HOMA-B and triglycerides, decreased HDL-cholesterol, which suggests a possible role in metabolic syndrome. This genetics approach contributes to an improved understanding of the pathways involved in the development of T2D and to propose new therapeutic targets
Sanchez-Blanco, Cristina. "Studies of the protein tyrosine phosphatase PTPN22/Lyp in Ptpn22 deficient mice." Thesis, King's College London (University of London), 2015. http://kclpure.kcl.ac.uk/portal/en/theses/studies-of-the-protein-tyrosine-phosphatase-ptpn22lyp-in-ptpn22-deficient-mice(cbcf6c1c-7d57-4df9-95ef-8696a7856858).html.
Повний текст джерелаMaisonneuve, Pierre. "Etude structurale et fonctionnelle de la phosphatase humaine PTPN4." Thesis, Paris 6, 2014. http://www.theses.fr/2014PA066673/document.
Повний текст джерелаThe function of signaling proteins is determined by the nature of the domains from which they are made up. A better understanding of cell signaling pathways will result from the study of these domains and their regulation. PTPN4 is a non-receptor tyrosine phosphatase with an anti-apoptotic function. Upon infection with an attenuated rabies virus, its function is hijacked, which subsequently leads to cell death. This phenotype is arises from the interaction of the PDZ binding motif (PBM) of the viral glycoprotein with the PDZ domain of PTPN4. In this study, we show that this PDZ domain is an allosteric inhibitor of the catalytic activity of the PTPN4 phosphatase domain. This is the first description of the regulation of a phosphatase by a PDZ domain. This inhibition is released by the interaction of a ligand to the PDZ domain, such as the viral glycoprotein PBM. Our structural study revealed that the PBM recognition disrupts the transient inter-domain interactions and restores the complete phosphatase catalytic properties. As well, we identified a PTPN4 endogenous ligand, the MAP Kinase p38, which may participate in the regulation of the cellular homeostatic through its interaction with PTPN4. Thus, in addition to its phosphatase regulatory role, the PDZ domain also allows the recruitment of partners and the introduction of substrates to the PTPN4 phosphatase active site. This study contributes to our understanding of the role played by PDZ domains in cell signaling pathways
Bertola, Débora Romeo. "Estudo do gene PTPN11 nos pacientes afetados pela síndrome de Noonan." Universidade de São Paulo, 2006. http://www.teses.usp.br/teses/disponiveis/5/5141/tde-12042006-110700/.
Повний текст джерелаINTRODUCTION: Noonan syndrome is an autosomal dominant disorder comprising short stature, facial dysmorphisms (ocular hypertelorism, downslanting palpebral fissures, palpebral ptosis, high arched palate and dental malocclusion), short and/or webbed neck, heart defects, mainly valvar pulmonary stenosis, sternal deformity and cryptorchidism in males. The PTPN11 gene, localized in the long arm of chromosome 12 (12q24.1), is responsible for approximately 50% of the cases. OBJECTIVE: To detect the PTPN11 gene mutation rate in a cohort of clinically well-characterized patients with Noonan and Noonan-like syndromes and to study the genotype-phenotype correlation. METHODS: Fifty probands with Noonan syndrome ascertained according to well-established diagnostic criteria, 3 with LEOPARD syndrome, 3 with Noonan-like/multiple giant cell lesion syndrome and 2 with neurofibromatosis/Noonan were enrolled in this study. Mutational analysis was performed using denaturing high-performance liquid chromatography followed by sequencing of amplicons with an aberrant elution profile. RESULTS: Missense mutations in the PTPN11 gene were identified in 21 probands with Noonan syndrome (42%), in all three patients with LEOPARD syndrome, in one case with Noonan-like/multiple giant cell lesion syndrome and in one with neurofibromatosis-Noonan syndrome. This last patient also showed a NF1 gene mutation. The only anomaly that reached statistical significance when comparing probands with and without mutations was the hematological abnormalities. A Noonan syndrome patient presenting a myeloproliferative disorder showed a T73I mutation. CONCLUSION: Noonan syndrome is a heterogeneous disorder, once PTPN11 gene mutations is responsible for 42% of the cases. A definitive genotype-phenotype correlation is not established, but the T73I mutation seems to predispose to a myeloproliferative disorder. Regarding Noonan-like syndromes, the PTPN11 gene is the main one in LEOPARD syndrome and also plays a role in neurofibromatosis-Noonan syndrome. Noonan-like/multiple giant cell lesion syndrome, part of the spectrum of Noonan syndrome, is also heterogeneous.
Keren, Boris Verloes Alain. "Syndrome de Noonan et mutations du gène PTPN11 corrélations génotype-phénotype /." Créteil : Université de Paris-Val-de-Marne, 2006. http://doxa.scd.univ-paris12.fr:80/theses/th0247734.pdf.
Повний текст джерелаChadwick, Michelle. "Characterization of a Novel Mouse Model for Angiosarcoma in Which Combined Inhibition of mTOR and MEK Results in Tumor Suppression." University of Cincinnati / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=ucin1490353768809798.
Повний текст джерелаAbdessamad, Mahmoud. "Caractérisation moléculaire et fonctionnelle des signalosomes PTEN/MAGI-1b/TRIP6 et PTEN/PTPN13." Paris 7, 2012. http://www.theses.fr/2012PA077048.
Повний текст джерелаThe PTEN tumor suppressor is a multifunctional protein endowed with a phosphatase activity that dephosphorylates not only some phosphotyrosine residues, but also the phosphoinositides generated by PI3K. In its C-terminus, PTEN encodes a PDZ-binding motif. Our Team has demonstrated the critical role of the lipid phosphatase activity of PTEN in stabilizing junctional complexes and in reverting invasiveness. PTEN interacts with cadherin β3-catenin complexes through the PDZ domain containing- protein MAGI-1. To identify new molecular PTEN partners, we applied yeast-two-hybrid assay, and identified TRIP6 and PTPN13. We have demonstrated that TRIP6 induces invasiveness of the MDCK epithelial cells, through i) the competition with (3-catenin for binding to MAGI-1 b and the destabilization of junctional complexes, ii) the activation of the PI3K/ Akt, and NFKB signaling pathways (FASEB J 23:916,2009). PTPN13 is a tyrosine phosphatase with 5 PDZ domains. We have confirmed the interaction of PTEN C-terminus with the 2nd PDZ domain of PTPN13 in vitro and ex vivo. We showed that PTEN is a PTPN13 substrate in vitro. In line with these results, the overexpression of wild-type PTPN13, but not of a mutant deficient in phosphatase activity decreased PTEN phosphorylation. This overexpression did not alter Akt phosphorylation -a reflect of the activity of this kinase- in PTEN deficient cell lines, but potentiated PTEN effects on this downstream target of PI3K. Thus, our results demonstrated the critical role of PTPN13 in controling PTEN signaling pathway
Книги з теми "PTPN14"
Dulczewski, Zygmunt. Archiwum Floriana Znanieckiego PTPN w Poznaniu. Poznań: PTPN, 1999., 1999.
Знайти повний текст джерелаNurjanah. Kisah sukses mitra binaan PTPN VII. Bandarlampung: Perusahaan Perseroan, PT Perkebunan Nusantara VII, 2010.
Знайти повний текст джерелаBangun, Mulya. Pers reformasi Indonesia: Tantangan globalisasi BUMN-PTPN abad 21. [Medan]: HPI-PPI Tabloid Primadona, 2000.
Знайти повний текст джерелаAlijoyo, F. Antonius. Leaping to the next curve: Perjalanan PTPN 13 menuju organisasi kelas dunia. Jakarta: Salemba Empat, 2003.
Знайти повний текст джерелаAgustono, Budi. Badan Perjuangan Rakyat Penunggu Indonesia vs PTPN II: Sengketa tanah di Sumatera Utara. Bandung: Diterbitkan untuk Wahana Informasi Masyarakat (WIM) oleh Akatiga, Pusat Analisis Sosial, 1997.
Знайти повний текст джерелаAtikah, Warah. Sengketa tanah perkebunan: Studi kasus tanah kebun Kalibakar PTPN XII (Persero), Kecamatan Dampit, Kabupaten Malang : laporan penelitian. [Jember]: Departemen Pendidikan Nasional RI, Universitas Jember, Lembaga Penelitian, 2003.
Знайти повний текст джерелаWahyudi. Formasi dan struktur gerakan sosial petani: Studi kasus reklaiming/penjarahan atas tanah PTPN XII (Persero) Kalibakar, Malang Selatan. Malang: UMM Press, 2005.
Знайти повний текст джерелаEyre, Steve, and Jane Worthington. Genetics of rheumatoid arthritis. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199642489.003.0040.
Повний текст джерелаEyre, Steve, Jane Worthington, and Sebastien Viatte. Genetics of rheumatoid arthritis. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780199642489.003.0040_update_003.
Повний текст джерелаJerzy, Świdziński, and Poznańskie Towarzystwo Przyjaciół Nauk. Komisja Filologiczna., eds. Z problematyki współczesnych przekładów twórczośći Mickiewicza na języki obce: Materiały ze spotkania tłumaczy Mickiewicza zorganizowanego przez Komisję Filologiczną PTPN w dniu 30 maja 1995 w Śmiełowie. Poznań: Wydawn. Poznańskiego Tow. Przyjaciół Nauk, 1999.
Знайти повний текст джерелаЧастини книг з теми "PTPN14"
Bauler, Timothy J., and Philip D. King. "PTPN3/PTPN4." In Encyclopedia of Signaling Molecules, 4294–98. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_535.
Повний текст джерелаBauler, Timothy J., and Philip D. King. "PTPN3/PTPN4." In Encyclopedia of Signaling Molecules, 1–4. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_535-1.
Повний текст джерелаDonato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "PTPN3/PTPN4." In Encyclopedia of Signaling Molecules, 1509–12. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_535.
Повний текст джерелаStanford, Stephanie M., Massimo Bottini, and Nunzio Bottini. "PTPN22." In Encyclopedia of Medical Immunology, 931–41. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-0-387-84828-0_46.
Повний текст джерелаVillars, P., K. Cenzual, R. Gladyshevskii, O. Shcherban, V. Dubenskyy, V. Kuprysyuk, I. Savysyuk, and R. Zaremba. "PtPb4." In Landolt-Börnstein - Group III Condensed Matter, 609. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-22847-6_506.
Повний текст джерелаShio, Marina Tiemi, and Martin Olivier. "PTPN6." In Encyclopedia of Signaling Molecules, 4298–308. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_309.
Повний текст джерелаShio, Marina Tiemi, and Martin Olivier. "PTPN6." In Encyclopedia of Signaling Molecules, 1–11. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4614-6438-9_309-1.
Повний текст джерелаDonato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "PTPH1." In Encyclopedia of Signaling Molecules, 1509. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101123.
Повний текст джерелаDonato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "PTPN5." In Encyclopedia of Signaling Molecules, 1512. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_101125.
Повний текст джерелаDonato, Dominique M., Steven K. Hanks, Kenneth A. Jacobson, M. P. Suresh Jayasekara, Zhan-Guo Gao, Francesca Deflorian, John Papaconstantinou, et al. "PTPN6." In Encyclopedia of Signaling Molecules, 1512–20. New York, NY: Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_309.
Повний текст джерелаТези доповідей конференцій з теми "PTPN14"
Liu, Xiaojun, Nuo Yang, Sheila A. Figel, Kayla E. Wilson, Carl D. Morrison, Irwin H. Gelman, and Jianmin Zhang. "Abstract LB-520: PTPN14 interacts with and negatively regulates the oncogenic function of YAP." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-lb-520.
Повний текст джерелаRužickij, Robert, and Raimondas Grubliauskas. "PADANGŲ TEKSTILĖS PLUOŠTO ATLIEKŲ LYGINAMOJO GARSO SUGERTIES KOEFICIENTO TYRIMAS IR VERTINIMAS." In 25-osios jaunųjų mokslininkų konferencijos „Mokslas – Lietuvos ateitis“ teminės konferencijos APLINKOS APSAUGOS INŽINERIJA. Vilniaus Gedimino Technikos Universitetas, 2022. http://dx.doi.org/10.3846/aainz.2022.010.
Повний текст джерелаQuintero, Luis Alberto Perez, and Michel L. Tremblay. "Abstract 1741: Reduced PTPN1/PTPN2 activity synergistically enhanced anti-tumoraleffector functionof CD8 T cells." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1741.
Повний текст джерелаPerez-Quintero, Luis Alberto, Yevgen Zolotarov, Zuzet Martinez-Cardoba, Chu Han Feng, Alexandre Poirier, Kelly Anne Pike, Jean-Sebastien Delisle, and Michel L. Tremblay. "Abstract NG16: Concomitant reduction of PTPN1/PTPN2 activity synergistically enhanced antitumoral effector function of CD8 T cells." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-ng16.
Повний текст джерелаAbdelsalam, Shahenda Salaheldine, and Abdelali Agouni. "Protein Tyrosine Phosphatase (PTP) 1B Inhibition Improves Endoplasmic Reticulum Stress-Induced Apoptosis and Impaired Angiogenic Response in Endothelial Cells." In Qatar University Annual Research Forum & Exhibition. Qatar University Press, 2021. http://dx.doi.org/10.29117/quarfe.2021.0110.
Повний текст джерелаRuess, D., G. Heynen, K. Ciecielski, W. Birchmeier, R. Schmid, and H. Algül. "PO-201 Mutant KRAS-driven cancers depend on PTPN11/SHP2 phosphatase." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.719.
Повний текст джерелаMainardi, S., A. Mulero-Sánchez, A. Prahallad, G. Germano, A. Bosma, C. Lieftink, E. Nadal, A. Bardelli, A. Villanueva, and R. Bernards. "PO-019 PTPN11 is a therapeutic target in KRAS mutant lung cancer." In Abstracts of the 25th Biennial Congress of the European Association for Cancer Research, Amsterdam, The Netherlands, 30 June – 3 July 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/esmoopen-2018-eacr25.554.
Повний текст джерелаGhazalpour, A., RP Bender, MJ McGinniss, and R. Ashfaq. "PD08-09: PTPN12 Gene Expression Signature in Triple Negative Breast Cancer Cohort." In Abstracts: Thirty-Fourth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 6‐10, 2011; San Antonio, TX. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/0008-5472.sabcs11-pd08-09.
Повний текст джерелаHill, Kristen Suzanne, Evan Roberts, Ellen Marin, Xue Wang, Jamie Teer, Jane Messina, Jerry Wu, and Minjung Kim. "Abstract 2387: The oncogenic role and therapeutic potential of PTPN11 in melanoma." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-2387.
Повний текст джерелаVermeer, Paola D., Nichole Haag, Kimberly M. Lee, Daniel W. Vermeer, Bryant G. Wieking, and John H. Lee. "Abstract 2114: PTPN13 regulates ephrinB1 reverse signaling, MAP kinase signaling and tumor growth." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2114.
Повний текст джерелаЗвіти організацій з теми "PTPN14"
Huang, Jiaoti. Function of PTP1B in Neuroendocrine Differentiation of Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, January 2008. http://dx.doi.org/10.21236/ada481731.
Повний текст джерелаDickman, Martin B., and Oded Yarden. Modulation of the Redox Climate and Phosphatase Signaling in a Necrotroph: an Axis for Inter- and Intra-cellular Communication that Regulates Development and Pathogenicity. United States Department of Agriculture, August 2011. http://dx.doi.org/10.32747/2011.7697112.bard.
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