PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 31570383-3 2020 PTEN encodes a dual lipid and protein phosphatase that dephosphorylates the lipid phosphatidylinositol-3,4,5-trisphosphate (PIP3), in turn negatively regulating the oncogenic PI3K-AKT pathway, a key proto-oncogenic player in cancer development and progression. phosphatidylinositol 3,4,5-triphosphate 82-122 phosphatase and tensin homolog Mus musculus 0-4 33276499-3 2020 PTEN negatively regulates PI3K/AKT signalling by dephosphorylating PtdIns(3,4,5)P3 to form PtdIns(4,5)P2. phosphatidylinositol 3,4,5-triphosphate 67-82 phosphatase and tensin homolog Mus musculus 0-4 33065020-2 2020 While the role of PTEN lipid-phosphatase activity on PtdIns(3,4,5)P3 and inhibition of PI3K pathway is well characterized, the biological relevance of PTEN protein-phosphatase activity remains undefined. phosphatidylinositol 3,4,5-triphosphate 53-68 phosphatase and tensin homolog Mus musculus 18-22 24658595-2 2014 By acting as a unique lipid phosphatase converting phosphatidylinositol-3,4,5,- trisphosphate (PIP3) to phosphatidylinositol-4,5,-bisphosphate (PIP2), phosphatase and tensin homolog (PTEN) acts as the major cellular suppressor of PI3K signaling and AKT activation. phosphatidylinositol 3,4,5-triphosphate 51-93 phosphatase and tensin homolog Mus musculus 183-187 25520316-5 2015 Enhanced O2 - led to activation of the phosphatases PTP1B and PTEN, which via dephosphorylation of the IGF-1 receptor and phosphatidylinositol 3,4,5-triphosphate dampened IGF-1 signalling. phosphatidylinositol 3,4,5-triphosphate 122-161 phosphatase and tensin homolog Mus musculus 62-66 24805236-2 2014 PTEN dephosphorylates phosphatidylinositol (3,4,5)-triphosphate, thereby opposing the activity of class I phosphatidylinositol 3-kinases that mediate growth- and survival-factor signalling through phosphatidylinositol 3-kinase effectors such as AKT and mTOR. phosphatidylinositol 3,4,5-triphosphate 22-63 phosphatase and tensin homolog Mus musculus 0-4 24766807-2 2014 Here, we show that PTEN homodimerizes and, in this active conformation, exerts lipid phosphatase activity on PtdIns(3,4,5)P3. phosphatidylinositol 3,4,5-triphosphate 109-124 phosphatase and tensin homolog Mus musculus 19-23 24392697-4 2014 One of the most studied tumor suppressors in these pathways is the lipid phosphatase PTEN (phosphatase and tensin homolog deleted on chromosome ten), which dephosphorylates the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate (PIP3), thus preventing activation of the oncogenic kinase AKT (v-akt murine thymoma viral oncogene homolog). phosphatidylinositol 3,4,5-triphosphate 200-240 phosphatase and tensin homolog Mus musculus 85-89 22150431-3 2012 PTEN is a phosphatase with selectivity for PtdIns(3,4,5)P3, which is produced by the class I isoforms of PI3K (p110alpha, p110beta, p110gamma and p110delta). phosphatidylinositol 3,4,5-triphosphate 43-58 phosphatase and tensin homolog Mus musculus 0-4 24048858-3 2013 Conversely, PTEN (phosphatase and tensin homolog on chromosome 10) dephosphorylates PtdIns(3,4,5)P3 and negatively regulates the AKT pathway and myelination. phosphatidylinositol 3,4,5-triphosphate 84-99 phosphatase and tensin homolog Mus musculus 12-16 19286998-3 2009 Phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P(3)) signaling in neutrophils was elevated by depleting PTEN, a phosphatidylinositol 3"-phosphatase that hydrolyzes PtdIns(3,4,5)P(3). phosphatidylinositol 3,4,5-triphosphate 0-40 phosphatase and tensin homolog Mus musculus 112-116 21521784-8 2011 Together, these observations demonstrate that the innate immune responses can be enhanced and the severity of neutropenia-related infection can be alleviated by augmenting phosphatidylinositol (3,4,5)-trisphosphate in transfused neutrophils with PTEN inhibitor SF1670, providing a therapeutic strategy for improving the efficacy of granulocyte transfusion. phosphatidylinositol 3,4,5-triphosphate 172-214 phosphatase and tensin homolog Mus musculus 246-250 21531890-3 2011 The phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is phosphatidylinositol phosphate phosphatase, which negatively controls PI3K by dephosphorylating the signaling lipid, phosphatidylinositol 3,4,5-triphosphate. phosphatidylinositol 3,4,5-triphosphate 187-226 phosphatase and tensin homolog Mus musculus 61-65 19875726-4 2009 For example, the PTEN (phosphatase and tensin homolog) tumor suppressor protein is a phosphoinositide 3-phosphatase that, by metabolizing phosphatidylinositol 3,4,5-trisphosphate (PtdIns[3,4,5]P(3), PIP3), acts in direct antagonism to growth factor-stimulated PI3K. phosphatidylinositol 3,4,5-triphosphate 138-178 phosphatase and tensin homolog Mus musculus 17-21 21926349-4 2011 Here we report that dysregulation of PI3K signaling in mice by deletion of the phosphatase and tensin homolog (Pten) gene (which regulates the levels of the PI3K product, phosphatidylinositol 3,4,5-trisphosphate) caused mast cell hyperplasia and increased numbers in various organs. phosphatidylinositol 3,4,5-triphosphate 171-211 phosphatase and tensin homolog Mus musculus 111-115 18794881-1 2008 The PTEN tumour suppressor is a lipid and protein phosphatase that inhibits phosphoinositide 3-kinase (PI3K)-dependent signalling by dephosphorylating phosphatidylinositol 3,4,5-trisphosphate (PtdInsP(3)). phosphatidylinositol 3,4,5-triphosphate 151-191 phosphatase and tensin homolog Mus musculus 4-8 18178811-1 2008 Control of the intracellular levels of phosphatidylinositol-(3, 4, 5)-trisphosphate by PI3K and phosphatase and tensin homolog (PTEN) is essential for B cell development and differentiation. phosphatidylinositol 3,4,5-triphosphate 39-83 phosphatase and tensin homolog Mus musculus 128-132 18339867-2 2008 Most of the tumor suppressor function of PTEN has been attributed to its ability to dephosphorylate the second messenger, phosphatidylinositol 3,4,5-triphosphate, resulting in the biological control of the phosphatidylinositol 3-kinase (PI3K)/AKT pathway. phosphatidylinositol 3,4,5-triphosphate 122-161 phosphatase and tensin homolog Mus musculus 41-45 18201277-2 2008 The major substrate of PTEN is phosphatidylinositol-3,4,5-trisphosphate (PI(3,4,5)P3), a second messenger molecule produced following PI3K activation induced by a variety of stimuli. phosphatidylinositol 3,4,5-triphosphate 31-71 phosphatase and tensin homolog Mus musculus 23-27 17195063-2 2007 The protein/lipid phosphatase Pten (phosphatase and tensin homologue deleted on chromosome 10) attenuates PI3K signalling by dephosphorylating the phosphatidylinositol 3,4,5-trisphosphate generated by PI3K. phosphatidylinositol 3,4,5-triphosphate 147-187 phosphatase and tensin homolog Mus musculus 30-34 17371230-2 2007 The major substrate of PTEN is PIP(3) (phosphatidylinositol 3,4,5-trisphosphate) generated by the action of PI3Ks (phosphoinositide 3-kinases). phosphatidylinositol 3,4,5-triphosphate 39-79 phosphatase and tensin homolog Mus musculus 23-27 17341655-2 2007 PTEN is a dual protein/lipid phosphatase and its main substrate phosphatidyl-inositol 3,4,5 triphosphate (PIP3) is the product of PI3K. phosphatidylinositol 3,4,5-triphosphate 64-104 phosphatase and tensin homolog Mus musculus 0-4 16214396-1 2005 Phosphatase and tensin homolog (PTEN) is a multifunctional phosphatase whose substrate is phosphatidylinositol-3,4,5-triphosphate (PIP3), and it is also a ubiquitously expressed tumor suppressor gene that down-regulates phosphatidylinositol-3-kinases (PI3Ks). phosphatidylinositol 3,4,5-triphosphate 90-129 phosphatase and tensin homolog Mus musculus 32-36 16880400-4 2006 This increased Akt activity correlates with increased phosphatidylinositol (3,4,5)-trisphosphate levels which are due, at least in part, to diminished activity of the (3,4,5)-trisphosphate phosphatase PTEN. phosphatidylinositol 3,4,5-triphosphate 54-96 phosphatase and tensin homolog Mus musculus 201-205 15467489-7 2004 PTEN opposes the action of PI3-kinase by dephosphorylating the signaling lipid phosphatidylinositol 3,4,5-triphosphate. phosphatidylinositol 3,4,5-triphosphate 79-118 phosphatase and tensin homolog Mus musculus 0-4 15289934-1 2004 The tumor suppressor function of PTEN is attributed to its phospholipid phosphatase activity that dephosphorylates the plasma membrane phosphatidylinositol-(3,4,5)-triphosphate [PtdIns(3,4,5)P3]. phosphatidylinositol 3,4,5-triphosphate 135-176 phosphatase and tensin homolog Mus musculus 33-37 15289934-1 2004 The tumor suppressor function of PTEN is attributed to its phospholipid phosphatase activity that dephosphorylates the plasma membrane phosphatidylinositol-(3,4,5)-triphosphate [PtdIns(3,4,5)P3]. phosphatidylinositol 3,4,5-triphosphate 178-193 phosphatase and tensin homolog Mus musculus 33-37 15289934-2 2004 Implicit in this notion is that PTEN needs to be targeted to the plasma membrane to dephosphorylate PtdIns(3,4,5)P3. phosphatidylinositol 3,4,5-triphosphate 100-115 phosphatase and tensin homolog Mus musculus 32-36 12671058-2 2003 PTEN blocks the action of PI3K by dephosphorylating the signaling lipid phosphatidylinositol 3,4,5-triphosphate. phosphatidylinositol 3,4,5-triphosphate 72-111 phosphatase and tensin homolog Mus musculus 0-4 12563260-1 2003 Phosphoinositide 3-kinase (PI3K) and phosphatase and tensin homolog (PTEN) phosphatase serve essential functions in the regulation of cell growth, differentiation and survival by modulating intracellular phosphatidylinositol-3,4,5-trisphosphate (PI-3,4,5-P3) concentrations. phosphatidylinositol 3,4,5-triphosphate 204-244 phosphatase and tensin homolog Mus musculus 69-73 10339565-0 1999 PTEN modulates cell cycle progression and cell survival by regulating phosphatidylinositol 3,4,5,-trisphosphate and Akt/protein kinase B signaling pathway. phosphatidylinositol 3,4,5-triphosphate 70-111 phosphatase and tensin homolog Mus musculus 0-4 10339565-5 1999 Inactivation of PTEN in ES cells and in embryonic fibroblasts resulted in elevated levels of phosphatidylinositol 3,4,5,-trisphosphate, a product of phosphatidylinositol 3 kinase. phosphatidylinositol 3,4,5-triphosphate 93-134 phosphatase and tensin homolog Mus musculus 16-20 10339565-8 1999 Our studies suggest that PTEN regulates the phosphatidylinositol 3,4, 5,-trisphosphate and Akt signaling pathway and consequently modulates two critical cellular processes: cell cycle progression and cell survival. phosphatidylinositol 3,4,5-triphosphate 44-86 phosphatase and tensin homolog Mus musculus 25-29 12163562-7 2002 Similar alterations are seen in T cells from mice which are haploinsufficient for PTEN, a lipid phosphatase that regulates phosphatidylinositol-3,4,5-trisphosphate (PIP(3)) and influences PKBalpha activity. phosphatidylinositol 3,4,5-triphosphate 123-163 phosphatase and tensin homolog Mus musculus 82-86 11916922-2 2002 PTEN (MMAC1) is a lipid/protein phosphatase that can negatively regulate the PI3K pathway by dephosphorylating phosphatidylinositol (3,4,5)-triphosphate, but it is unclear whether PTEN is physiologically relevant to insulin signaling in vivo. phosphatidylinositol 3,4,5-triphosphate 111-152 phosphatase and tensin homolog Mus musculus 0-4 11916922-2 2002 PTEN (MMAC1) is a lipid/protein phosphatase that can negatively regulate the PI3K pathway by dephosphorylating phosphatidylinositol (3,4,5)-triphosphate, but it is unclear whether PTEN is physiologically relevant to insulin signaling in vivo. phosphatidylinositol 3,4,5-triphosphate 111-152 phosphatase and tensin homolog Mus musculus 6-11 9778245-5 1998 Furthermore, PTEN negatively regulates intracellular levels of phosphatidylinositol (3,4,5) trisphosphate in cells and dephosphorylates it in vitro. phosphatidylinositol 3,4,5-triphosphate 63-105 phosphatase and tensin homolog Mus musculus 13-17