PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33987937-0 2021 Lovastatin reduces PEL cell survival by phosphorylating ERK1/2 that blocks the autophagic flux and engages a cross-talk with p53 to activate p21. Lovastatin 0-10 H3 histone pseudogene 16 Homo sapiens 141-144 33987937-4 2021 At molecular level, Lovastatin by dephosphorylating STAT3, induced ERK1/2 activation that inhibited autophagy and phosphorylated p53ser15 that in turn maintained ERK1/2 activated and up-regulated p21. Lovastatin 20-30 H3 histone pseudogene 16 Homo sapiens 196-199 33987937-5 2021 However, p21 played a pro-survival role in this setting, as its inhibition by UC2288 further reduced cell survival in PEL cells undergoing Lovastatin treatment. Lovastatin 139-149 H3 histone pseudogene 16 Homo sapiens 9-12 33987937-6 2021 In conclusion, this study suggests that Lovastatin may represent a valid therapeutic alternative against PEL cells, especially if used in combination with p21 inhibitors. Lovastatin 40-50 H3 histone pseudogene 16 Homo sapiens 155-158 30939155-0 2019 Regulatory mechanisms of fluvastatin and lovastatin for the p21 induction in human cervical cancer HeLa cells. Lovastatin 41-51 H3 histone pseudogene 16 Homo sapiens 60-63 30939155-5 2019 Our data showed that the statins-fluvastatin and lovastatin-induced p21 expression as general histone deacetylase inhibitors in a p53-independent manner, which is mediated through various pathways, such as apoptosis, autophagy, cell cycle progression, and DNA damage, to be involved in the function of p21 in HeLa cells. Lovastatin 49-59 H3 histone pseudogene 16 Homo sapiens 68-71 30939155-5 2019 Our data showed that the statins-fluvastatin and lovastatin-induced p21 expression as general histone deacetylase inhibitors in a p53-independent manner, which is mediated through various pathways, such as apoptosis, autophagy, cell cycle progression, and DNA damage, to be involved in the function of p21 in HeLa cells. Lovastatin 49-59 H3 histone pseudogene 16 Homo sapiens 302-305 30939155-6 2019 The curative effect repositioning of digoxin, a cardiovascular medication, was combined with fluvastatin and lovastatin, and the results further implied that p21 induction is involved in a p53-dependent and p53-independent manner. Lovastatin 109-119 H3 histone pseudogene 16 Homo sapiens 158-161 21907187-4 2011 Western blot analysis revealed that lovastatin caused an increase of the protein level of p27 and cyclin-dependent kinase (CDK)4 and a decrease of the protein level of cyclin A2, cyclin D3, and phosphorylated Rb (pRb), but did not significantly change the protein levels of p21, cyclins D1 and E, and CDK2, in ARO cells. Lovastatin 36-46 H3 histone pseudogene 16 Homo sapiens 274-295 26713523-7 2015 Treatment with 2.5mumol/L SAHA significantly up-regulated the expression of p21 protein in 48 h, while the protein expression was reduced in combined treatment with 5mumol/L lovastatin. Lovastatin 174-184 H3 histone pseudogene 16 Homo sapiens 76-79 22294184-6 2012 A marked rise in the cell-cycle inhibitor p21, together with reduction of aurora kinases A and B, cyclins B1 and D1 proteins was induced by lovastatin alone or in combination with docetaxel. Lovastatin 140-150 H3 histone pseudogene 16 Homo sapiens 42-45 24556504-6 2014 Lovastatin supplementation arrested cells in the G0/G1 phase and enhanced expression levels of p21, whereas the conjugate did not demonstrate cell cycle arrest nor increased p21 expression. Lovastatin 0-10 H3 histone pseudogene 16 Homo sapiens 95-98 16985065-9 2006 All three statins (lovastatin, fluvastatin, and simvastatin) inhibited cyclin E/cdk2 kinase leading to hypophosphorylation of Rb, but this inhibition was correlated with a loss of the activating phosphorylation on Thr160 of cyclin E-associated cdk2 and not dependent on the cdk inhibitors p21 and p27. Lovastatin 19-29 H3 histone pseudogene 16 Homo sapiens 289-292 16467108-10 2006 Lovastatin affected various IR-induced stress responses in HUVEC: It attenuated the increase in p53/p21 protein level and impaired the activation of nuclear factor-kappaB, Chk-1, and Akt kinase but did not inhibit extracellular signal-regulated kinase activation. Lovastatin 0-10 H3 histone pseudogene 16 Homo sapiens 100-103 12434292-8 2002 In our previous report, we proved that lovastatin, a pharmacological inhibitor of p21(ras) function, also reversed the increase of cortisol level in mutant K-ras stably transfected human adrenocortical cells. Lovastatin 39-49 H3 histone pseudogene 16 Homo sapiens 82-85 11307620-3 2001 Lovastatin and phenylacetate promote p21 accumulation but fail to induce cell cycle arrest. Lovastatin 0-10 H3 histone pseudogene 16 Homo sapiens 37-40 10502413-4 1999 The induction of the CKIs by modulators of cAMP such as cholera toxin (CT) + 1-isobutyl-3-methylxanthine (IBMX) and lovastatin fluctuates with biphasic kinetics (although the kinetics of CKI induction with CT + IBMX treatment are different from that of lovastatin) and is depicted by the periodic accumulation of lower molecular weight forms of p21 and p27 which also correlate with fluctuations in CDK2 activity. Lovastatin 116-126 H3 histone pseudogene 16 Homo sapiens 345-348 10502413-9 1999 Last, treatment of MDA-MB-157 cells with lovastatin, another known cAMP modulator which also causes growth arrest, resulted in the induction of p21 and p27 without any increase in PKA activity. Lovastatin 41-51 H3 histone pseudogene 16 Homo sapiens 144-147 9811471-4 1998 However, the binding of p21 and p27 to CDK2 increases significantly following treatment of cells with lovastatin leading to inhibition of CDK2 activity and a subsequent arrest of cells in G1. Lovastatin 102-112 H3 histone pseudogene 16 Homo sapiens 24-27 10399961-4 1999 We show that p21 ras processing is blocked by lovastatin, suggesting that inhibition of isoprenylation may be important in lovastatin-induced apoptosis. Lovastatin 46-56 H3 histone pseudogene 16 Homo sapiens 13-16 10399961-4 1999 We show that p21 ras processing is blocked by lovastatin, suggesting that inhibition of isoprenylation may be important in lovastatin-induced apoptosis. Lovastatin 123-133 H3 histone pseudogene 16 Homo sapiens 13-16 9811471-0 1998 Lovastatin mediated G1 arrest in normal and tumor breast cells is through inhibition of CDK2 activity and redistribution of p21 and p27, independent of p53. Lovastatin 0-10 H3 histone pseudogene 16 Homo sapiens 124-127 9811471-2 1998 In the present study we have investigated the nature of the CKIs (p21 and p27) alterations resulting in G1 arrest in both normal and tumor breast cell lines by lovastatin. Lovastatin 160-170 H3 histone pseudogene 16 Homo sapiens 66-69 9811471-3 1998 We show that even though lovastatin treatment causes G1 arrest in a wide variety of normal and tumor breast cells irrespective of their p53 or pRb status, the p21 and p27 protein levels are not increased in all cell lines treated suggesting that the increase in p21 and p27 protein expression per se is not necessary for lovastatin mediated G1 arrest. Lovastatin 25-35 H3 histone pseudogene 16 Homo sapiens 262-265 9811471-5 1998 The increased CKI binding to CDK2 is achieved by the redistribution of both p21 and p27 from CDK4 to CDK2 complexes subsequent to decreases in CDK4 and cyclin D3 expression following lovastatin treatment. Lovastatin 183-193 H3 histone pseudogene 16 Homo sapiens 76-79 8425769-5 1993 Under the experimental conditions used, lovastatin prevented the membrane association, but not the biosynthesis, of p21. Lovastatin 40-50 H3 histone pseudogene 16 Homo sapiens 116-119 2278880-3 1990 Lovastatin, a competitive inhibitor of 3-hydroxy-3-methylglutaryl coenzyme A reductase, may prevent the farnesylation of de novo synthesized ras p21. Lovastatin 0-10 H3 histone pseudogene 16 Homo sapiens 145-148