Proteolytic cleavage of the mdm2 oncoprotein during apoptosis.
about
Caspase-2-mediated cleavage of Mdm2 creates a p53-induced positive feedback loopA dual role of cyclin E in cell proliferation and apoptosis may provide a target for cancer therapyTranscription factor AP-2alpha is preferentially cleaved by caspase 6 and degraded by proteasome during tumor necrosis factor alpha-induced apoptosis in breast cancer cellsMDM2 interacts with MDMX through their RING finger domainsActivation of p53 signalling in acetylsalicylic acid-induced apoptosis in OC2 human oral cancer cellsMDMX stability is regulated by p53-induced caspase cleavage in NIH3T3 mouse fibroblastsIdentification of a CK2 phosphorylation site in mdm2.ATM activates p53 by regulating MDM2 oligomerization and E3 processivityMdm2: the ups and downs.Development and characterization of 5 canine B-cell lymphoma cell linesMolecular interaction map of the mammalian cell cycle control and DNA repair systems.Mdm2 links genotoxic stress and metabolism to p53.Autoactivation of the MDM2 E3 ligase by intramolecular interaction.The N-end rule pathway and regulation by proteolysisProteolytic cleavage of cyclin E leads to inactivation of associated kinase activity and amplification of apoptosis in hematopoietic cells.Inhibition of Mdm2 sensitizes human retinal pigment epithelial cells to apoptosis.MDM2 promotes ubiquitination and degradation of MDMXSynergistic activation of p53 by inhibition of MDM2 expression and DNA damage.Microvesicles from Mesenchymal Stromal Cells Are Involved in HPC-Microenvironment Crosstalk in Myelodysplastic Patients.Differential regulation of p21 (waf1) protein half-life by DNA damage and Nutlin-3 in p53 wild-type tumors and its therapeutic implications.Expression of caspases 3, 6 and 8 is increased in parallel with apoptosis and histological aggressiveness of the breast lesion.microRNA-1827 represses MDM2 to positively regulate tumor suppressor p53 and suppress tumorigenesis.Structurally novel steroidal spirooxindole by241 potently inhibits tumor growth mainly through ROS-mediated mechanismsRegulation of SirT1-nucleomethylin binding by rRNA coordinates ribosome biogenesis with nutrient availabilityXPO1 (CRM1) inhibition represses STAT3 activation to drive a survivin-dependent oncogenic switch in triple-negative breast cancer.A piRNA-like Small RNA Induces Chemoresistance to Cisplatin-Based Therapy by Inhibiting Apoptosis in Lung Squamous Cell Carcinoma.Colorectal cancer stem cells and cell death.MDM2 acts downstream of p53 as an E3 ligase to promote FOXO ubiquitination and degradation.Carboxyl-terminal proteolytic processing of CUX1 by a caspase enables transcriptional activation in proliferating cells.Critical loss of CBP/p300 histone acetylase activity by caspase-6 during neurodegeneration.Mechanisms of thymidine kinase/ganciclovir and cytosine deaminase/ 5-fluorocytosine suicide gene therapy-induced cell death in glioma cells.Estradiol stabilizes p53 protein in breast cancer cell line, MCF-7.Caspase-8 activation is necessary but not sufficient for tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-mediated apoptosis in the prostatic carcinoma cell line LNCaP.Exploitation of a non-apoptotic caspase to regulate the abundance of the cdkI p27(KIP1) in transformed lymphoid cells.p27KIP1 is down-regulated by two different mechanisms in human lymphoid cells undergoing apoptosis.Activation of an MDM2-specific caspase by p53 in the absence of apoptosis.Proteasome inhibitors induce mitochondria-independent apoptosis in human glioma cells.The role of Pten/Akt signaling pathway involved in BPA-induced apoptosis of rat Sertoli cells.Histopathological evaluation of apoptosis in cancer.Survivin regulates the p53 tumor suppressor gene family.
P2860
Q24310683-2BF1C396-402E-4272-B318-E72221CF3E0DQ24538802-555EDEA1-3F03-43C1-8EE0-4F92982A55BFQ24550911-ECD22310-AE22-4A29-AA0D-E0F8F92C282CQ28142437-F844CE6B-3739-42F4-A769-02A701863122Q28165459-9E8F8E97-F623-4E48-94D8-BC23DACA771BQ28200748-094AE184-F7AF-42A1-97BC-60238EFD940DQ30812794-5E095B9B-615E-4147-B1D9-2CCE9FAAE577Q33552958-143D7E8F-8A07-4718-8028-742F30EC3B6BQ33594040-1AA52D7A-ABAA-4089-A10F-FA8FDAFEAD7BQ33600546-43E0D184-3363-4479-8C8A-6FFB5148A255Q33704559-F3BE322E-A4D5-495A-8A36-05CE37598A28Q33788018-2C60AB27-0887-4B94-B6E5-7DEC21D261F7Q34056449-6FE0EA79-1E92-4047-99C1-FD0E9BE8C894Q34189152-E82304A6-DE85-465B-A9E5-4D58DC587122Q34275891-5C9E70F7-4D27-40A2-831A-1384091022EEQ35027581-14A7A9A2-D4A8-46CE-82B9-C5A1FED05ED7Q35161842-8BF871F1-26AF-45AB-AAE1-0ACC46DB8B77Q35671727-81C69C4A-9FE3-43BB-A431-CE48E9A64765Q35911998-DD311BA8-31CF-4B17-8BFB-0C0E9E9DE11BQ36289902-8791CB7A-2E77-40F6-AA35-67B0E044A195Q36619676-0217003D-5BD6-426C-B107-E4B120F6B994Q36962411-54A650A1-3795-4E67-ABBB-CF7FD7D084CAQ37177557-ADCEF846-C49A-42BD-8F1B-5B5CFBBF97ECQ37264969-A3F62BAE-7BD6-4041-AA38-D34BD807EF8DQ37637565-DBD84BF2-EE46-41EC-8547-E64239182352Q37718215-AAACE22C-B470-43EE-98E7-084D9AC689AAQ38161357-1430FB20-FDEC-4862-9BCD-63205BA7E018Q39868313-1965110B-68A5-4771-ABAB-C34C8621E164Q40097270-EA61D744-DB17-4D64-A135-C6D0CFC40B8BQ40323686-EC1D8664-DA74-4E43-9719-FD5E05B1DC53Q40481710-578D7732-F53C-455D-AB68-4202774A0F13Q40652110-7DBC7BBD-2F04-4315-BA23-903B5D80C14FQ40734169-8BC3A40A-8FB0-44A9-9DEB-7C6B82867466Q40796996-6C68CEFC-6185-4B6E-B433-6247F7F0F450Q40871184-2550DB5A-A846-4F8A-B372-01BF31A41D4DQ40954121-A7C18214-426C-48B6-9FE1-D6107AD55549Q40973489-D885DB32-2E1F-4468-9CD1-E54DA28F7A81Q42707163-E28782E4-E6E9-4F13-8BC7-1CDBE075CEABQ42850802-05948238-F28D-4A93-9A7A-4A945D862C66Q45054535-7728AC01-DE8F-4566-AAF7-356C7DBF07A7
P2860
Proteolytic cleavage of the mdm2 oncoprotein during apoptosis.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Proteolytic cleavage of the mdm2 oncoprotein during apoptosis.
@en
type
label
Proteolytic cleavage of the mdm2 oncoprotein during apoptosis.
@en
prefLabel
Proteolytic cleavage of the mdm2 oncoprotein during apoptosis.
@en
P2093
P2860
P356
P1476
Proteolytic cleavage of the mdm2 oncoprotein during apoptosis.
@en
P2093
P2860
P304
22966-22973
P356
10.1074/JBC.272.36.22966
P407
P577
1997-09-01T00:00:00Z