14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
about
sameAs
JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of c-Abl in the apoptotic response to DNA damageRsk-mediated phosphorylation and 14-3-3ɛ binding of Apaf-1 suppresses cytochrome c-induced apoptosisRegulation of MDMX nuclear import and degradation by Chk2 and 14-3-3.Protein phosphatase 2A dephosphorylation of phosphoserine 112 plays the gatekeeper role for BAD-mediated apoptosisThe permeability transition pore triggers Bax translocation to mitochondria during neuronal apoptosisProteomic and biochemical analysis of 14-3-3-binding proteins during C2-ceramide-induced apoptosisLoss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosisA house divided: ceramide, sphingosine, and sphingosine-1-phosphate in programmed cell deathCell cycle regulators guide mitochondrial activity in radiation-induced adaptive responseProtein kinase Cepsilon interacts with Bax and promotes survival of human prostate cancer cells14-3-3 proteins--an updateThe Cytotoxicity Mechanism of 6-Shogaol-Treated HeLa Human Cervical Cancer Cells Revealed by Label-Free Shotgun Proteomics and Bioinformatics AnalysisEdaravone protects cortical neurons from apoptosis by inhibiting the translocation of BAX and Increasing the interaction between 14-3-3 and p-BADBid activation in kidney cells following ATP depletion in vitro and ischemia in vivoMelatonin attenuates the focal cerebral ischemic injury by inhibiting the dissociation of pBad from 14-3-3Differential profile of Nix upregulation and translocation during hypoxia/ischaemia in vivo versus in vitroThe lysosome-associated apoptosis-inducing protein containing the pleckstrin homology (PH) and FYVE domains (LAPF), representative of a novel family of PH and FYVE domain-containing proteins, induces caspase-independent apoptosis via the lysosomal-m14-3-3theta protects against neurotoxicity in a cellular Parkinson's disease model through inhibition of the apoptotic factor BaxLoss of function of Ywhah in mice induces deafness and cochlear outer hair cells' degeneration.No widespread induction of cell death genes occurs in pure motoneurons in an amyotrophic lateral sclerosis mouse model.LongSAGE analysis of skeletal muscle at three prenatal stages in Tongcheng and Landrace pigsProteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca2+ signallingCooperative effect of p21Cip1/WAF-1 and 14-3-3sigma on cell cycle arrest and apoptosis induction by p14ARF.14-3-3sigma Modulates pancreatic cancer cell survival and invasivenessA megakaryocyte with no platelets: anti-platelet antibodies, apoptosis, and platelet production.HSV-1 ICP27 induces apoptosis by promoting Bax translocation to mitochondria through interacting with 14-3-3θ.Peroxisome Proliferator-Activated Receptors Protect against Apoptosis via 14-3-3.Muscarinic receptor activation protects cells from apoptotic effects of DNA damage, oxidative stress, and mitochondrial inhibitionPhosphorylation of 14-3-3ζ at serine 58 and neurodegeneration following kainic acid-induced excitotoxicity.Genomic analysis reveals pre- and postchallenge differences in a rhesus macaque AIDS vaccine trial: insights into mechanisms of vaccine efficacyMiR-27a functions as a tumor suppressor in acute leukemia by regulating 14-3-3θ.System in biology leading to cell pathology: stable protein-protein interactions after covalent modifications by small molecules or in transgenic cells.Regulated cell death in AKI.Levels of pro-apoptotic regulator Bad and anti-apoptotic regulator Bcl-xL determine the type of the apoptotic logic gate.Altered expression of 14-3-3ζ protein in spinal cords of rat fetuses with spina bifida apertaMetabolic control of oocyte apoptosis mediated by 14-3-3zeta-regulated dephosphorylation of caspase-2Differential expression of 14-3-3 isoforms in human alcoholic brain.Differential protective effects of exenatide, an agonist of GLP-1 receptor and Piragliatin, a glucokinase activator in beta cell response to streptozotocin-induced and endoplasmic reticulum stressesComparative proteomic analysis of the hepatic response to heat stress in Muscovy and Pekin ducks: insight into thermal tolerance related to energy metabolismMolecular mechanisms of 3,3'-dichlorobenzidine-mediated toxicity in HepG2 cells.
P2860
Q24294273-8BC53A7A-A933-4C73-A7F5-912F8AAE0A8EQ24301885-68EA6E7B-924C-4F23-8274-22706B435263Q24306287-BA288F82-FD63-49B4-845B-89335918F276Q24318719-665E7508-68A9-4E97-A106-09C31652A163Q24337594-5F2FBF60-2789-40B4-997C-F984A7E83526Q24338378-196733E3-CF7D-477A-8A4B-9096F915B3AFQ24534937-0B4B9BF5-A479-4403-BE36-9645418C0591Q24675372-6876DB9D-85DB-4C3A-9393-A5A3E7734CD0Q27014767-82537EA0-72B8-4BB6-89CB-32D6CAAE0B9EQ28206601-6B2B6E7F-7202-4DDD-BF83-D39113391E44Q28247242-43EF949F-0BFB-4BD6-A5F7-FF95B5581A14Q28391923-91324D86-F93F-4954-976F-949E0A715CF8Q28570114-F7C13918-A9DF-4FDC-BFCA-A6B5784959C2Q28571372-68742133-41C6-42E2-AB43-109BE96F750CQ28576697-93D43804-5195-4D90-95E1-110978091CEAQ28578192-603A7F82-935E-4F2E-98D2-E91BAF45674BQ28591419-8A38EDD0-EE35-4D84-A8BB-0EAA25414D84Q28742388-E1C2ED20-8ED5-4344-82B6-52E173B9CBE3Q30382075-8FAF560B-3EF8-420E-880D-184A5C9E5421Q33224176-301415E0-1CE3-4B5A-B462-C4780C5925FCQ33287976-C87852D6-10DF-4533-B977-CC733DB4A9C5Q33291681-E5581A4D-BB05-48D7-B084-D42252357997Q33370904-1690C6CA-FCB2-4916-A61D-907D772183FCQ33388611-A34BF704-8038-4A04-A0F9-1A61B87A6F35Q33402025-071BDA28-FE06-41B5-A498-5F602A1FD0ECQ33763388-A8DD4AC2-710E-49ED-B376-290E81E8FCB1Q34123741-65B4A330-6943-4384-9F57-ED3C177B5C60Q34338754-0DF58FEA-9CDC-4D6B-8AF8-5EA8B76B02C6Q34389442-D161DC6A-9B1A-42B6-9B1B-9A6925BA2E3CQ34485178-BBA69C24-08A8-4353-80DB-FACA5710CD96Q34510548-9447A632-A584-432D-8824-71F79BC1D8FFQ34564273-F30E458A-2E9D-462C-9D27-3756B43B3799Q34568839-9B4DC30B-1812-4E4B-99A6-A45340C840F8Q34863536-33C70D92-5C3A-4621-A608-4764DF7626AFQ34925869-1178C15A-55D1-4B9C-9512-0EBA9F41D8F9Q34987200-4ACA31DE-5EA2-4A3A-B4AB-7B2C62A7E640Q34990168-A2C54BA9-B769-4AE1-A521-87C2079E9260Q34998652-E22F4628-0A30-4BF2-8135-8F2E59F2F23BQ35014970-CD3E1E13-FFF8-4C87-A06C-4459D855739CQ35113557-A61FE942-5A1F-4548-BE5B-CE88EC6C9DFF
P2860
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
description
2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2003
@ast
im Januar 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific article (publication date: 17 January 2003)
@en
vedecký článok (publikovaný 2003/01/17)
@sk
vědecký článek publikovaný v roce 2003
@cs
wetenschappelijk artikel (gepubliceerd op 2003/01/17)
@nl
наукова стаття, опублікована в січні 2003
@uk
name
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@ast
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@en
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@nl
type
label
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@ast
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@en
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@nl
prefLabel
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@ast
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@en
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@nl
P2093
P2860
P356
P1476
14-3-3 Interacts directly with and negatively regulates pro-apoptotic Bax
@en
P2093
Hikaru Matsuda
Masaya Nomura
Shigeomi Shimizu
Toshinori Ito
Yoshihide Tsujimoto
P2860
P304
P356
10.1074/JBC.M207880200
P407
P577
2003-01-17T00:00:00Z