JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins. - Wikidata - awgldk - TriplyDB

JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins.

JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins.

http://www.wikidata.org/entity/Q40568858

about

MUC1 oncoprotein blocks nuclear targeting of c-Abl in the apoptotic response to DNA damage Protein kinase A phosphorylates and regulates dimerization of 14-3-3 epsilon GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis and slows growth The interaction between casein kinase Ialpha and 14-3-3 is phosphorylation dependent Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle and cell death in neurons G2019S leucine-rich repeat kinase 2 causes uncoupling protein-mediated mitochondrial depolarization Mutually exclusive subsets of BH3-only proteins are activated by the p53 and c-Jun N-terminal kinase/c-Jun signaling pathways during cortical neuron apoptosis induced by arsenite The functional contrariety of JNK A house divided: ceramide, sphingosine, and sphingosine-1-phosphate in programmed cell death JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships 14-3-3 zeta as novel molecular target for cancer therapy Molecular mechanisms of liver injury and hepatocarcinogenesis: focusing on the role of stress-activated MAPK Tumor and host factors that may limit efficacy of chemotherapy in non-small cell and small cell lung cancer The regulation of Bax by c-Jun N-terminal protein kinase (JNK) is a prerequisite to the mitochondrial-induced apoptotic pathway Serine 58 of 14-3-3zeta is a molecular switch regulating ASK1 and oxidant stress-induced cell death MyD88-5 links mitochondria, microtubules, and JNK3 in neurons and regulates neuronal survival Edaravone protects cortical neurons from apoptosis by inhibiting the translocation of BAX and Increasing the interaction between 14-3-3 and p-BAD Hexavalent chromium-induced apoptosis of granulosa cells involves selective sub-cellular translocation of Bcl-2 members, ERK1/2 and p53 Differential profile of Nix upregulation and translocation during hypoxia/ischaemia in vivo versus in vitro JNK phosphorylates synaptotagmin-4 and enhances Ca2+-evoked release 14-3-3theta protects against neurotoxicity in a cellular Parkinson's disease model through inhibition of the apoptotic factor Bax Alcohol and thiamine deficiency trigger differential mitochondrial transition pore opening mediating cellular death c-Jun N-terminal kinase mediates mouse liver injury through a novel Sab (SH3BP5)-dependent pathway leading to inactivation of intramitochondrial Src.Hepatitis C virus infection promotes hepatic gluconeogenesis through an NS5A-mediated, FoxO1-dependent pathway.Bcl-x(L)-mediated changes in metabolic pathways of breast cancer cells: from survival in the blood stream to organ-specific metastasis.Bimodal regulation of FoxO3 by AKT and 14-3-3 Proteomic screen in the simple metazoan Hydra identifies 14-3-3 binding proteins implicated in cellular metabolism, cytoskeletal organisation and Ca2+ signalling 14-3-3 protein masks the DNA binding interface of forkhead transcription factor FOXO4.Mitogen-activated protein kinase signaling in male germ cell apoptosis in the rat The JNK inhibitor SP600125 enhances dihydroartemisinin-induced apoptosis by accelerating Bax translocation into mitochondria in human lung adenocarcinoma cells.c-Jun N-terminal kinase enhances MST1-mediated pro-apoptotic signaling through phosphorylation at serine 82 HSV-1 ICP27 induces apoptosis by promoting Bax translocation to mitochondria through interacting with 14-3-3θ.Vinblastine induces acute, cell cycle phase-independent apoptosis in some leukemias and lymphomas and can induce acute apoptosis in others when Mcl-1 is suppressed.c-Jun N-terminal kinase modulates oxidant stress and peroxynitrite formation independent of inducible nitric oxide synthase in acetaminophen hepatotoxicity.Akt-phosphorylated mitogen-activated kinase-activating death domain protein (MADD) inhibits TRAIL-induced apoptosis by blocking Fas-associated death domain (FADD) association with death receptor 4 Lack of neuroprotection of inhibitory peptides targeting Jun/JNK after transient focal cerebral ischemia in spontaneously hypertensive rats.Cellular stress/the unfolded protein response: relevance to sleep and sleep disorders.Protein modifications regulate the role of 14-3-3γ adaptor protein in cAMP-induced steroidogenesis in MA-10 Leydig cells.Serum cholesterol selectively regulates glucocorticoid sensitivity through activation of JNK Inositol hexakisphosphate kinase-2, a physiologic mediator of cell death.

P2860

Q24298896-BCEFFB18-8123-4DA6-A4B4-F12F1016277E Q24299787-7717E471-3742-428E-BAF8-A3E4CDE5E6F1 Q24308802-9203715B-ABA5-4B7F-BD2F-E32F468D97B6 Q24311162-BF9CE654-6EC5-4295-8B20-A583C7097E64 Q24313181-61C4CE5B-C819-441A-A8FE-7207D8DE2479 Q24339009-163195C7-8D80-41A1-9590-59EE12E3C6CF Q24534853-6802DC92-6944-41F7-A590-0A0FA9D1D62F Q24633325-992E7783-8EE7-49A5-BAC5-5D64687D463B Q24675372-0A9299B3-D32D-40A2-8900-FB487F39387C Q26741279-3E31EDB6-780D-4B5D-B587-EB9A14B2DE8E Q28264735-BA8DA0F8-E7DF-45B3-A848-08D901DD9EBB Q28384866-76D5088B-53AA-4B65-919C-C5ED113CBCB3 Q28396304-25A515A8-E816-4A5F-807B-7D1AC3B79641 Q28508684-42D2FFFA-DE60-4CBB-A199-43A2DF77CBF9 Q28510422-D05C0D89-3EF2-4C0E-8EAE-B5A7CF2B9B4E Q28512388-E467E4C1-ED55-4245-801B-3B11C5239408 Q28570114-DC62A483-AA8C-4947-8A9A-88E1252B14A1 Q28575955-7BC26300-AC8F-4C3D-BFE0-54AFE5C21308 Q28578192-9A17779A-AD6B-4D21-8C12-D281C1797B99 Q28584289-35F59E26-0A0D-4238-9D3B-1D80ECDFCE59 Q28742388-A4BAD82C-C84D-4587-94DE-A3332FBC2C52 Q29994621-EDF47744-9D2A-48AA-B1E0-0E6FCEAE4F23 Q30009024-17FF402B-673D-4809-AF86-C999977D6D1F Q30395512-0C4379C1-D129-4870-99F6-7E843F6DECFE Q33224181-D0FF3A49-E5C9-430E-A214-6E643BA2165E Q33289348-880CB6FA-97B6-4178-A92E-93254BBD56AD Q33291681-C73C6442-2BDF-4759-AE56-1AC53ED5EFCE Q33439373-76D714FE-2CB3-4246-A675-0B9373C88DDD Q33583761-8D4BBB7F-6FA6-4FD1-90C4-612E8F5DADC4 Q33657899-13D33B9A-C7C8-4FA1-BA26-07A256D48416 Q33673579-5E25D488-054D-4F26-ACB1-DD7DD747FCD9 Q33763388-2F0CDC05-8DA5-4719-82CB-6B8A21C639CB Q33780816-AAA06529-5A5A-4EEA-ABD7-5BDD65B057E8 Q33912798-2D00FC2C-ED49-42EE-82CB-ACFF7505C5BA Q33991166-158F07FE-B3F2-49F0-AE92-91472C1019AA Q34039925-EBD28E43-C4C9-4AA2-90A5-AC3A80676538 Q34241641-87A7FDB1-EA9B-42C4-95E0-10C9577B4656 Q34249076-04FEBEB4-0D6F-4562-8D52-F67688F5C2A5 Q34312197-73A8F863-BD72-447C-BF2E-380CC50E4B64 Q34366232-4E0632D2-C366-4062-AAA8-3FBE12414412

P2860

JNK promotes Bax translocation to mitochondria through phosphorylation of 14-3-3 proteins.

http://www.wikidata.org/entity/Q40568858

description

2004 nî lūn-bûn

@nan

2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

2004年论文

@zh

2004年论文

@zh-cn

name

JNK promotes Bax translocation ...... horylation of 14-3-3 proteins.

@en

type

label

JNK promotes Bax translocation ...... horylation of 14-3-3 proteins.

@en

prefLabel

JNK promotes Bax translocation ...... horylation of 14-3-3 proteins.

@en

P1433

Q40568858-964EA78D-C746-4423-A4B3-DF46FC6B5802

P1476

Q40568858-47ED76EC-C17F-4327-B15B-D23909543A7F

P2093

Q40568858-046EFAA3-282C-4AB1-BF70-7CF69F43B6CA

Q40568858-1B6F9ED9-898E-44AF-A51C-FF9AFDAE02F3

Q40568858-3F0F7202-D5A1-4398-8427-6C84A9911999

Q40568858-7BF73E26-ABAA-4FBF-B6EB-BF6A34C5082E

Q40568858-8184DCA7-B73A-4CB1-A353-8C538B4F9710

Q40568858-9C407367-D999-4047-98B4-D52CF57F3F3C

Q40568858-D3B09EB4-7414-4EEA-BE1A-6347FFCF1799

Q40568858-DBAA4F6A-7E2B-4506-B05E-D923CA87D1F4

Q40568858-F1B2D509-E3E6-47EA-83F8-F1FD41B607B8

P2860

Q40568858-0A53FF32-09CD-43BB-B76B-A9A302F92704

Q40568858-0B7AA533-5CF5-480E-BF3A-A5BBCEA1C370

Q40568858-151CF6EF-C76B-485B-BAF5-220D5F555584

Q40568858-1F19579E-E400-43D9-A747-33DF83300F6A

Q40568858-2342D0F7-103B-4BD3-8019-59057E6458D6

Q40568858-26DCD5CA-E3BE-40FE-9171-3646809A8C6E

Q40568858-2913C580-97DA-4316-934C-B9B3C6C5AF7D

Q40568858-2AA13C13-422D-4AB2-92BA-C3749AEF0946

Q40568858-3246CA70-3B3F-4FA6-8D01-486FB732357D

Q40568858-34801DF8-8CBE-44E5-8DB3-B200091FABBE

P304

Q40568858-A60D615B-669D-4679-B530-84C795C5251E

P31

Q40568858-763C10A6-EA71-488D-BE8D-0D8993E75B2C

P356

Q40568858-DCABFAD4-EB64-4099-A934-E2EBA843D354

P407

Q40568858-E47F072C-F6A6-4F99-9549-33A42DD927EE

P433

Q40568858-A74BD981-1DC5-4438-8A22-7D554E01EE84

P478

Q40568858-408B6CF5-703D-478E-A0E6-C7A24AFF36B2

P577

Q40568858-BA612A66-DEB1-40F6-8067-6D0E445823A5

P5875

Q40568858-E64E4DF0-922C-4564-904A-998F9AD8312E

P698

Q40568858-51CC83A0-75FD-4BC1-8685-FFF057B5D515

P921

Q40568858-60E12AD5-3B45-4A75-8411-6FF8EBA55FCB

Q40568858-F180CBB9-B372-48AB-84C6-381529808D8D

P932

Q40568858-A4CEAB10-0D81-40CF-BA04-00AC06211457

P356

SJ.EMBOJ.7600194

P1433

The EMBO Journal

P1476

JNK promotes Bax translocation ...... horylation of 14-3-3 proteins.

@en

P2093

Fuminori Tsuruta

http://www.w3.org/2001/XMLSchema#string

Jun Sunayama

http://www.w3.org/2001/XMLSchema#string

Katsuji Yoshioka

http://www.w3.org/2001/XMLSchema#string

Norihisa Masuyama

http://www.w3.org/2001/XMLSchema#string

Seisuke Hattori

http://www.w3.org/2001/XMLSchema#string

Shigeomi Shimizu

http://www.w3.org/2001/XMLSchema#string

Yasunori Mori

http://www.w3.org/2001/XMLSchema#string

Yoshihide Tsujimoto

http://www.w3.org/2001/XMLSchema#string

Yukiko Gotoh

http://www.w3.org/2001/XMLSchema#string

P2860

Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC

The G2/M regulator 14-3-3sigma prevents apoptosis through sequestration of Bax

Humanin peptide suppresses apoptosis by interfering with Bax activation

Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

Conformation of the Bax C-terminus regulates subcellular location and cell death

The Bax subfamily of Bcl2-related proteins is essential for apoptotic signal transduction by c-Jun NH(2)-terminal kinase

Phosphorylation of Thr-948 at the C terminus of the plasma membrane H(+)-ATPase creates a binding site for the regulatory 14-3-3 protein

JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis

Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis

P304

1889-1899

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/SJ.EMBOJ.7600194

http://www.w3.org/2001/XMLSchema#string

P407

P433

8

http://www.w3.org/2001/XMLSchema#string

P478

23

http://www.w3.org/2001/XMLSchema#string

P577

2004-04-08T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

8629328

http://www.w3.org/2001/XMLSchema#string

P698

15071501

http://www.w3.org/2001/XMLSchema#string

P921

phosphorylation

P932

394248

http://www.w3.org/2001/XMLSchema#string