Mutant p53 gain of function: reduction of tumor malignancy of human cancer cell lines through abrogation of mutant p53 expression. - Wikidata - wikimedia - TriplyDB

Mutant p53 gain of function: reduction of tumor malignancy of human cancer cell lines through abrogation of mutant p53 expression.

Mutant p53 gain of function: reduction of tumor malignancy of human cancer cell lines through abrogation of mutant p53 expression.

http://www.wikidata.org/entity/Q46709821

about

Modulation of the vitamin D3 response by cancer-associated mutant p53 Mutant p53 and ETS2, a Tale of Reciprocity Mutant p53: One, No One, and One Hundred Thousand The Contrived Mutant p53 Oncogene - Beyond Loss of Functions Mutant p53: Multiple Mechanisms Define Biologic Activity in Cancer Links between mutant p53 and genomic instability Resistance and gain-of-resistance phenotypes in cancers harboring wild-type p53 The rebel angel: mutant p53 as the driving oncogene in breast cancer.Emerging Non-Canonical Functions and Regulation by p53: p53 and Stemness p53 as a Regulator of Lipid Metabolism in Cancer Novel role of PELP1 in regulating chemotherapy response in mutant p53-expressing triple negative breast cancer cells Predicting transcriptional activity of multiple site p53 mutants based on hybrid properties miR-600 inhibits cell proliferation, migration and invasion by targeting p53 in mutant p53-expressing human colorectal cancer cell lines.Mutant p53 gain-of-function in cancer.Degradation of mutant p53H175 protein by Zn(II) through autophagy.Mutant p53-induced up-regulation of mitogen-activated protein kinase kinase 3 contributes to gain of function Characterization of functional domains necessary for mutant p53 gain of function.Cys-141 glutathionylation of human p53: Studies using specific polyclonal antibodies in cancer samples and cell lines.Protein identification using customized protein sequence databases derived from RNA-Seq data.Selective depletion of mutant p53 by cancer chemopreventive isothiocyanates and their structure-activity relationships Down-regulation of the antisense mitochondrial non-coding RNAs (ncRNAs) is a unique vulnerability of cancer cells and a potential target for cancer therapy.Estradiol agonists inhibit human LoVo colorectal-cancer cell proliferation and migration through p53 Mitotic arrest and apoptosis in breast cancer cells induced by Origanum majorana extract: upregulation of TNF-α and downregulation of survivin and mutant p53.Dominant-negative features of mutant TP53 in germline carriers have limited impact on cancer outcomes.Mutant p53 protein is targeted by arsenic for degradation and plays a role in arsenic-mediated growth suppression.Functional inactivation of endogenous MDM2 and CHIP by HSP90 causes aberrant stabilization of mutant p53 in human cancer cells A bioinformatics workflow for variant peptide detection in shotgun proteomics Upregulation of the mitochondrial transport protein, Tim50, by mutant p53 contributes to cell growth and chemoresistance Comparison of effects of p53 null and gain-of-function mutations on salivary tumors in MMTV-Hras transgenic mice.Trans-splicing repair of mutant p53 suppresses the growth of hepatocellular carcinoma cells in vitro and in vivo.SAHA shows preferential cytotoxicity in mutant p53 cancer cells by destabilizing mutant p53 through inhibition of the HDAC6-Hsp90 chaperone axis.Functional repair of p53 mutation in colorectal cancer cells using trans-splicing.MicroRNAs: short non-coding players in cancer chemoresistance.Cancer-derived p53 mutants suppress p53-target gene expression--potential mechanism for gain of function of mutant p53.Rhus coriaria induces senescence and autophagic cell death in breast cancer cells through a mechanism involving p38 and ERK1/2 activation.MicroRNA-128-2 targets the transcriptional repressor E2F5 enhancing mutant p53 gain of function CCN5/WISP-2: A micromanager of breast cancer progression Mutant p53: one name, many proteins.Zn(II)-curc targets p53 in thyroid cancer cells Evolutionary Action Score of TP53 Coding Variants Is Predictive of Platinum Response in Head and Neck Cancer Patients

P2860

Q24302430-BDFCEB8B-E1EA-476F-B377-526260BCD3FF Q26765746-63E9CA0F-E821-4E12-A30D-C615101A7568 Q26770576-EF169425-3D1B-4CB0-A43D-5B03160AF126 Q26772237-D974F79C-B1B8-440C-9D02-610E99FAEE3F Q26776020-098158F8-AF9F-40FA-ACB6-F19F23DD4BA3 Q26864033-D8DB4EBB-B1FA-486D-82A7-A267CC834B0B Q27006998-A650CFD9-B1C2-4C5D-B76F-3E4DEFDB460C Q27686765-BE51946A-F7CB-40B4-B246-B6E533905FD5 Q28077156-011184B4-2AB7-4776-91BE-2E7B1527528A Q28079393-61C089E7-31DE-432B-AE50-ED894708810C Q28259152-63F3BC20-1F46-44D8-94F0-6F8214FF3A7F Q28476462-3619ED3F-3B0C-4AE3-AC56-154DE81E42C1 Q33599315-CC47928E-1A69-45A5-9444-BBB77363B5FC Q33687048-0273AE0E-051A-47E5-AAF5-4090B5C36F70 Q33709136-1245AAD4-9F1C-42BA-B85D-49CAA755E4CA Q33825046-A1EA0115-1C64-4E22-A0FD-72B1B3E6CE17 Q33825155-2BEF4C76-1CA1-4E0B-B1E0-CCBBDA4A8998 Q34040102-6446FE13-ED79-438F-B590-52BCF37F9822 Q34079606-FA65AE44-C2CC-4994-B302-7ED6A7D2536E Q34159403-61A8FDEA-5F37-46C9-B8F1-57A9DC7F0052 Q34245117-76A71F69-97AE-4292-998E-EFB8C8871614 Q34589775-1D3556DF-7806-40CE-A2EC-8506BCD5566D Q34602465-14DA06DE-7894-45A9-9E47-476EC52BE2ED Q34802295-032E6958-0DE6-4B3A-BBD9-26487412380F Q34978872-66A56127-1CD2-4B56-8C8B-CEF3855F1F9A Q34989395-0E0079F7-EC2E-4B45-9309-DE9CB5888F9F Q34994365-8B49BEEF-56B0-4AAC-9CA6-8B41545C2A68 Q35086367-CB018635-FCF2-48CD-BBDA-F5C4AF0B8FEE Q35103336-AFFE40B1-F91B-4C6C-A80B-AAD700BEBF6E Q35138721-9EFB38BA-4472-465E-911F-3674312ED95B Q35207366-DC5EA03D-9B94-4280-8BC4-2C8F05AA3AC0 Q35273347-74D375AB-E6EB-459B-8A42-187D63E9E4AE Q35673637-DE9C6F09-F501-4781-83E6-44579FEAE795 Q35804653-099B40F5-D99A-435F-9E33-90FDBB0D6FB2 Q35942243-9D9C8B93-0569-4A35-9A2A-DACDD0B3F643 Q35965859-0671B800-E02D-450F-878C-A38A745796C8 Q36010510-91506CF7-82FA-47A2-90AD-C4F0C2DC7EDB Q36070574-B5EFB612-6D29-4AB2-BD97-6D11C1C8D09A Q36094135-D12F61A8-76D0-4146-AF36-9B575A677277 Q36191292-D4B65145-A172-4215-BB29-276A9E95A3D9

P2860

Mutant p53 gain of function: reduction of tumor malignancy of human cancer cell lines through abrogation of mutant p53 expression.

http://www.wikidata.org/entity/Q46709821

description

2006 nî lūn-bûn

@nan

2006年の論文

@ja

2006年学术文章

@wuu

2006年学术文章

@zh

2006年学术文章

@zh-cn

2006年学术文章

@zh-hans

2006年学术文章

@zh-my

2006年学术文章

@zh-sg

2006年學術文章

@yue

2006年學術文章

@zh-hant

name

Mutant p53 gain of function: r ...... tion of mutant p53 expression.

@en

Mutant p53 gain of function: r ...... tion of mutant p53 expression.

@nl

type

label

Mutant p53 gain of function: r ...... tion of mutant p53 expression.

@en

Mutant p53 gain of function: r ...... tion of mutant p53 expression.

@nl

prefLabel

Mutant p53 gain of function: r ...... tion of mutant p53 expression.

@en

Mutant p53 gain of function: r ...... tion of mutant p53 expression.

@nl

P1433

Q46709821-EDA68582-85A4-4177-94FC-5ABC174674B7

P1476

Q46709821-83A5AA55-0030-494C-9DF5-DC5086A3916C

P2093

Q46709821-01EFEA4A-159B-4041-AEFE-2D5880024C07

Q46709821-0831DF88-6999-4F11-8911-7A2A1AC31D43

Q46709821-13E24D75-0B3D-4368-867E-CBEB4BB9BE83

Q46709821-67B596DD-2468-4168-8B75-21B9535FACE2

Q46709821-8B606AA6-6755-4053-A2F1-B8B8A90AB7E9

Q46709821-F036F573-A664-43C0-95B1-9D2E0EE2FA8D

P2860

Q46709821-0178EBF0-9ACE-4BCC-A921-8C6E8774AEE4

Q46709821-096CDEA1-A385-4CB3-92B8-98F50C2C46DF

Q46709821-2092AF15-D56A-45A1-A21B-9DDF48184317

Q46709821-2FC71CC5-7014-4AF7-82EC-8BE9F464BA00

Q46709821-50E5093C-8A32-4BC3-95F9-2201E2E89792

Q46709821-64D68DB9-C8E0-4440-A497-E3E40FDF93F1

Q46709821-71204802-22F7-4BEE-8F4E-34A9029D0E0F

Q46709821-75D12361-42CD-4D35-819A-57C4B729F2A4

Q46709821-7AA5D6A9-5837-4B9F-BE04-4BA64C43D626

Q46709821-8A0C932B-2F58-47D0-863A-2A6E9CA14928

P2888

Q46709821-EC8CEF2E-959F-4884-B6C8-1555C95AD863

P304

Q46709821-50B87F63-B99C-4CF3-A312-4D3010FF9744

P31

Q46709821-DC3371D7-10CE-47BD-8326-14D31097112E

P356

Q46709821-F78BEF38-D314-4A1D-B995-549E70A1730B

P407

Q46709821-1E1FD660-B696-4740-932A-251298AF41FF

P433

Q46709821-E0CD4DB8-9E78-4052-977B-B2C6E2647D6F

P478

Q46709821-8C7E0959-2AC7-492F-ADAC-B417869AB6C9

P577

Q46709821-31EFB883-6FDA-45F5-A670-C3CCE85A030D

P5875

Q46709821-CF86D564-F408-4C3A-8115-AA77C586DD75

P6179

Q46709821-C5B64163-37E9-4A6B-A86C-8E3F2C290D93

P698

Q46709821-D77BD562-403C-4854-AEDA-567CAD590EC5

P356

P1433

P1476

Mutant p53 gain of function: r ...... tion of mutant p53 expression.

@en

P2093

Blandino G

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

Bossi G

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

Lapi E

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

Rinaldo C

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

Sacchi A

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

Strano S

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

P2860

A system for stable expression of short interfering RNAs in mammalian cells

The effects of wild-type p53 tumor suppressor activity and mutant p53 gain-of-function on cell growth.

Identification of a minimal transforming domain of p53: negative dominance through abrogation of sequence-specific DNA binding.

Transactivation of the EGR1 gene contributes to mutant p53 gain of function.

Activation of c-myc gene expression by tumor-derived p53 mutants requires a discrete C-terminal domain.

Tumor-derived p53 mutants induce oncogenesis by transactivating growth-promoting genes.

Mutant p53 cooperates with ETS and selectively up-regulates human MDR1 not MRP1.

'Gain of function' phenotype of tumor-derived mutant p53 requires the oligomerization/nonsequence-specific nucleic acid-binding domain.

Gain of function mutations in p53.

p53-R175H mutant gains new function in regulation of doxorubicin-induced apoptosis.

P2888

P304

304-309

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

P31

scholarly article

P356

10.1038/SJ.ONC.1209026

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

P407

P433

2

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

P478

25

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

P577

2006-01-01T00:00:00Z

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

P5875

7594121

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

P6179

1050372970

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

P698

16170357

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