BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells. - Wikidata - awgldk - TriplyDB

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

http://www.wikidata.org/entity/Q36548227

about

Cysteine cathepsins: their role in tumor progression and recent trends in the development of imaging probes Modeling vitamin D actions in triple negative/basal-like breast cancer.A fine-scale dissection of the DNA double-strand break repair machinery and its implications for breast cancer therapy.The impact of vitamin D in breast cancer: genomics, pathways, metabolism.DNA damage and lamins Methods to Monitor DNA Repair Defects and Genomic Instability in the Context of a Disrupted Nuclear Lamina.53BP1 expression is a modifier of the prognostic value of lymph node ratio and CA 19-9 in pancreatic adenocarcinoma.UbcH7 regulates 53BP1 stability and DSB repair The effect on quality of life of vitamin D administration for advanced cancer treatment (VIDAFACT study): protocol of a randomised controlled trial.Ectopic expression of RNF168 and 53BP1 increases mutagenic but not physiological non-homologous end joining.Genomic instability in human cancer: Molecular insights and opportunities for therapeutic attack and prevention through diet and nutrition.Cathepsin L targeting in cancer treatment.Muscadine grape skin extract can antagonize Snail-cathepsin L-mediated invasion, migration and osteoclastogenesis in prostate and breast cancer cells.Early breast cancer screening using iron/iron oxide-based nanoplatforms with sub-femtomolar limits of detection.Vitamin D/vitamin D receptor axis regulates DNA repair during oncogene-induced senescence.The two faces of DNA repair: disease and therapy.Novel roles of 1α,25(OH)2D3 on DNA repair provide new strategies for breast cancer treatment Targeting the Nuclear Cathepsin L CCAAT Displacement Protein/Cut Homeobox Transcription Factor-Epithelial Mesenchymal Transition Pathway in Prostate and Breast Cancer Cells with the Z-FY-CHO Inhibitor Regulatory cross-talk determines the cellular levels of 53BP1 protein, a critical factor in DNA repair.Cooperation between BRCA1 and vitamin D is critical for histone acetylation of the p21waf1 promoter and growth inhibition of breast cancer cells and cancer stem-like cells.Selective cancer targeting with prodrugs activated by histone deacetylases and a tumour-associated protease.Mechanisms of oncogene-induced genomic instability.Differences in 53BP1 and BRCA1 regulation between cycling and non-cycling cells.Vitamin D receptor signaling improves Hutchinson-Gilford progeria syndrome cellular phenotypes.Chronic Alcohol Exposure Decreases 53BP1 Protein Levels Leading to a Defective DNA Repair in Cultured Primary Cortical Neurons.Out-of-frame start codons prevent translation of truncated nucleo-cytosolic cathepsin L in vivo.Vitamin D deficiency accelerates ageing and age-related diseases: a novel hypothesis.MicroRNA-152 inhibits tumor cell growth while inducing apoptosis via the transcriptional repression of cathepsin L in gastrointestinal stromal tumor.Snail transcription factor NLS and importin β1 regulate the subcellular localization of Cathepsin L and Cux1.Clinical Impact of Cystatin C/Cathepsin L and Follistatin/Activin A Systems in Breast Cancer Progression: A Preliminary Report.Histone tail cleavage as a novel epigenetic regulatory mechanism for gene expression.PARP inhibitors: the journey from research hypothesis to clinical approval.Association of Epithelial Mesenchymal Transition with prostate and breast health disparities Down-regulation of cathepsin S and matrix metalloproteinase-9 via Src, a non-receptor tyrosine kinase, suppresses triple-negative breast cancer growth and metastasis

P2860

Q26827307-A7822FDC-ADFA-47C2-B23D-4AA16E3147F7 Q27693209-903F19BE-5C39-41AB-AE8D-F5309D926A7B Q33698648-F8583F5E-6B7F-460E-8A1B-EBFB96B480C0 Q33749897-D3E7DF0E-8113-47AF-BEE5-D2976474AA71 Q33844504-594B315A-BE55-41A4-A409-A0A256F79BA9 Q34525056-82D79640-9D24-4791-A466-66E48DC2A49C Q34636501-9A128DD7-DD6C-4D9F-839E-477DFDE2B92E Q34709157-D71FCDBF-A7A7-4C3D-B971-8090A7BC6EFD Q34799604-38F95C00-7A7C-441D-A05C-40CC0925385D Q35656738-CAA122CD-A7FE-472D-B011-50A0D32BE0E6 Q36144711-DBE80F8B-E29E-40A7-A3E9-405E4BF43525 Q36218199-C2DDF8C4-6864-4950-8929-6CC047F82F8E Q36276616-9E9EF839-5F9F-44C3-8E4C-66085ABB408A Q36991435-8C80383A-FB4E-4A12-9A26-C8DBC12BFE9C Q37309834-8607EF05-71B7-4418-B4B1-B9095ECA5E0C Q37662303-FDF9E9CC-6605-48DD-9DCE-3A0834C73775 Q37669695-FBDBCAA4-9983-4329-BB84-26A52513544D Q38726531-4FA5945C-58E0-4F66-AF97-73BC45DE8BF4 Q38932240-6D79FB73-868A-4561-9A61-8825335302BB Q38933663-B41F7BEA-E9F1-4A73-8B83-65D87F36B8C5 Q39066800-9DC68A8A-BE4B-426E-90C3-DD07F86ED2AC Q39078422-1DE0FDBA-CAB9-4BC3-988C-D3E7C9DFD7FE Q39087801-E8A0C413-2886-4E14-B808-2EF9D47C1558 Q41416839-8B181ADC-7A3E-4E38-9338-231F7B92608B Q41492449-55023091-FEC0-4F49-B714-03C599146C2C Q42682011-0FD88EC2-46D1-4199-BFEC-305E43D1102F Q46300548-1E81A59E-E1B4-4246-9B78-1F9CBC5191A2 Q49571147-9CB53E34-96C3-4C34-9C2E-CCC1B68DDF24 Q50534969-4F51025C-9DCC-4D65-846A-97657584633B Q51498595-C13E4E99-733E-4894-BE04-807967E346F1 Q51763123-9F9F4ACF-174C-4D12-AD0D-E489B515AC87 Q53682668-5D881293-A79A-4DB3-B02D-0712E10ADC3F Q58756554-3AFBAA6C-A013-4510-BF8A-AEB7A31E1AAA Q58763841-C2E74F47-23BA-4EB4-AD1A-DA58FF0104EF

P2860

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

http://www.wikidata.org/entity/Q36548227

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

@ast

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

@en

type

label

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

@ast

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

@en

prefLabel

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

@ast

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

@en

P1433

Q36548227-52CDA63B-4E0B-4594-9661-CEA9435708AF

P1476

Q36548227-0FA2CF64-84DD-45C8-97BB-9602897D6A58

P2093

Q36548227-02F6C45D-47FD-4E23-807E-8E210E7394BC

Q36548227-0F4F1E82-70E0-43CA-BF9C-EEC0AD8656B2

Q36548227-210E5B7B-F480-4884-8E02-99A910FF502F

Q36548227-3807DB4A-F3C7-49BD-B83C-969877F244B2

Q36548227-3E2BF533-F3C1-4128-B16C-AE6A3BF5B06E

Q36548227-3E9D9BB8-92B2-47BB-A2C5-DB0CA640402C

Q36548227-4960E43B-A87E-41F1-8841-1AFE52807F2C

Q36548227-59589072-BF3F-49AA-AD50-BA690FEB1F24

Q36548227-5C67A101-A680-442C-B57A-C872D268E72D

Q36548227-7214B624-6EF7-43A8-B1BA-966E43F0752A

P2860

Q36548227-0FE40212-EF2C-4284-9C4C-8D142C2E23B3

Q36548227-17A910F4-820D-4A3B-9912-8BDE8248EF59

Q36548227-1AD50F9E-55C6-465B-AE4E-D7BE341A15C7

Q36548227-1B64AF50-8D9F-434D-8BC3-3292579B4651

Q36548227-1E85DFF7-4FD4-4A61-8F02-71EE22E667FB

Q36548227-1EF2FD37-4AB1-4317-9715-C40BEE8C8A54

Q36548227-24C90BBC-F399-4B70-940F-667861C36CC4

Q36548227-3649F8E0-C009-46B0-AD86-7C11AA379C46

Q36548227-36BA705E-B64E-4E6B-9BF8-2491D6F60702

Q36548227-3E7E1E0D-52FF-4BAE-A168-ED63CB541D5F

P304

Q36548227-750E3AAA-21EE-43F6-901F-581353081637

P31

Q36548227-B5B909D3-0D42-44A4-BCEB-153AA2E72309

P356

Q36548227-F11E08B7-A7B2-4607-8DB4-D3D28F6BF0CF

P407

Q36548227-D47F9EDA-20A8-41AE-831D-8CBDADC9386D

P433

Q36548227-F2E8A2B6-EEAE-4F5B-A554-03BFC678FDC0

P478

Q36548227-4FABA990-D3F7-42DC-BFAB-BB4084592BE1

P577

Q36548227-485BCC06-DFB5-427A-9D48-C1D1C9C3F5B4

P5875

Q36548227-E7F71A30-0B54-4D05-9F56-FE6EAE663921

P698

Q36548227-AADEA90E-8BE3-4AFB-9C66-E4DCA7BEB8DF

P932

Q36548227-8B55B9C4-7D64-4F7C-A9F8-D300C0537597

P356

P1433

Journal of Cell Biology

P1476

BRCA1 loss activates cathepsin L-mediated degradation of 53BP1 in breast cancer cells.

@en

P2093

Abena B Redwood

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

Adriana Dusso

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

Anna Novell

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

David A Grotsky

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

Enrique Lerma

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

Ignacio Gonzalez-Suarez

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

Junran Zhang

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

Martin A Neumann

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

Monica Croke

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

Montserrat Martinez-Alonso

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

P2860

BRCA1 is associated with a human SWI/SNF-related complex: linking chromatin remodeling to breast cancer

BRCA1 affects global DNA methylation through regulation of DNMT1

53BP1 loss rescues BRCA1 deficiency and is associated with triple-negative and BRCA-mutated breast cancers

Inhibition of poly(ADP-ribose) polymerase in tumors from BRCA mutation carriers.

Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy

Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase

DNA damage-induced G2-M checkpoint activation by histone H2AX and 53BP1

A dual role for A-type lamins in DNA double-strand break repair

A selective requirement for 53BP1 in the biological response to genomic instability induced by Brca1 deficiency

P304

187-202

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

P31

scholarly article

P356

10.1083/JCB.201204053

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

P407

P433

2

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

P478

200

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

P577

2013-01-01T00:00:00Z

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

P5875

234822441

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

P698

23337117

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

P932

3549967

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