SILAC-based quantitative proteomic analysis of human lung cell response to copper oxide nanoparticles. - Test2 - elhamkhani - TriplyDB

SILAC-based quantitative proteomic analysis of human lung cell response to copper oxide nanoparticles.

SILAC-based quantitative proteomic analysis of human lung cell response to copper oxide nanoparticles.

http://www.wikidata.org/entity/Q34627914

about

Comparative proteomic analysis of the molecular responses of mouse macrophages to titanium dioxide and copper oxide nanoparticles unravels some toxic mechanisms for copper oxide nanoparticles in macrophages.Plumbagin suppresses epithelial to mesenchymal transition and stemness via inhibiting Nrf2-mediated signaling pathway in human tongue squamous cell carcinoma cells.Copper oxide nanoparticle toxicity profiling using untargeted metabolomics Can CuO nanoparticles lead to epigenetic regulation of antioxidant enzyme system?Systems Biology to Support Nanomaterial Grouping.Role of omics techniques in the toxicity testing of nanoparticles.Biological responses to nanomaterials: understanding nano-bio effects on cell behaviors.

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SILAC-based quantitative proteomic analysis of human lung cell response to copper oxide nanoparticles.

http://www.wikidata.org/entity/Q34627914

description

2014 nî lūn-bûn

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2014 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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SILAC-based quantitative prote ...... to copper oxide nanoparticles.

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SILAC-based quantitative prote ...... to copper oxide nanoparticles.

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SILAC-based quantitative prote ...... to copper oxide nanoparticles.

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SILAC-based quantitative prote ...... to copper oxide nanoparticles.

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SILAC-based quantitative prote ...... to copper oxide nanoparticles.

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SILAC-based quantitative prote ...... to copper oxide nanoparticles.

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SILAC-based quantitative prote ...... to copper oxide nanoparticles.

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Bindu Nanduri

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Caitlin D Naske

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Keisha B Walters

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Leslie A Shack

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Mariola J Edelmann

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P2860

USP47 is a deubiquitylating enzyme that regulates base excision repair by controlling steady-state levels of DNA polymerase β

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis

The THAP domain of THAP1 is a large C2CH module with zinc-dependent sequence-specific DNA-binding activity

The THAP-zinc finger protein THAP1 regulates endothelial cell proliferation through modulation of pRB/E2F cell-cycle target genes

Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress

Structural basis and specificity of human otubain 1-mediated deubiquitination

Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1

The human THAP9 gene encodes an active P-element DNA transposase

Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting with the eukaryotic translation initiation factor 3 subunit p44 (eIF3g)

Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain

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