Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome.

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Human ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Functional Assays for Measuring the Catalytic Activity of Ribosome Inactivating Proteins.

P2860

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Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome.

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http://www.wikidata.org/entity/Q38745809

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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name

Toxicity of ricin A chain is r ...... interaction with the ribosome.

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Toxicity of ricin A chain is r ...... interaction with the ribosome.

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Toxicity of ricin A chain is r ...... interaction with the ribosome.

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P1476

Toxicity of ricin A chain is r ...... interaction with the ribosome.

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P2093

Amanda E Jetzt

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Nilgun E Tumer

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

Wendie S Cohick

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Xiao-Ping Li

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P2860

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7-Substituted pterins provide a new direction for ricin A chain inhibitors

Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B

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Small-molecule inhibitor leads of ribosome-inactivating proteins developed using the doorstop approach

Shiga toxins stimulate secretion of interleukin-8 from intestinal epithelial cells.

The A1 Subunit of Shiga Toxin 2 Has Higher Affinity for Ribosomes and Higher Catalytic Activity than the A1 Subunit of Shiga Toxin 1.

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120-128

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scholarly article

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10.1016/J.TAAP.2016.09.004

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310

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2016-09-14T00:00:00Z

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27639428

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P932

5079286

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Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome.

about

P2860

P2860

Toxicity of ricin A chain is reduced in mammalian cells by inhibiting its interaction with the ribosome.

description

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P1433

P1476

P2093

P2860

P304

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P356

P478

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P698

P932

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P1433

P1476

P2093

P2860

P304

P31

P356

P478

P577

P698

P932