Charged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins (Q34166278)

31 July 2017

title

Charged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins (English)

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31 July 2017

1 reference

Andrew J McCluskey

1

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31 July 2017

Eleonora Bolewska-Pedyczak

2

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31 July 2017

Nick Jarvik

3

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31 July 2017

Gang Chen

4

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31 July 2017

Sachdev S Sidhu

5

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31 July 2017

Jean Gariépy

6

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31 July 2017

language of work or name

English

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publication date

15 February 2012

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31 July 2017

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31 July 2017

volume

7

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31 July 2017

issue

2

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31 July 2017

page(s)

e31191

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Creative Commons Attribution 4.0 International

31 July 2017

copyright license

start time

15 February 2012

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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The C-terminal fragment of the ribosomal P protein complexed to trichosanthin reveals the interaction between the ribosome-inactivating protein and the ribosome

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The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae

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Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses

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The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins

5 July 2018

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The acidic protein binding site is partially hidden in the free Saccharomyces cerevisiae ribosomal stalk protein P0.

5 July 2018

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

5 July 2018

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5 July 2018

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5 July 2018

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5 July 2018

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5 July 2018

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5 July 2018

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5 July 2018

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5 July 2018

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DOI

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31 July 2017

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31 July 2017

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