Quantitative analysis of ribosome–mRNA complexes at different translation stages-Reference-Cited by-同舟云学术

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Quantitative analysis of ribosome–mRNA complexes at different translation stages

Published:2009-11-11 Issue:3 Volume:38 Page:e15-e15
ISSN:0305-1048
Container-title:Nucleic Acids Research
language:en
Short-container-title:

Author:

Shirokikh Nikolay E.,Alkalaeva Elena Z.,Vassilenko Konstantin S.,Afonina Zhanna A.,Alekhina Olga M.,Kisselev Lev L.,Spirin Alexander S.

Publisher

Oxford University Press (OUP)

Subject

Genetics

Link

http://academic.oup.com/nar/article-pdf/38/3/e15/16768090/gkp1025.pdf

Reference28 articles.

1. Extension inhibition analysis of translation initiation complexes;Hartz;Methods Enzymol.,1988

2. Analysis of 40 S and 80 S complexes with mRNA as measured by sucrose density gradients and primer extension inhibition;Anthony;J. Biol. Chem.,1992

3. Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry;Pestova;Mol. Cell. Biol.,1996

4. In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3;Alkalaeva;Cell,2006

5. Toeprint analysis of the positioning of translation apparatus components at initiation and termination codons of fungal mRNAs;Sachs;Methods,2002

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1. Eukaryotic initiation factors eIF4F and eIF4B promote translation termination upon closed-loop formation;2024-09-10

2. DMDA-PatA mediates RNA sequence-selective translation repression by anchoring eIF4A and DDX3 to GNG motifs;Nature Communications;2024-09-02

3. Functional Activity of Isoform 2 of Human eRF1;International Journal of Molecular Sciences;2024-07-22

4. The impact of mRNA poly(A) tail length on eukaryotic translation stages;Nucleic Acids Research;2024-06-14

5. Pateamine A mediates RNA sequence-selective translation repression by anchoring eIF4A and DDX3 to GNG motifs;2023-09-21

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