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Genetics|November 18, 2021
uS5/Rps2 residues at the 40S ribosome entry channel enhance initiation at suboptimal start codons in vivoJinsheng Dong, Alan G Hinnebusch
Genes & Development|May 23, 2002
Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2Hongfang Qiu, Cuihua Hu, Jinsheng Dong, et al.
Molecular and Cellular Biology|July 20, 2007
Yeast cap binding complex impedes recruitment of cleavage factor IA to weak termination sitesChi-Ming Wong, Hongfang Qiu, Cuihua Hu, et al.
Molecular and Cellular Biology|September 1, 2010
The beta/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivoKamal Dev, Hongfang Qiu, Jinsheng Dong, et al.
Molecular and Cellular Biology|November 2, 2005
The novel ATP-binding cassette protein ARB1 is a shuttling factor that stimulates 40S and 60S ribosome biogenesisJinsheng Dong, Ruby Lai, Jennifer L Jennings, et al.
Nucleic Acids Research|October 14, 2021
Large-scale movement of eIF3 domains during translation initiation modulate start codon selectionJose L Llácer, Tanweer Hussain, Jinsheng Dong, et al.
The Journal of Biological Chemistry|July 28, 2004
The essential ATP-binding cassette protein RLI1 functions in translation by promoting preinitiation complex assemblyJinsheng Dong, Ruby Lai, Klaus Nielsen, et al.
The Journal of Biological Chemistry|January 20, 2006
The essential vertebrate ABCE1 protein interacts with eukaryotic initiation factorsZhang-Qun Chen, Jinsheng Dong, Akihiko Ishimura, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 4, 2004
Recruitment of the ArgR/Mcm1p repressor is stimulated by the activator Gcn4p: a self-checking activation mechanismSungpil Yoon, Chhabi K Govind, Hongfang Qiu, et al.
Letters in Applied Microbiology|January 23, 2023
Lactobacillus fermentum 1.2133 display probiotic potential in vitro and protect against Salmonella pullorum in chicken of infectionMin Wang, Jie Hu, Han Yu, et al.
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