Author

Y. Gordiyenko

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Assay:cryo-EM· 2 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Assay:structural biology· 1

Frequent Co-Authors

V. Ramakrishnan· 3 shared J. L. Llacer· 2 shared A. G. Hinnebusch· 1 shared A. K. Saini· 1 shared C. S. Fraser· 1 shared I. Diaz-Lopez· 1 shared J. Brito Querido· 1 shared J. D. Nanda· 1 shared

Activity by Year

2018-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiophysics

V. Ramakrishnan

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3 papers

Recent·Most cited

Human tumor suppressor protein Pdcd4 binds at the mRNA entry channel in 40S small ribosomal subunit

J. Brito Querido, M. Sokabe, I. Diaz-Lopez, Y. Gordiyenko, P. Zuber, Y. Du, L. Albacete-Albacete, V. Ramakrishnan, C. S. Fraser

This study determines the structure of Pdcd4 bound to the 40S ribosomal subunit, revealing its binding site and mechanism in translational control.

bioRxiv · May 1, 2024 · PreprintBiochemistry

Structural basis for the inhibition of translation through eIF2α phosphorylation

Y. Gordiyenko, J. L. Llacer, V. Ramakrishnan

The paper determines the cryo-EM structure of eIF2B complexed with phosphorylated eIF2, revealing how Ser51 phosphorylation inhibits translation initiation by altering eIF2B interactions.

bioRxiv · Dec 21, 2018Biophysics

Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal subunit to promote start-codon recognition

J. L. Llacer, T. Hussain, A. K. Saini, J. D. Nanda, S. Kaur, Y. Gordiyenko, R. Kumar, A. G. Hinnebusch, J. R. Lorsch, V. Ramakrishnan

The paper presents a cryo-EM structure of a 48S pre-initiation complex showing eIF5's role in promoting start-codon recognition by stabilizing the Met-tRNAi-codon interaction.

bioRxiv · Jul 10, 2018Biophysics