Author

V. Ramakrishnan

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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Biochemistry· 3 Biophysics· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Assay:cryo-EM· 4 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Organism:C. elegans· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

Y. Gordiyenko· 3 shared J. L. Llacer· 2 shared A. G. Hinnebusch· 1 shared A. K. Saini· 1 shared C. S. Fraser· 1 shared E. A. Miska· 1 shared H. Yang· 1 shared I. Diaz-Lopez· 1 shared

Activity by Year

2017-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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3 shared papersBiophysics

Y. Gordiyenko

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Author profile →

5 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

Visualising formation of the ribosomal active site in mitochondria

V. Chandrasekaran, N. Desai, N. O. Burton, H. Yang, J. L. Price, E. A. Miska, V. Ramakrishnan

The paper uses cryo-electron microscopy to visualize mitoribosome biogenesis, showing how GTPBP7 and NSUN4/MTERF4 regulate PTC formation and mitochondrial function.

bioRxiv · Mar 19, 2021Biochemistry

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

GTP Hydrolysis by eIF5B in the Last Step of Translation Initiation Is Activated by a Rotation of the Small Ribosomal Subunit.

I. S. Fernandez, V. Ramakrishnan

The paper reports a cryoEM structure of a yeast 80S/tRNAiMet/eIF5B complex, showing how a conserved tyrosine couples small subunit rotation to GTP hydrolysis during translation initiation.

bioRxiv · Aug 4, 2017Biochemistry