Author

J. R. Lorsch

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· 2 Biophysics· 2

Signature Assays, Organisms & Methods

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Research Focus:cell signaling & trafficking· 4 Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Assay:bulk RNA-seq· 1 Research Focus:clustering· 1 Assay:cryo-EM· 1 Approach:deep learning· 1

Frequent Co-Authors

A. G. Hinnebusch· 4 shared F. Zhou· 2 shared N. Gupta· 2 shared A. K. Saini· 1 shared C. E. Aitken· 1 shared D. Qin· 1 shared J. D. Nanda· 1 shared J. L. Llacer· 1 shared

Activity by Year

2017-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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4 shared papersBiochemistry

A. G. Hinnebusch

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4 papers

Recent·Most cited

Transcriptome-wide analysis of the function of Ded1 in translation preinitiation complex assembly in a reconstituted in vitro system

F. Zhou, J. M. Bocetti, M. Hou, D. Qin, A. G. Hinnebusch, J. R. Lorsch

This study uses Rec-Seq to show Ded1 promotes 48S PIC formation on mRNAs with long 5UTRs and that eIF4A is required for PIC assembly on all mRNAs.

bioRxiv · Oct 16, 2023Biochemistry

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

Yeast Ded1 promotes 48S translation pre-initiation complex assembly in an mRNA-specific and eIF4F-dependent manner

N. Gupta, J. R. Lorsch, A. G. Hinnebusch

This study shows Ded1 promotes 48S PIC assembly on mRNAs in a structure-dependent and eIF4F-dependent manner.

bioRxiv · Jun 21, 2018Biochemistry

eIF4A is stimulated by the pre-initiation complex and enhances recruitment of mRNAs regardless of structural complexity

P. Yourik, C. E. Aitken, F. Zhou, N. Gupta, A. G. Hinnebusch, J. R. Lorsch

This study shows eIF4A enhances mRNA recruitment by interacting with the PIC and modulating ribosomal subunit conformation, regardless of mRNA structural complexity.

bioRxiv · Aug 24, 2017Biophysics