Dylan Girodat
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Assistant Professor, University of Lethbridge
Formerly Arkansas Assistant Professor, University of Arkansas through 2024; now Assistant Professor, University of Lethbridge.
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Dylan Girodat's research investigates the molecular mechanisms of protein synthesis and RNA pathways, with a particular focus on the ribosome. His work utilizes computational approaches, including molecular dynamics simulations, to understand the dynamic interactions between ribosomal components, transfer RNA (tRNA), and elongation factors during translation. Recent publications explore the role of specific RNA modifications in cancer, the function of elongation factor Tu in tRNA selection and proofreading, and the structural basis for the ribosome's P stalk interaction with elongation factor 2. Girodat also studies the cleavage of RNA by RNase E and the conformational changes within the ribosome that facilitate mRNA and tRNA translocation. His research network includes collaborators from the University of Arkansas at Fayetteville, such as Divya Sapkota and Anuradha Chowdhury.
Metrics
- h-index: 9
- Publications: 33
- Citations: 590
Positions
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Assistant Professor 2024–presentUniversity of Lethbridge Chemsitry and Biochemistry ORCID
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Assistant Professor 2022–2024University of Arkansas Chemistry and Biochemistry ORCID
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Postdoctoral Fellow 2019–2022Los Alamos National Laboratory Theoretical Biology and Biophysics ORCID
Selected Publications
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Human protein synthesis requires aminoacyl-tRNA pivoting during proofreading (2025)
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Solution Structure Determination and Biophysical Studies of 7SK RNP and 7SL SRP RNAs (2025)
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Human Protein Synthesis Requires aminoacyl-tRNA Pivoting During Proofreading (2025)
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BPS2025 - Human aminoacyl-tRNA pivots during accommodation (2025)
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BPS2025 - Diamond-Blackfan anemia-associated mutations perturb uL5 helix stability and conformational ensemble (2025)
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BPS2025 - Measurement of nucleotide triphosphate hydrolysis rates and inorganic phosphate release using a coumarin-labeled phosphate binding protein (2025)
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Alternate conformational trajectories in ribosome translocation (2024)
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Implementing Cryo-EM Manual Plunger Techniques in University Workshops and Teaching Laboratories (2024)
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Alternate conformational trajectories in protein synthesis (2024)
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Conformational changes of ribosomes during translation elongation resolved by molecular dynamics simulations (2024)
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Divergent pathways of ribosomal motions during protein synthesis (2024)
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Development of a non-radioactive based assay to measure GTP and ATP hydrolysis rates (2024)
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Impact of Diamond-Blackfan anemia associated mutations on structural dynamics of ribosomal protein uL5 (2024)
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Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding (2023)
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Ribosome hyper-swivel head domain motions are required for translocation and resetting (2023)
Collaboration Network
Top Collaborators
- Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding
- Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding
- Human protein synthesis requires aminoacyl-tRNA pivoting during proofreading
- Ribosome hyper-swivel head domain motions are required for translocation and resetting
- Divergent pathways of ribosomal motions during protein synthesis
Showing 5 of 7 shared publications
- Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding
- Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding
- Ribosome hyper-swivel head domain motions are required for translocation and resetting
- Divergent pathways of ribosomal motions during protein synthesis
- Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding
- Geometric alignment of aminoacyl-tRNA relative to catalytic centers of the ribosome underpins accurate mRNA decoding
- Divergent pathways of ribosomal motions during protein synthesis
- Conformational changes of ribosomes during translation elongation resolved by molecular dynamics simulations
- Impact of Diamond-Blackfan anemia associated mutations on structural dynamics of ribosomal protein uL5
- BPS2025 - Diamond-Blackfan anemia-associated mutations perturb uL5 helix stability and conformational ensemble
- Conformational changes of ribosomes during translation elongation resolved by molecular dynamics simulations
- Human protein synthesis requires aminoacyl-tRNA pivoting during proofreading
- Human Protein Synthesis Requires aminoacyl-tRNA Pivoting During Proofreading
- Impact of Diamond-Blackfan anemia associated mutations on structural dynamics of ribosomal protein uL5
- BPS2025 - Diamond-Blackfan anemia-associated mutations perturb uL5 helix stability and conformational ensemble
- Development of a non-radioactive based assay to measure GTP and ATP hydrolysis rates
- BPS2025 - Measurement of nucleotide triphosphate hydrolysis rates and inorganic phosphate release using a coumarin-labeled phosphate binding protein
- Alternate conformational trajectories in ribosome translocation
- Alternate conformational trajectories in protein synthesis
- Alternate conformational trajectories in ribosome translocation
- Alternate conformational trajectories in protein synthesis
- Alternate conformational trajectories in ribosome translocation
- Alternate conformational trajectories in protein synthesis
- Alternate conformational trajectories in ribosome translocation
- Alternate conformational trajectories in protein synthesis
- Alternate conformational trajectories in ribosome translocation
- Alternate conformational trajectories in protein synthesis
- Alternate conformational trajectories in ribosome translocation
- Alternate conformational trajectories in protein synthesis
- Ribosome hyper-swivel head domain motions are required for translocation and resetting
- Ribosome hyper-swivel head domain motions are required for translocation and resetting
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