Joseph Chihade
Professor
Also affiliated: Scripps Research Institute (1998–2000); Centre National de la Recherche Scientifique (2016); Carleton College (2006–2022); Wellesley College (2024); St. Olaf College (2008); Tellabs (Canada) (2008); South College (2000); In-Q-Tel (2008); Architecture et Réactivité de l'arN (2016); Institut de Biologie Moléculaire et Cellulaire (2016); Eton College (2021); Université de Strasbourg (2016); Columbia University (1996)
Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Joseph Chihade's research focuses on aminoacyl-tRNA synthetases, particularly human mitochondrial variants. His work investigates the stability and activity of these enzymes, including pathogenic mutations. Chihade also explores methods for expressing these enzymes, specifically helminth and human mitochondrial aminoacyl-tRNA synthetases, in bacterial systems. His publications include work on extending coupled assays to measure enzyme activity and bacterial expression of unstable mutants. Chihade has a h-index of 11, with 33 total publications and 381 total citations. He has collaborated with J. Sharman Mathew and Jim A. Bartel at the University of Arkansas at Fayetteville.
Metrics
- h-index: 11
- Publications: 33
- Citations: 393
Positions
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Professor 2003–presentCarleton College Chemistry ORCID
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Professor publications 2025University of Arkansas at Fayetteville ORCID
Selected Publications
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Dataset: Gene models of four Schistocephalus solidus aminoacyl-tRNA synthetases (2026)
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Dataset: Gene models of four Schistocephalus solidus aminoacyl-tRNA synthetases (2026)
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Abstract 1993 Relative stability of pathogenic human mitochondrial alanyl-tRNA synthetase mutants (2025)
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Abstract 1804 Extending the scope of a coupled assay to measure alanyl-tRNA synthetase activity (2024)
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Abstract 1744 Bacterial expression of helminth aminoacyl-tRNA synthetases (2024)
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Abstract 2055: Bacterial expression of unstable mutants of a human mitochondrial aminoacyl-tRNA synthetase (2023)
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Abstract 2035: Towards bacterial expression of helminth mitochondrial aminoacyl-tRNA synthetases (2023)
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Expression and Characterization of Helminthic Aminoacyl‐tRNA Synthetases (2022)
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Towards Bacterial Expression of Unstable Mutants of a Mitochondrial Enzyme (2022)
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A 360˚ View of COVID-19 (2021)
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Improving Prediction of Helminth Aminoacyl‐tRNA Synthetases through Manual Analysis of Genomic Data (2021)
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A 360˚ View of COVID‐19: Multidisciplinary approach to teaching the science of the pandemic (2021)
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COVID-360: A Collaborative Effort to Develop a Multidisciplinary Set of Online Resources for Engaging Teaching on the COVID-19 Pandemic (2021)
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Mitochondrial aminoacyl-tRNA synthetases (2020)
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Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs (2020)
Collaboration Network
Top Collaborators
- Origin of mitochondria in relation to evolutionary history of eukaryotic alanyl-tRNA synthetase
- Relaxed sequence constraints favor mutational freedom in idiosyncratic metazoan mitochondrial tRNAs
- Strong Selective Pressure To Use G:U To Mark an RNA Acceptor Stem for Alanine
- Assembly of a catalytic unit for RNA microhelix aminoacylation using nonspecific RNA binding domains
- COVID-360: A Collaborative Effort to Develop a Multidisciplinary Set of Online Resources for Engaging Teaching on the COVID-19 Pandemic
- A 360˚ View of COVID‐19: Multidisciplinary approach to teaching the science of the pandemic
- A 360˚ View of COVID-19
- COVID-360: A Collaborative Effort to Develop a Multidisciplinary Set of Online Resources for Engaging Teaching on the COVID-19 Pandemic
- A 360˚ View of COVID‐19: Multidisciplinary approach to teaching the science of the pandemic
- A 360˚ View of COVID-19
- COVID-360: A Collaborative Effort to Develop a Multidisciplinary Set of Online Resources for Engaging Teaching on the COVID-19 Pandemic
- A 360˚ View of COVID‐19: Multidisciplinary approach to teaching the science of the pandemic
- A 360˚ View of COVID-19
- COVID-360: A Collaborative Effort to Develop a Multidisciplinary Set of Online Resources for Engaging Teaching on the COVID-19 Pandemic
- A 360˚ View of COVID‐19: Multidisciplinary approach to teaching the science of the pandemic
- A 360˚ View of COVID-19
- COVID-360: A Collaborative Effort to Develop a Multidisciplinary Set of Online Resources for Engaging Teaching on the COVID-19 Pandemic
- A 360˚ View of COVID‐19: Multidisciplinary approach to teaching the science of the pandemic
- A 360˚ View of COVID-19
- Human mitochondrial alanyl‐tRNA synthetase: A variant mode of RNA recognition
- Metazoan mitochondrial alanyl‐tRNA synthetases – varying roles for a C‐terminal domain
- Human mitochondrial alanyl‐tRNA synthetase: A variant mode of RNA recognition
- Metazoan mitochondrial alanyl‐tRNA synthetases – varying roles for a C‐terminal domain
- Human mitochondrial alanyl‐tRNA synthetase: A variant mode of RNA recognition
- Metazoan mitochondrial alanyl‐tRNA synthetases – varying roles for a C‐terminal domain
- Human mitochondrial alanyl‐tRNA synthetase: A variant mode of RNA recognition
- Metazoan mitochondrial alanyl‐tRNA synthetases – varying roles for a C‐terminal domain
- Human mitochondrial alanyl‐tRNA synthetase: A variant mode of RNA recognition
- Metazoan mitochondrial alanyl‐tRNA synthetases – varying roles for a C‐terminal domain
- Structural modeling of tissue-specific mitochondrial alanyl-tRNA synthetase (AARS2) defects predicts differential effects on aminoacylation
- Editing activity for eliminating mischarged tRNAs is essential in mammalian mitochondria
- Structural modeling of tissue-specific mitochondrial alanyl-tRNA synthetase (AARS2) defects predicts differential effects on aminoacylation
- Editing activity for eliminating mischarged tRNAs is essential in mammalian mitochondria
- Structural modeling of tissue-specific mitochondrial alanyl-tRNA synthetase (AARS2) defects predicts differential effects on aminoacylation
- Editing activity for eliminating mischarged tRNAs is essential in mammalian mitochondria
- Understanding the basis of pathogenicity in the R592W mutant of human mitochondrial alanyl‐tRNA synthetase
- Biochemical Characterization of Pathogenic Mutations in Human Mitochondrial tRNA‐Ala and Alanyl‐tRNA Synthetase
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