Chenguang Fan
Affiliation confirmed via AI analysis of OpenAlex, ORCID, and web sources.
Assistant Professor
Also affiliated: University of Iowa (1999–2004); Brigham and Women's Hospital (2007); National Institutes of Health (2005); Children's National (2005–2006); Harvard University (2015–2018); University of Kansas (2026); University of Alberta (2010–2012); Iowa State University (2008–2012); Chinese Academy of Sciences (2022); Whitney Museum of American Art (2014–2016); Yale University (2012–2016); Beijing Solar Energy Research Institute (2022); Institute of Molecular and Cell Biology (2026); Institute of Electrical Engineering (2022); National Eye Institute (2005); Institut für Soziale Arbeit (2016); Iowa City Public Library (2003); University of Chinese Academy of Sciences (2022)
Faculty Researcher
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Chenguang Fan's research focuses on the fundamental mechanisms of protein modification and gene expression, particularly in the context of bacterial and human biology. He has received significant federal funding from the NIH/National Institute of General Medical Sciences for two projects totaling over $1 million. One grant supports his investigation into the role of lysine acetylation of human threonyl-tRNA synthetase, while the other funds his work studying lysine aminoacylation of human metabolic enzymes. These projects aim to elucidate the post-translational modifications of key human enzymes.
Fan's laboratory group also explores bacterial genetics and physiology, as evidenced by publications on genome-wide screening of oxidizing agent resistance genes in *Escherichia coli* and studies on orthogonal translation for site-specific installation of post-translational modifications. His work has also extended to investigating acetylation of specific human enzymes, such as aconitase isozymes and glucokinase, utilizing genetic code expansion techniques. Collaborations with researchers at the University of Arkansas at Fayetteville and the University of Arkansas for Medical Sciences contribute to his publication record.
Metrics
- h-index: 34
- Publications: 79
- Citations: 4,195
Selected Publications
-
Crystal structures of <i>Escherichia coli</i> glucokinase acetylation-mimicking variants and insights into the impact of acetylation (2026)
-
Expanding the Genetic Code with Lysine Aminoacylation (2026)
-
Additional file 1 of Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655 (2026)
-
Additional file 1 of Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655 (2026)
-
Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655 (2026)
-
Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655 (2026)
-
Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655 (2026)
-
Crystal structures of <i>Escherichia coli</i> glucokinase and insights into phosphate binding (2025)
-
Functional consequences of lysine acetylation of phosphofructokinase isozymes (2025)
-
Orthogonal Translation for Site-Specific Installation of Post-translational Modifications (2024)
-
Characterizing lysine acetylation of glucokinase (2023)
-
Studying lysine acetylation of citric acid cycle enzymes by genetic code expansion (2023)
-
“<scp>Not‐so‐popular</scp>” orthogonal pairs in genetic code expansion (2022)
-
Modifications of cellulose-based biomaterials for biomedical applications (2022)
-
Editorial: Engineering Nucleic Acids-Based Functional Nanomaterials, Nanodrugs, and Biosensors (2022)
Federal Grants 2 $1,012,500 total
The role of lysine acetylation of human threonyl-tRNA synthetase
Collaboration Network
Top Collaborators
- Orthogonal Translation for Site-Specific Installation of Post-translational Modifications
- Genome-Wide Screening of Oxidizing Agent Resistance Genes in Escherichia coli
- “<scp>Not‐so‐popular</scp>” orthogonal pairs in genetic code expansion
- Studying Acetylation of Aconitase Isozymes by Genetic Code Expansion
- Introducing noncanonical amino acids for studying and engineering bacterial microcompartments
Showing 5 of 12 shared publications
- Modifications of cellulose-based biomaterials for biomedical applications
- Characterizing lysine acetylation of glucokinase
- Studying lysine acetylation of citric acid cycle enzymes by genetic code expansion
- Functional consequences of lysine acetylation of phosphofructokinase isozymes
- Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655
- Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655
- Additional file 1 of Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655
- Additional file 1 of Genome-wide screening of antibiotic survival genes in Escherichia coli MG1655
- Genome-Wide Screening of Oxidizing Agent Resistance Genes in Escherichia coli
- Introducing noncanonical amino acids for studying and engineering bacterial microcompartments
- Studying Acetylation of Aconitase Isozymes by Genetic Code Expansion
- Introducing noncanonical amino acids for studying and engineering bacterial microcompartments
- Characterizing lysine acetylation of glucokinase
- Functional consequences of lysine acetylation of phosphofructokinase isozymes
- Introducing noncanonical amino acids for studying and engineering bacterial microcompartments
- Genome-Wide Screening of Oxidizing Agent Resistance Genes in Escherichia coli
- Genome-Wide Screening of Oxidizing Agent Resistance Genes in Escherichia coli
- Genome-Wide Screening of Oxidizing Agent Resistance Genes in Escherichia coli
- Editorial: Synthetic Nucleic Acids for Expanding Genetic Codes and Probing Living Cells
- Editorial: Synthetic Nucleic Acids for Expanding Genetic Codes and Probing Living Cells
- Studying Acetylation of Aconitase Isozymes by Genetic Code Expansion
- Studying Acetylation of Aconitase Isozymes by Genetic Code Expansion
- Editorial: Engineering Nucleic Acids-Based Functional Nanomaterials, Nanodrugs, and Biosensors
Similar Researchers
Based on overlapping research topics