Joseph C. Bryant
Researcher
Also affiliated: Mississippi State University (2016)
Unknown Researcher
Research Areas
Biomedical Subjects
Biography and Research Information
OverviewAI-generated summary
Joseph C. Bryant's research focuses on the molecular mechanisms governing bacterial cell division and cell wall synthesis in *Escherichia coli*. His work investigates how gene expression and metabolic pathways impact bacterial growth and structure. Recent publications explore the role of specific proteins, such as the DigH glycosyl hydrolase, in daughter cell separation and how dysregulation of nucleotidyltransferases can lead to defects in division and surface glycan production by altering metabolite levels.
Bryant has collaborated with researchers at the University of Arkansas for Medical Sciences, including Matthew A. Jorgenson, Intawat Nookaew, Alongkorn Kurilung, and Emily J. Robbs, on multiple publications. His scholarship metrics include an h-index of 4, with 9 total publications and 88 citations. His recent activity indicates ongoing contributions to the field of bacterial genetics and cell biology.
Metrics
- h-index: 4
- Publications: 9
- Citations: 92
Selected Publications
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Dysregulation of a nucleotidyltransferase induces division and surface glycan defects in <i>Escherichia coli</i> by altering related metabolite levels (2026)
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The DigH glycosyl hydrolase is conditionally required for daughter cell separation in <i>Escherichia coli</i> (2025)
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Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology (2024)
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A genetic screen to identify factors affected by undecaprenyl phosphate recycling uncovers novel connections to morphogenesis in <i>Escherichia coli</i> (2020)
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A genetic screen to identify factors affected by undecaprenyl phosphate recycling uncovers novel connections to morphogenesis in <i>Escherichia coli</i> (2020)
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Simultaneously inhibiting undecaprenyl phosphate production and peptidoglycan synthases promotes rapid lysis in <i>Escherichia coli</i> (2019)
Collaboration Network
Top Collaborators
- Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology
- The DigH glycosyl hydrolase is conditionally required for daughter cell separation in <i>Escherichia coli</i>
- Dysregulation of a nucleotidyltransferase induces division and surface glycan defects in <i>Escherichia coli</i> by altering related metabolite levels
- Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology
- Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology
- Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology
- Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology
- Engineering Escherichia coli for increased Und-P availability leads to material improvements in glycan expression technology
- The DigH glycosyl hydrolase is conditionally required for daughter cell separation in <i>Escherichia coli</i>
- The DigH glycosyl hydrolase is conditionally required for daughter cell separation in <i>Escherichia coli</i>
- The DigH glycosyl hydrolase is conditionally required for daughter cell separation in <i>Escherichia coli</i>
- The DigH glycosyl hydrolase is conditionally required for daughter cell separation in <i>Escherichia coli</i>
- Dysregulation of a nucleotidyltransferase induces division and surface glycan defects in <i>Escherichia coli</i> by altering related metabolite levels
- Dysregulation of a nucleotidyltransferase induces division and surface glycan defects in <i>Escherichia coli</i> by altering related metabolite levels
- Dysregulation of a nucleotidyltransferase induces division and surface glycan defects in <i>Escherichia coli</i> by altering related metabolite levels
- Dysregulation of a nucleotidyltransferase induces division and surface glycan defects in <i>Escherichia coli</i> by altering related metabolite levels
- Dysregulation of a nucleotidyltransferase induces division and surface glycan defects in <i>Escherichia coli</i> by altering related metabolite levels
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