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, particularly in *Escherichia coli*. His work has investigated the role of undecaprenyl phosphate (Und-P), a key lipid carrier in peptidoglycan biosynthesis. Bryant has explored how inhibiting Und-P production or recycling affects bacterial lysis and morphogenesis. He has also studied the function of specific proteins, such as pyruvate oxidase in *Streptococcus pneumoniae* and the DigH glycosyl hydrolase in *Escherichia coli*, in processes like protein release and cell separation. His research has involved genetic screens to identify factors influencing Und-P metabolism and has explored engineering bacteria for improved glycan expression. Bryant has a h-index of 4 with 9 total publications and 93 total citations.
Metrics
- h-index: 4
- Publications: 9
- Citations: 95
Positions
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Research Associate III 2018–presentUniversity of Arkansas for Medical Sciences Department of Microbiology and Immunology ORCID
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
- Simultaneously inhibiting undecaprenyl phosphate production and peptidoglycan synthases promotes rapid lysis in <i>Escherichia coli</i>
- A genetic screen to identify factors affected by undecaprenyl phosphate recycling uncovers novel connections to morphogenesis in <i>Escherichia coli</i>
- 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
Showing 5 of 6 shared publications
- Simultaneously inhibiting undecaprenyl phosphate production and peptidoglycan synthases promotes rapid lysis in <i>Escherichia coli</i>
- Simultaneously inhibiting undecaprenyl phosphate production and peptidoglycan synthases promotes rapid lysis in <i>Escherichia coli</i>
- Simultaneously inhibiting undecaprenyl phosphate production and peptidoglycan synthases promotes rapid lysis in <i>Escherichia coli</i>
- 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
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