1992 - Fellow of the American Association for the Advancement of Science (AAAS)
His scientific interests lie mostly in Cell division, Min System, Cell biology, Biochemistry and Escherichia coli. The various areas that Lawrence I. Rothfield examines in his Cell division study include Cell cycle and Nucleoid. His Cell biology study incorporates themes from Cell, Cell polarity, Microbiology and Bacterial cell structure.
In his study, which falls under the umbrella issue of Cell polarity, Prokaryotic cytoskeleton is strongly linked to Intermediate filament. His Escherichia coli study combines topics in areas such as Heptose, Bacillus subtilis, Bacteria and Cell Cycle Protein. His Bacillus subtilis research includes themes of Crystallography, Crescentin, MreB and Biophysics.
Lawrence I. Rothfield mainly focuses on Biochemistry, Cell biology, Cell division, Escherichia coli and Membrane. His Cell biology research is multidisciplinary, relying on both Cell, Cytoskeleton, Cell polarity and Prokaryotic cytoskeleton. Cell division is a subfield of Genetics that Lawrence I. Rothfield explores.
The Escherichia coli study combines topics in areas such as Plasmid, Molecular biology and Cell Cycle Protein. His Membrane study combines topics in areas such as Monolayer, Biophysics and Fractionation. His Min System research integrates issues from Cell division site and Bacillus subtilis.
Lawrence I. Rothfield mainly investigates Cell biology, Cell division, Biochemistry, Division and Cytoskeleton. His Cell biology research includes themes of Membrane protein, FtsZ, Prokaryotic cytoskeleton and Cell polarity. The Cell division study which covers Escherichia coli that intersects with Bacillus subtilis.
His work in Biochemistry is not limited to one particular discipline; it also encompasses Bacterial cell structure. His Escherichia coli Proteins research focuses on Cell Cycle Protein and how it relates to Min System. The various areas that Lawrence I. Rothfield examines in his Min System study include Biophysics and Microbiology.
His primary areas of study are Min System, Cell biology, Biochemistry, Escherichia coli and Cell division. His research in Min System intersects with topics in Chloroplast and Transmembrane domain. His study deals with a combination of Cell biology and Division.
His work in the fields of ATPase, Inner membrane, Sequence motif and Peptide sequence overlaps with other areas such as Ring. Lawrence I. Rothfield has included themes like Bacillus subtilis and Cell Cycle Protein in his Escherichia coli study. His research is interdisciplinary, bridging the disciplines of Biophysics and Cell division.
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A division inhibitor and a topological specificity factor coded for by the minicell locus determine proper placement of the division septum in E. coli
Piet A.J. de Boer;Robin E. Crossley;Lawrence I. Rothfield.
The essential bacterial cell-division protein FtsZ is a GTPase
Piet de Boer;Robin Crossley;Lawrence Rothfield.
Bacterial Cell Division
L Rothfield;S Justice;J García-Lara.
Annual Review of Genetics (1990)
Structure and function of biological membranes
Lawrence I. Rothfield.
Division site selection in Escherichia coli involves dynamic redistribution of Min proteins within coiled structures that extend between the two cell poles
Yu-Ling Shih;Trung Le;Lawrence Rothfield.
Proceedings of the National Academy of Sciences of the United States of America (2003)
The MinD protein is a membrane ATPase required for the correct placement of the Escherichia coli division site.
P. A. J. De Boer;R. E. Crossley;A. R. Hand;L. I. Rothfield.
The EMBO Journal (1991)
The Bacterial Cytoskeleton
Yu-Ling Shih;Lawrence Rothfield.
Microbiology and Molecular Biology Reviews (2006)
Spatial control of bacterial division-site placement
Lawrence Rothfield;Aziz Taghbalout;Yu-Ling Shih.
Nature Reviews Microbiology (2005)
Roles of MinC and MinD in the site-specific septation block mediated by the MinCDE system of Escherichia coli.
P. A. J. De Boer;R. E. Crossley;L. I. Rothfield.
Journal of Bacteriology (1992)
Synthesis and assembly of bacterial membrane components. A lipopolysaccharide-phospholipid-protein complex excreted by living bacteria.
L. Rothfield;M. Pearlman-Kothencz.
Journal of Molecular Biology (1969)
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