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Roberto Kolter
Researcher at Harvard University
Publications - 318
Citations - 58161
Roberto Kolter is an academic researcher from Harvard University. The author has contributed to research in topics: Biofilm & Bacillus subtilis. The author has an hindex of 120, co-authored 315 publications receiving 52942 citations. Previous affiliations of Roberto Kolter include University of California, Los Angeles & Boston Children's Hospital.
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Cloning and sequencing of Escherichia coli murZ and purification of its product, a UDP-N-acetylglucosamine enolpyruvyl transferase.
TL;DR: The Escherichia coli gene murZ, encoding the enzyme UDP-N-acetylglucosamine enolpyruvyl transferase, has been cloned and sequenced and Sequence analysis of the predicted product revealed 44% identity to OrfR from Bacillus subtilis, suggesting that orfR may also encode a UDP
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An E. coli promoter induced by the cessation of growth.
TL;DR: Levels of transcription were reduced in ompR backgrounds, in contrast, mutations in other global regulatory loci, fnr, relA and cya had little or no effect and starvation for nitrogen, phosphate or carbon sources all induced transcription from the promoter.
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Why are bacteria refractory to antimicrobials
Deborah A. Hogan,Roberto Kolter +1 more
TL;DR: It is now apparent that bacteria have complex, intrinsic resistance mechanisms that are often not detected in the standard antibiotic sensitivity tests performed in clinical laboratories, and the development of resistance in bacteria found in surface-associated aggregates or biofilms, owing to these intrinsic mechanisms, is paramount.
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A functionally diverse enzyme superfamily that abstracts the alpha protons of carboxylic acids
Patricia C. Babbitt,Gregory T. Mrachko,Miriam S. Hasson,Gjalt W. Huisman,Roberto Kolter,Dagmar Ringe,Gregory A. Petsko,George L. Kenyon,John A. Gerlt +8 more
TL;DR: The structural similarity to mandelate racemase of a previously unidentified gene product was used to deduce its function as a galactonate dehydratase and supports the hypothesis that new enzymatic activities evolve by recruitment of a protein catalyzing the same type of chemical reaction.
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Four plasmid genes are required for colicin V synthesis, export, and immunity.
TL;DR: It is concluded that the cvaC gene codes for the structural gene for colicin V, while cvaA and cvaB are apparently needed for the normal export of the colingin.