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Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family

Overview of attention for article published in BMC Biology, May 2010
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Title
Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family
Published in
BMC Biology, May 2010
DOI 10.1186/1741-7007-8-70
Pubmed ID
Authors

Daniel H Haft, Malay Kumar Basu, Douglas A Mitchell

Abstract

A new family of natural products has been described in which cysteine, serine and threonine from ribosomally-produced peptides are converted to thiazoles, oxazoles and methyloxazoles, respectively. These metabolites and their biosynthetic gene clusters are now referred to as thiazole/oxazole-modified microcins (TOMM). As exemplified by microcin B17 and streptolysin S, TOMM precursors contain an N-terminal leader sequence and C-terminal core peptide. The leader sequence contains binding sites for the posttranslational modifying enzymes which subsequently act upon the core peptide. TOMM peptides are small and highly variable, frequently missed by gene-finders and occasionally situated far from the thiazole/oxazole forming genes. Thus, locating a substrate for a particular TOMM pathway can be a challenging endeavor.

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Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 163 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 2 1%
United Kingdom 1 <1%
Denmark 1 <1%
Germany 1 <1%
Unknown 158 97%

Demographic breakdown

Readers by professional status Count As %
Researcher 34 21%
Student > Ph. D. Student 33 20%
Student > Master 26 16%
Student > Bachelor 18 11%
Student > Doctoral Student 7 4%
Other 24 15%
Unknown 21 13%
Readers by discipline Count As %
Agricultural and Biological Sciences 59 36%
Biochemistry, Genetics and Molecular Biology 36 22%
Chemistry 30 18%
Immunology and Microbiology 4 2%
Environmental Science 3 2%
Other 9 6%
Unknown 22 13%