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Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E.

Overview of attention for article published in BMC Microbiology, February 2013
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Title
Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coliviability
Published in
BMC Microbiology, February 2013
DOI 10.1186/1471-2180-13-26
Pubmed ID
Authors

Jae Yen Shin, Waldemar Vollmer, Rosalba Lagos, Octavio Monasterio

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 37 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Slovakia 1 3%
Unknown 36 97%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 10 27%
Researcher 7 19%
Student > Master 3 8%
Student > Postgraduate 2 5%
Professor > Associate Professor 2 5%
Other 5 14%
Unknown 8 22%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 11 30%
Agricultural and Biological Sciences 10 27%
Chemistry 2 5%
Mathematics 1 3%
Social Sciences 1 3%
Other 3 8%
Unknown 9 24%