ssb Gene Duplication Restores the Viability of ΔholC and ΔholD Escherichia coli Mutants
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Title
ssb Gene Duplication Restores the Viability of ΔholC and ΔholD Escherichia coli Mutants
Authors
Keywords
Gene duplication, Polymerases, DNA replication, DNA-binding proteins, Point mutation, Protein interactions, Suppressor genes, DNA clamps
Journal
PLoS Genetics
Volume 10, Issue 10, Pages e1004719
Publisher
Public Library of Science (PLoS)
Online
2014-10-21
DOI
10.1371/journal.pgen.1004719
References
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- (2012) J. M. H. Heltzel et al. JOURNAL OF BACTERIOLOGY
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