Cyclic-di-GMP binding induces structural rearrangements in the PlzA and PlzC proteins of the Lyme disease and relapsing fever spirochetes: a possible switch mechanism for c-di-GMP-mediated effector functions
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Title
Cyclic-di-GMP binding induces structural rearrangements in the PlzA and PlzC proteins of the Lyme disease and relapsing fever spirochetes: a possible switch mechanism for c-di-GMP-mediated effector functions
Authors
Keywords
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Journal
Pathogens and Disease
Volume 74, Issue 8, Pages ftw105
Publisher
Oxford University Press (OUP)
Online
2016-10-19
DOI
10.1093/femspd/ftw105
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- (2009) John C. Freedman et al. FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY
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- (2009) E. A. Rogers et al. INFECTION AND IMMUNITY
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- (2008) Tso-Ning Li et al. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
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