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Pauline Macheboeuf

Researcher at University of Grenoble

Publications -  20
Citations -  1384

Pauline Macheboeuf is an academic researcher from University of Grenoble. The author has contributed to research in topics: Penicillin binding proteins & ESCRT. The author has an hindex of 13, co-authored 19 publications receiving 1205 citations. Previous affiliations of Pauline Macheboeuf include Joseph Fourier University & University of California, San Diego.

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Penicillin Binding Proteins: key players in bacterial cell cycle and drug resistance processes

TL;DR: Structural, functional and biological features of penicillin-binding proteins, albeit having initially been identified several decades ago, are now being aggressively pursued as highly attractive targets for the development of novel antibiotherapies.
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Coiled-coil irregularities and instabilities in group A Streptococcus M1 are required for virulence.

TL;DR: The structure revealed substantial irregularities and instabilities throughout the coiled coil of the M1 fragment as discussed by the authors, explaining the patterns of cross-reactivity seen in autoimmune sequelae of GAS infection.
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Streptococcal M1 protein constructs a pathological host fibrinogen network.

TL;DR: A conformationally dynamic coiled-coil dimer of M1 was found to organize four fibrinogen molecules into a specific cross-like pattern that supported the construction of a supramolecular network that was required for neutrophil activation but was distinct from a fibrIn clot.
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Intrinsic Dynamics in ECFP and Cerulean Control Fluorescence Quantum Yield

TL;DR: The results highlight the considerable dynamical flexibility that exists in the vicinity of the tryptophan-based chromophore of these engineered fluorescent proteins and provide insights that should allow the design of mutants with enhanced optical properties.
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Active site restructuring regulates ligand recognition in class A penicillin-binding proteins

TL;DR: The structure of PBP1b* complexed with beta-lactam antibiotics reveals that ligand recognition requires a conformational modification involving conserved elements within the cleft, and suggest how class A PBPs may become activated as novel peptidoglycan synthesis becomes necessary during the cell division process.