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Nichole M. Lareau

Researcher at Vanderbilt University

Publications -  8
Citations -  445

Nichole M. Lareau is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Mass spectrometry & Ion-mobility spectrometry. The author has an hindex of 5, co-authored 8 publications receiving 383 citations. Previous affiliations of Nichole M. Lareau include The College of New Jersey & GlaxoSmithKline.

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Conformational ordering of biomolecules in the gas phase: nitrogen collision cross sections measured on a prototype high resolution drift tube ion mobility-mass spectrometer

TL;DR: Comparisons made between helium and nitrogen-derived CCS measurements demonstrate that nitrogen CCS values are systematically larger than helium values; however, general separation trends between chemical classes are retained regardless of the drift gas, underscore that, for the highest CCS accuracy, care must be exercised when utilizing helium-derivedCCS values to calibrate measurements obtained in nitrogen.
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Bond-specific dissociation following excitation energy transfer for distance constraint determination in the gas phase.

TL;DR: Chemistry that enables excitation energy transfer (EET) to be accurately measured via action spectroscopy on gaseous ions in an ion trap is reported and it is demonstrated that EET between tryptophan or tyrosine and a disulfide bond leads to excited state, homolytic fragmentation of the disulfides bond.
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Non-derivatized Glycan Analysis by Reverse Phase Liquid Chromatography and Ion Mobility-Mass Spectrometry

TL;DR: A simple method for the analysis of non-derivatized glycans using a reverse phase column on a liquid chromatography-ion mobility-mass spectrometry (LC-IM-MS) instrument that supports both glycomic and proteomic work flows without the necessity of switching columns.
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An Iron-Regulated Autolysin Remodels the Cell Wall To Facilitate Heme Acquisition in Staphylococcus lugdunensis

TL;DR: These studies establish IsdP as an autolysin that functions in heme acquisition and describe a role for isdP in cell wall reorganization to accommodate nutrient uptake systems during infection.
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Imaging mass spectrometry reveals direct albumin fragmentation within the diabetic kidney

TL;DR: Specific albumin fragments accumulating in the lumen of diabetic renal tubules were identified and predicted the enzymatic action of cathepsin D based on cleavage specificity and in vitro digestions and was demonstrated directly in the renal tissue with the endogenous nonlabeled murine albumin.