H
Helen J. Cooper
Researcher at University of Birmingham
Publications - 154
Citations - 6036
Helen J. Cooper is an academic researcher from University of Birmingham. The author has contributed to research in topics: Mass spectrometry & Electron-capture dissociation. The author has an hindex of 38, co-authored 145 publications receiving 5359 citations. Previous affiliations of Helen J. Cooper include Thermo Electron & University of Warwick.
Papers
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Journal ArticleDOI
The role of electron capture dissociation in biomolecular analysis.
TL;DR: A major theme of this review is the role of ECD in proteomics, particularly for characterization of post-translational modifications and the top-down approach to protein identification.
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Resolution and identification of elemental compositions for more than 3000 crude acids in heavy petroleum by negative-ion microelectrospray high-field Fourier transform ion cyclotron resonance mass spectrometry
Kuangnan Qian,Winston K. Robbins,Christine A. Hughey,Helen J. Cooper,Ryan P. Rodgers,Alan G. Marshall +5 more
TL;DR: In this paper, negative-ion electrospray ionization (ESI) high-field Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) was used to identify crude acids.
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Electron Capture Dissociation and Infrared Multiphoton Dissociation MS/MS of an N-Glycosylated Tryptic Peptide To Yield Complementary Sequence Information
Kristina Håkansson,Helen J. Cooper,Mark R. Emmett,Catherine E. Costello,and Alan G. Marshall,Carol L. Nilsson +5 more
TL;DR: The applicability of ECD for glycopeptide analysis to N-glycosylated peptides and to peptides containing branched, highly substituted glycans is extended and the two types of spectra, obtained with the same instrument, provide complementary structural information about the glycopePTide.
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Dynamic Range and Mass Accuracy of Wide-Scan Direct Infusion Nanoelectrospray Fourier Transform Ion Cyclotron Resonance Mass Spectrometry-Based Metabolomics Increased by the Spectral Stitching Method
TL;DR: An optimized strategy for wide-scan DI nESI FT-ICR MS that increases dynamic range but maintains high mass accuracy is reported, which increases metabolome coverage, has very highmass accuracy, and at 5.5 min/sample is conducive for high-throughput metabolomics.
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Higher energy collision dissociation (HCD) product ion-triggered electron transfer dissociation (ETD) mass spectrometry for the analysis of N-linked glycoproteins.
TL;DR: The results show that the product ion-triggered approach shows promise for the field of glycoproteomics and highlight the requirement for more sophisticated data mining tools.