ArticleJournal of the American Society for Mass Spectrometry2010
Structural analysis of prion proteins by means of drift cell and traveling wave ion mobility mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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Who cites it
16 citing papers in PubMed, 47 citations in OpenAlex.
- Transient multimers modulate conformer abundances of prion protein monomer through conformational selection.Scientific reports · 2019Article
- Interpreting the Collision Cross Sections of Native-like Protein Ions: Insights from Cation-to-Anion Proton-Transfer Reactions.Analytical chemistry · 2017Article
- Native-Like and Denatured Cytochrome c Ions Yield Cation-to-Anion Proton Transfer Reaction Products with Similar Collision Cross-Sections.Journal of the American Society for Mass Spectrometry · 2017Article
- Monitoring Conformational Landscape of Ovine Prion Protein Monomer Using Ion Mobility Coupled to Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2017Article
- Ion Mobility Collision Cross Section Compendium.Analytical chemistry · 2017Review
- Folding of Protein Ions in the Gas Phase after Cation-to-Anion Proton-Transfer Reactions.Journal of the American Chemical Society · 2016Article
- Structural Characterisation of Non-Deamidated Acidic Variants of Erwinia chrysanthemi L-asparaginase Using Small-Angle X-ray Scattering and Ion-Mobility Mass Spectrometry.Pharmaceutical research · 2015Article
- An integrative approach combining ion mobility mass spectrometry, X-ray crystallography, and nuclear magnetic resonance spectroscopy to study the conformational dynamics of α1 -antitrypsin upon ligand binding.Protein science : a publication of the Protein Society · 2015Article
- Review on ion mobility spectrometry. Part 1: current instrumentation.The Analyst · 2015Review
- Ion mobility spectrometry: A personal view of its development at UCSB.International journal of mass spectrometry · 2014Article
- Amphitrite: A program for processing travelling wave ion mobility mass spectrometry data.International journal of mass spectrometry · 2013Article
- Structural dynamics associated with intermediate formation in an archetypal conformational disease.Structure (London, England : 1993) · 2012Article
- Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone.PloS one · 2012Article
- Dividing to unveil protein microheterogeneities: traveling wave ion mobility study.Analytical chemistry · 2011Article
- Ion mobility-mass spectrometry study of folded ubiquitin conformers induced by treatment with cis-[Pd(en)(H2O2]2+.Journal of the American Society for Mass Spectrometry · 2011Article
- Traveling-wave ion mobility mass spectrometry analysis of isomeric modified peptides arising from chemical cross-linking.Journal of the American Society for Mass Spectrometry · 2010Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The prion protein (PrP) is implicitly involved in the pathogenesis of transmissible spongiform encephalopathies (TSEs). The conversion of normal cellular PrP (PrP(C)), a protein that is predominantly alpha-helical, to a beta-sheet-rich isoform (PrP(Sc)), which has a propensity to aggregate, is the key molecular event in prion diseases. During its short life span, PrP can experience two different pH environments; a mildly acidic environment, whilst cycling within the cell, and a neutral pH when it is glycosyl phosphatidylinositol (GPI)-anchored to the cell membrane. Ion mobility (IM) combined with mass spectrometry has been employed to differentiate between two conformational isoforms of recombinant Syrian hamster prion protein (SHaPrP). The recombinant proteins studied were alpha-helical SHaPrP(90-231) and beta-sheet-rich SHaPrP(90-231) at pH 5.5 and pH 7.0. The recombinant proteins have the same nominal mass-to-charge ratio (m/z) but differ in their secondary and tertiary structures. A comparison of traveling-wave (T-Wave) ion mobility and drift cell ion mobility (DCIM) mass spectrometry estimated and absolute cross-sections showed an excellent agreement between the two techniques. The use of T-Wave ion mobility as a shape-selective separation technique enabled differentiation between the estimated cross-sections and arrival time distributions (ATDs) of alpha-helical SHaPrP(90-231) and beta-sheet-rich SHaPrP(90-231) at pH 5.5. No differences in cross-section or ATD profiles were observed between the protein isoforms at pH 7.0. The findings have potential implications for a new ante-mortem screening assay, in bodily fluids, for prion misfolding diseases such as TSEs.
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