ArticleJournal of the American Society for Mass Spectrometry2006
Localization of noncovalent complexes in MALDI-preparations by CLSM.
Article in Journal of the American Society for Mass Spectrometry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 29 citations in OpenAlex.
- 6-Aza-2-Thiothymine as an Alternative Matrix for Spatial Proteomics with MALDI-MSI.International journal of molecular sciences · 2024Article
- FT-ICR Mass Spectrometry Imaging at Extreme Mass Resolving Power Using a Dynamically Harmonized ICR Cell with 1ω or 2ω Detection.Analytical chemistry · 2022Article
- Observation of Intact and Proteolytically Cleaved Amyloid-Beta (1-40)-Oleuropein Noncovalent Complex at Neutral pH by Mass Spectrometry.Molecules (Basel, Switzerland) · 2021Article
- Liquid Native MALDI Mass Spectrometry for the Detection of Protein-Protein Complexes.Journal of the American Society for Mass Spectrometry · 2018Article
- Cracking the Sugar Code by Mass Spectrometry : An Invited Perspective in Honor of Dr. Catherine E. Costello, Recipient of the 2017 ASMS Distinguished Contribution Award.Journal of the American Society for Mass Spectrometry · 2018Article
- Imaging of noncovalent complexes by MALDI-MS.Journal of the American Society for Mass Spectrometry · 2013Article
- Solid state nuclear magnetic resonance as a tool to explore solvent-free MALDI samples.Journal of the American Society for Mass Spectrometry · 2009Article
- Investigation of calmodulin-Peptide interactions using matrix-assisted laser desorption/ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 2009Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The unambiguous detection of noncovalent complexes (NCCs) by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) is still a far cry from being routine. For protein NCCs such as their quaternary structure it has been reported that signals of the intact complex are only obtained for the first or at most the first few laser exposures of a given sample area. This observation was called the first-shot phenomenon. In the present study, this first-shot phenomenon has been investigated for the hexameric protein complex allophycocyanine (APC) by two independent methods, MALDI-MS with a (nearly) pH-neutral matrix 6-aza-2-thiothymine (6-ATT) and by imaging the fluorescence of the complex in APC-6-ATT preparations by confocal laser scan microscopy (CLSM). The intact APC heterohexamer loses its visible fluorescence upon dissociation into its subunits. Both methods consistently show that intact APC complexes are precipitated at the matrix crystal surface, but dissociate upon incorporation into the matrix crystals.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.