ArticleMass spectrometry (Tokyo, Japan)2013
Integrating Native Mass Spectrometry and Top-Down MS for Defining Protein Interactions Important in Biology and Medicine.
Article in Mass spectrometry (Tokyo, Japan), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Development of Native MS Capabilities on an Extended Mass Range Q-TOF MS.International journal of mass spectrometry · 2020Article
- Top-Down Protein Identification using a Time-of-Flight Mass Spectrometer and Data Independent Acquisition.International journal of mass spectrometry · 2019Article
- Enhancing Sensitivity of Liquid Chromatography-Mass Spectrometry of Peptides and Proteins Using Supercharging Agents.International journal of mass spectrometry · 2018Article
- Characterization of trimethoprim resistantChemical science · 2017Article
- Ion Mobility-Mass Spectrometry Analysis of Cross-Linked Intact Multiprotein Complexes: Enhanced Gas-Phase Stabilities and Altered Dissociation Pathways.Analytical chemistry · 2016Article
- Online Hydrophobic Interaction Chromatography-Mass Spectrometry for Top-Down Proteomics.Analytical chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Native protein mass spectrometry (MS), the measurement of proteins and protein complexes from non-denaturing solutions, with electrospray ionization (ESI) has utility in the biological sciences. Protein complexes exceeding 1 MDa have been measured by MS and ion mobility spectrometry (IMS), and the data yields information not only regarding size, but structural details can be revealed also. ESI-IMS allows the relative stability of protein-ligand binding to be measured. Top-down MS, the direct dissociation of the intact gas phase biomolecule, can generate sequence and identity information for monomeric (denatured) proteins, and topology information for noncovalent protein complexes. For protein complexes with small molecule ligands, i.e., drugs, cofactors, metals, etc., top-down MS with electron capture dissociation can be used to elucidate the site(s) of ligand binding. Increasing protein ESI charging, e.g., supercharging, enhances the efficiency for dissociation of protein complexes.
Indexed as
Identifiers
What OpenQuestion holds
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.