ArticleInternational journal of molecular sciences2012
Proteomic analysis of the organ of corti using nanoscale liquid chromatography coupled with tandem mass spectrometry.
Article in International journal of molecular sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 12 citations in OpenAlex.
- Article
- Article
- Label-free quantitative mass spectrometry analysis of differential protein expression in the developing cochlear sensory epithelium.Proteome science · 2018Article
- Global Analysis of Protein Expression of Inner Ear Hair Cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Bottom-up and shotgun proteomics to identify a comprehensive cochlear proteome.Journal of visualized experiments : JoVE · 2014Article
- In-depth proteomic analysis of mouse cochlear sensory epithelium by mass spectrometry.Journal of proteome research · 2013Article
- The Transcriptomics to Proteomics of Hair Cell Regeneration: Looking for a Hair Cell in a Haystack.Microarrays (Basel, Switzerland) · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The organ of Corti (OC) in the cochlea plays an essential role in auditory signal transduction in the inner ear. For its minute size and trace amount of proteins, the identification of the molecules in pathophysiologic processes in the bone-encapsulated OC requires both delicate separation and a highly sensitive analytical tool. Previously, we reported the development of a high resolution metal-free nanoscale liquid chromatography system for highly sensitive phosphoproteomic analysis. Here this system was coupled with a LTQ-Orbitrap XL mass spectrometer to investigate the OC proteome from normal hearing FVB/N male mice. A total of 628 proteins were identified from six replicates of single LC-MS/MS analysis, with a false discovery rate of 1% using the decoy database approach by the OMSSA search engine. This is currently the largest proteome dataset for the OC. A total of 11 proteins, including cochlin, myosin VI, and myosin IX, were identified that when defective are associated with hearing impairment or loss. This study demonstrated the effectiveness of our nanoLC-MS/MS platform for sensitive identification of hearing loss-associated proteins from minute amount of tissue samples.
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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.