MassIVE MSV000089498

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Cyclophilin B function elucidated by electrochemical sensors

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Description

We have investigated the function of CypB through negative ionization high resolution LCMS and examined the purity of a CypB protein with intact mass analyzes on a Q Exactive mass spectrometer. [doi:10.25345/C5K06X48W] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Intact protein ; CypB ; Nuclease

Contact

Principal Investigators:
(in alphabetical order) 		Benjamin C Orsburn, Johns Hopkins, USA
Submitting User: ben_orsburn

Publications

Clark V, Waters K, Orsburn B, Bumpus NN, Kundu N, Sczepanski JT, Ray P, Arroyo-Currás N.
Human Cyclophilin B Nuclease Activity Revealed via Nucleic Acid-Based Electrochemical Sensors.
Angew Chem Int Ed Engl. Epub 2022 Aug 23.

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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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Number of distinct proteins found to be differentially abundant in at least one comparison across all analyses (original submission and reanalyses) associated with this dataset.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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