Cargando…
Characterization and Quantification of Intact 26S Proteasome Proteins by Real-Time Measurement of Intrinsic Fluorescence Prior to Top-down Mass Spectrometry
Quantification of gas-phase intact protein ions by mass spectrometry (MS) is impeded by highly-variable ionization, ion transmission, and ion detection efficiencies. Therefore, quantification of proteins using MS-associated techniques is almost exclusively done after proteolysis where peptides serve...
Autores principales: | Russell, Jason D., Scalf, Mark, Book, Adam J., Ladror, Daniel T., Vierstra, Richard D., Smith, Lloyd M., Coon, Joshua J. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3594244/ https://www.ncbi.nlm.nih.gov/pubmed/23536786 http://dx.doi.org/10.1371/journal.pone.0058157 |
Ejemplares similares
-
Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation
por: Marshall, Richard S., et al.
Publicado: (2019) -
Best practices and benchmarks for intact protein analysis for top-down mass spectrometry
por: Donnelly, Daniel P., et al.
Publicado: (2019) -
Dual function of Rpn5 in two PCI complexes, the 26S proteasome and COP9 signalosome
por: Yu, Zanlin, et al.
Publicado: (2011) -
Degradation of Intrinsically Disordered Proteins by the NADH 26S Proteasome
por: Tsvetkov, Peter, et al.
Publicado: (2020) -
Top-Down and Intact Protein Mass Spectrometry Data Visualization for
Proteoform Analysis Using VisioProt-MS
por: Lesne, Jean, et al.
Publicado: (2019)