Cargando…
Characterization of Complete Histone Tail Proteoforms Using Differential Ion Mobility Spectrometry
[Image: see text] Histone proteins are subject to dynamic post-translational modifications (PTMs) that cooperatively modulate the chromatin structure and function. Nearly all functional PTMs are found on the N-terminal histone domains (tails) of ∼50 residues protruding from the nucleosome core. Usin...
Autores principales: | Shliaha, Pavel V., Baird, Matthew A., Nielsen, Mogens M., Gorshkov, Vladimir, Bowman, Andrew P., Kaszycki, Julia L., Jensen, Ole N., Shvartsburg, Alexandre A. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2017
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5436587/ https://www.ncbi.nlm.nih.gov/pubmed/28406606 http://dx.doi.org/10.1021/acs.analchem.7b00379 |
Ejemplares similares
-
FLASHIda enables intelligent data acquisition for top–down proteomics to boost proteoform identification counts
por: Jeong, Kyowon, et al.
Publicado: (2022) -
Multiplexed Mass Spectrometry of Individual Ions Improves Measurement of Proteoforms and Their Complexes
por: Kafader, Jared O., et al.
Publicado: (2020) -
Orbitrap Mass
Spectrometry and High-Field Asymmetric
Waveform Ion Mobility Spectrometry (FAIMS) Enable the in-Depth Analysis
of Human Serum Proteoforms
por: Kline, Jake T., et al.
Publicado: (2023) -
Highly multiplexed, label-free proteoform imaging of tissues by individual ion mass spectrometry
por: Su, Pei, et al.
Publicado: (2022) -
Proteoform‐Selective Imaging of Tissues Using Mass Spectrometry
por: Yang, Manxi, et al.
Publicado: (2022)