Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Santosh G. Valeja"'
Autor:
Zachery R. Gregorich, Huseyin Guner, Wenxuan Cai, Serife Ayaz-Guner, Ying Ge, Santosh G. Valeja, Xiaowen Liu, Albert J. Chen, Ying Peng
Publikováno v:
Molecular & Cellular Proteomics. 15:703-714
Top-down mass spectrometry (MS)-based proteomics is arguably a disruptive technology for the comprehensive analysis of all proteoforms arising from genetic variation, alternative splicing, and posttranslational modifications (PTMs). However, the comp
Publikováno v:
Analytical Chemistry. 88:1885-1891
Recent progress in top-down proteomics has led to a demand for mass spectrometry (MS)-compatible chromatography techniques to separate intact proteins using volatile mobile phases. Conventional hydrophobic interaction chromatography (HIC) provides hi
Publikováno v:
Analytical Chemistry. 87:5363-5371
To address the complexity of the proteome in mass spectrometry (MS)-based top-down proteomics, multidimensional liquid chromatography (MDLC) strategies that can effectively separate proteins with high resolution and automation are highly desirable. A
Autor:
Santosh G. Valeja, Albert J. Chen, Wenxuan Cai, Denise J. Schwahn, Ying Peng, Timothy A. Hacker, Zachery R. Gregorich, Ying Ge, Xiaowen Liu, Huseyin Guner, Yi-Chen Chen, Han Zhang
Publikováno v:
Molecular & Cellular Proteomics : MCP
Heart failure (HF) is a leading cause of morbidity and mortality worldwide and is most often precipitated by myocardial infarction. However, the molecular changes driving cardiac dysfunction immediately after myocardial infarction remain poorly under
Publikováno v:
Analytical Chemistry
One of the challenges in proteomics is the proteome’s complexity, which necessitates the fractionation of proteins prior to the mass spectrometry (MS) analysis. Despite recent advances in top-down proteomics, separation of intact proteins remains c
Publikováno v:
Journal of the American Society for Mass Spectrometry. 24:1722-1726
Fourier transform mass spectrometry (FTMS) of the isolated isotopic distribution for a highly charged biomolecule produces time-domain signal containing large amplitude signal "beats" separated by extended periods of much lower signal magnitude. Sign
Publikováno v:
Analytical Chemistry. 85:4239-4246
Top-down electron capture dissociation (ECD) Fourier transform ion cyclotron resonance (FTICR) mass spectrometry was performed for structural analysis of an intact monoclonal antibody (IgG1kappa (κ) isotype, ~148 kDa). Simultaneous ECD for all charg
Autor:
Santosh G. Valeja, Christopher L. Hendrickson, Nathan K. Kaiser, Alan G. Marshall, Jason C. Rouse, Feng Xian
Publikováno v:
Analytical Chemistry. 83:8391-8395
Fourier transform ion cyclotron resonance mass spectrometry (FTICR MS) provides the highest mass resolving power and mass measurement accuracy for unambiguous identification of biomolecules. Previously, the highest-mass protein for which FTICR unit m
Autor:
Zachery R. Gregorich, Song Jin, Wenxuan Cai, Serife Ayaz-Guner, Ying Ge, Leekyoung Hwang, Santosh G. Valeja
Analysis of protein phosphorylation remains a significant challenge due to the low abundance of phosphoproteins and the low stoichiometry of phosphorylation, which requires effective enrichment of phosphoproteins. Here we have developed superparamagn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2185322fc54e076fc34328b76205764
https://europepmc.org/articles/PMC4372338/
https://europepmc.org/articles/PMC4372338/
Hydrogen/deuterium exchange monitored by mass spectrometry is an important non-perturbing tool to study protein structure and protein–protein interactions. However, water in the reversed-phase liquid chromatography mobile phase leads to back-exchan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c8387e3acc3fa3cd9641bf2ef823ff7
https://europepmc.org/articles/PMC3835171/
https://europepmc.org/articles/PMC3835171/