Results 171 to 180 of about 11,604 (291)

Mass Spectrometry Structural Proteomics Enabled by Limited Proteolysis and Cross‐Linking

open access: yesMass Spectrometry Reviews, EarlyView.
ABSTRACT The exploration of protein structure and function stands at the forefront of life science and represents an ever‐expanding focus in the development of proteomics. As mass spectrometry (MS) offers readout of protein conformational changes at both the protein and peptide levels, MS‐based structural proteomics is making significant strides in the
Haiyan Lu   +4 more
wiley   +1 more source

Cold EI—The Way to Improve GC‐MS and Increase Its Range of Applications

open access: yesMass Spectrometry Reviews, EarlyView.
ABSTRACT Gas chromatography‐mass spectrometry (GC‐MS) with Cold electron ionization (EI) is based on interfacing the GC and MS with a supersonic molecular beam (SMB) along with electron ionization of vibrationally cold sample compounds in the SMB in a contact‐free fly‐through ion source (hence the name Cold EI).
Aviv Amirav   +3 more
wiley   +1 more source

Quantifying Protein–Glycan Interactions Using Native Mass Spectrometry

open access: yesMass Spectrometry Reviews, EarlyView.
ABSTRACT Interactions between glycan‐binding proteins (GBPs) and carbohydrates (glycans) are essential to many biological processes relevant to human health and disease. For most GBPs, however, their glycan interactome—the repertoire of glycans recognized and their specificities—is poorly defined.
Duong T. Bui   +4 more
wiley   +1 more source

Proteomics of Nitrotyrosine: Integrating Mass Spectrometry and Immunodetection in Redox‐Driven Pathology

open access: yesMass Spectrometry Reviews, EarlyView.
ABSTRACT Nitrooxidative stress, driven by excess reactive nitrogen species like peroxynitrite, contributes to the pathogenesis of many chronic diseases. Among its molecular footprints, 3‐nitrotyrosine (3NT) has emerged as a biologically relevant marker of protein nitration.
Brîndușa Alina Petre
wiley   +1 more source

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