ArticleMethods in enzymology2011
Probing serpin conformational change using mass spectrometry and related methods.
Article in Methods in enzymology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- Structural and functional characterization of human kallistatin.Biochemistry and biophysics reports · 2026Article
- Functional mass spectrometry indicates anti-protease and complement activity increase with COVID-19 severity.Experimental biology and medicine (Maywood, N.J.) · 2025Article
- Functional and dysfunctional conformers of human neuroserpin characterized by optical spectroscopies and Molecular Dynamics.Biochimica et biophysica acta · 2015Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The folding, misfolding, and inhibitory mechanisms of serpins are linked to both thermodynamic metastability and conformational flexibility. Characterizing the structural distribution of stability and flexibility in serpins in solution is challenging due to their large size and propensity for aggregation. Structural mass spectrometry techniques offer powerful tools for probing the mechanisms of serpin function and disfunction. In this chapter, we review the principles of the two most commonly employed structural mass spectrometry techniques--hydrogen/deuterium exchange and chemical footprinting--and describe their application to studying serpin flexibility, stability, and conformational change in solution. We also review the application of both hydrogen/deuterium exchange and ion mobility mass spectrometry to probe the mechanism of serpin polymerization and the structure of serpin polymers.
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