ArticleJournal of the American Society for Mass Spectrometry1998
Zinc-induced conformational changes in the DNA-binding domain of the vitamin D receptor determined by electrospray ionization mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 44 citations in OpenAlex.
- Zinc and its role in vitamin D function.Current research in physiology · 2022Review
- H/D exchange kinetics: experimental evidence for formation of different b fragment ion conformers/isomers during the gas-phase peptide sequencing.Journal of the American Society for Mass Spectrometry · 2010Article
- Mode of action of cGMP-dependent protein kinase-specific inhibitors probed by photoaffinity cross-linking mass spectrometry.The Journal of biological chemistry · 2009Article
- Expression and regulation of the vitamin D receptor in the zebrafish, Danio rerio.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2008Article
- Metal-binding properties of human centrin-2 determined by micro-electrospray ionization mass spectrometry and UV spectroscopy.Journal of the American Society for Mass Spectrometry · 2006Article
- Conformational changes in the herpes simplex virus ICP8 DNA-binding protein coincident with assembly in viral replication structures.Journal of virology · 2003Article
- Using nondenaturing mass spectrometry to detect fortuitous ligands in orphan nuclear receptors.Protein science : a publication of the Protein Society · 2003Article
- Probing metal ion binding and conformational properties of the colicin E9 endonuclease by electrospray ionization time-of-flight mass spectrometry.Protein science : a publication of the Protein Society · 2002Article
- Article
- Gas phase hydrogen deuterium exchange reactions of a model peptide: FT-ICR and computational analyses of metal induced conformational mutations.Journal of the American Society for Mass Spectrometry · 2001Article
- First observation by mass spectrometry of a 3+ oxidation state for a [4Fe-4S] metalloprotein: an ESI-FTICR mass spectrometry study of the high potential iron-sulfur protein from Chromatium vinosum.Journal of the American Society for Mass Spectrometry · 2001Article
- Effects of pH on the kinetic reaction mechanism of myoglobin unfolding studied by time-resolved electrospray ionization mass spectrometry.Journal of the American Society for Mass Spectrometry · 2000Article
- Copper binding to octarepeat peptides of the prion protein monitored by mass spectrometry.Protein science : a publication of the Protein Society · 2000Article
- Unfolding of proteins monitored by electrospray ionization mass spectrometry: a comparison of positive and negative ion modes.Journal of the American Society for Mass Spectrometry · 1998Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Electrospray ionization mass spectrometry (ESI-MS) was used to measure conformational changes within the DNA-binding domain of the vitamin D receptor (VDR DBD) upon binding zinc (Zn2+). As increasing concentrations of Zn2+ were added to the VDR DBD, a gradual shift in the mass envelope to lower charge states was observed in the multiply charged spectrum. The shift in the charge states was correlated to changes observed in the far-ultraviolet circular dichroic (far-UV CD) spectrum of the protein as it was titrated with Zn2+. Both the multiply charged ESI and far-UV CD spectra of the Zn(2+)-titrated protein show that the binding of the first Zn2+ ion to the protein results in very little conformational change in the protein. The binding of a second Zn2+ ion resulted in a significant alteration in the structure of the protein as indicated by changes in both the multiply charged ESI and far-UV CD spectra. Much smaller changes were seen within the multiply charged ESI or far-UV CD spectra upon increasing the Zn2+ concentration beyond 2 mol/mol of protein. The results presented indicate that ESI-MS in combination with CD is a powerful method to measure gross conformational changes induced by the binding of metals to metalloproteins.
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Registered trials
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