ArticleJournal of biomolecular NMR2009
Phosphorylation-induced changes in backbone dynamics of the dematin headpiece C-terminal domain.
Article in Journal of biomolecular NMR, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Dematin Regulates Calcium Mobilization, Thrombosis, and Early Akt Activation in Platelets.Molecular and cellular biology · 2023Article
- Unraveling axonal mechanisms of traumatic brain injury.Acta neuropathologica communications · 2022Article
- Distance-independent Cross-correlated Relaxation and Isotropic Chemical Shift Modulation in Protein Dynamics Studies.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Review
- Correlated motions of C'-N and CJournal of biomolecular NMR · 2018Article
- Cross-correlated relaxation rates between protein backbone H-X dipolar interactions.Journal of biomolecular NMR · 2017Article
- On the unyielding hydrophobic core of villin headpiece.Protein science : a publication of the Protein Society · 2012Article
- Comparison of fast backbone dynamics at amide nitrogen and carbonyl sites in dematin headpiece C-terminal domain and its S74E mutant.Journal of biomolecular NMR · 2010Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Dematin is an actin-binding protein abundant in red blood cells and other tissues. It contains a villin-type 'headpiece' F-actin-binding domain at its extreme C-terminus. The isolated dematin headpiece domain (DHP) undergoes a significant conformational change upon phosphorylation. The mutation of Ser74 to Glu closely mimics the phosphorylation of DHP. We investigated motions in the backbone of DHP and its mutant DHPS74E using several complementary NMR relaxation techniques: laboratory frame (15)N NMR relaxation, which is sensitive primarily to the ps-ns time scale, cross-correlated chemical shift modulation NMR relaxation detecting correlated mus-ms time scale motions of neighboring (13)C' and (15)N nuclei, and cross-correlated relaxation of two (15)N-(1)H dipole-dipole interactions detecting slow motions of backbone NH vectors in successive amino acid residues. The results indicate a reduction in mobility upon the mutation in several regions of the protein. The additional salt bridge formed in DHPS74E that links the N- and C-terminal subdomains is likely to be responsible for these changes.
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Registered trials
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