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David Staunton

Researcher at University of Oxford

Publications -  33
Citations -  1348

David Staunton is an academic researcher from University of Oxford. The author has contributed to research in topics: Leukemia inhibitory factor & Fibronectin. The author has an hindex of 19, co-authored 32 publications receiving 1260 citations.

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The crystal structure and biological function of leukemia inhibitory factor: Implications for receptor binding

TL;DR: The structure of murine leukemia inhibitory factor has been determined by X-ray crystallography at 2.0 A resolution and sequence alignments for the functionally related molecules oncostatin M and ciliary neurotrophic factor, when mapped to the LIF structure, indicate regions of conserved surface character.
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Crystal structure of a cytokine-binding region of gp130.

TL;DR: The structure of the cytokine‐binding homology region of the cell surface receptor gp130 has been determined by X‐ray crystallography at 2.0 Å resolution and suggests a limited flexibility in relative domain orientation of some 3°.
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The GPS Motif Is a Molecular Switch for Bimodal Activities of Adhesion Class G Protein-Coupled Receptors

TL;DR: It is shown that the GPCR proteolytic site (GPS) motif, the molecular hallmark feature of the entire aGPCR class, is essential for LAT-1 signaling serving in two different activity modes of the receptor.
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A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation

Huaying Zhao, +123 more
- 21 May 2015 - 
TL;DR: A multi-laboratory study to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques highlights the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies.
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Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis

TL;DR: This work presents the solution structures of the second type III domain of human FN (2FNIII), and that of an interaction complex between the first two type III domains (1−2FN III), and speculate on the importance of this interaction for FN function.