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Mark Youles

Researcher at University of East Anglia

Publications -  12
Citations -  1300

Mark Youles is an academic researcher from University of East Anglia. The author has contributed to research in topics: Synthetic biology & Effector. The author has an hindex of 6, co-authored 9 publications receiving 1021 citations. Previous affiliations of Mark Youles include Norwich Research Park & Medical Research Council.

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Journal ArticleDOI

A Golden Gate Modular Cloning Toolbox for Plants

TL;DR: A versatile resource for plant biologists comprising a set of cloning vectors and 96 standardized parts to enable Golden Gate construction of multigene constructs for plant transformation is presented.
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Standards for plant synthetic biology: a common syntax for exchange of DNA parts.

Nicola J. Patron, +67 more
- 01 Oct 2015 - 
TL;DR: A standard for Type IIS restriction endonuclease-mediated assembly is described, defining a common syntax of 12 fusion sites to enable the facile assembly of eukaryotic transcriptional units.
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Structural basis of hepatocyte growth factor/scatter factor and MET signalling.

TL;DR: The study shows how the proteolytic mechanism of activation of the complex proteinases has been adapted to cell signaling in vertebrate organisms, offers a description of monomeric and dimeric ligand-receptor complexes, and provides a foundation to the structural basis of HGF/SF-MET signaling.
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Functional map and domain structure of MET, the product of the c-met protooncogene and receptor for hepatocyte growth factor/scatter factor

TL;DR: 3D models and a functional map of the large ectodomain of MET are provided and they have broad implications for structure-function of the MET receptor and the related semaphorin and plexin proteins.
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Engineering the NK1 fragment of hepatocyte growth factor/scatter factor as a MET receptor antagonist.

TL;DR: A subset of mutants at the NK1 dimer interface, such as the linker mutants Y124A or N127A or the kringle mutant V140A:I142A, bind the MET receptor with affinities comparable to wild-type NK1 but fail to assemble a dimeric, signalling competent NK1-MET complex.