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Richard James

Researcher at University of East Anglia

Publications -  60
Citations -  3362

Richard James is an academic researcher from University of East Anglia. The author has contributed to research in topics: Colicin & Plasmid. The author has an hindex of 28, co-authored 60 publications receiving 3268 citations. Previous affiliations of Richard James include University of Leicester.

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Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana

TL;DR: Analysis of the sequence revealed an average gene density of one gene every 4.8 kilobases, and 54% of the predicted genes had significant similarity to known genes, and other interesting features were found, such as the sequence of a disease-resistance gene locus, the distribution of retroelements, and the frequent occurrence of clustered gene families.
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Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9.

TL;DR: The results show that the population of an intermediate in the refolding of the immunity protein structure is defined by the precise amino acid sequence rather than the global stability of the protein.
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The biology of E colicins: paradigms and paradoxes

TL;DR: The BRP is involved in release of the colicin-immunity protein complex from the producing cell and causes partial cell lysis upon strong induction of the SOS promoter.
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Structural and mechanistic basis of immunity toward endonuclease colicins

TL;DR: The crystal structure of the cytotoxic endonuclease domain from the bacterial toxin colicin E9 in complex with its cognate immunity protein Im9 reveals that the inhibitor does not bind at the active site, but rather at an adjacent position leaving theActive site exposed yet unable to bind DNA because of steric and electrostatic clashes with incoming substrate.
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Specificity in protein-protein interactions: the structural basis for dual recognition in endonuclease colicin-immunity protein complexes.

TL;DR: The 1.7 A crystal structure of the 24.5 kDa complex formed between the endonuclease domain of colicin E9 and its cognate immunity protein Im9 is reported, which provides a molecular rationale for this mechanism and highlights how specificity is achieved by very different interactions in the two complexes.