James Mitchell
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View article: A time-resolved Förster resonance energy transfer assay to investigate drug and inhibitor binding to ABCG2
A time-resolved Förster resonance energy transfer assay to investigate drug and inhibitor binding to ABCG2 Open
The human ATP-binding cassette (ABC) transporter, ABCG2, is responsible for multidrug resistance in some tumours. Detailed knowledge of its activity is crucial for understanding drug transport and resistance in cancer, and has implications…
View article: A time-resolved Förster resonance energy transfer assay to investigate inhibitor binding to ABCG2
A time-resolved Förster resonance energy transfer assay to investigate inhibitor binding to ABCG2 Open
The human ATP-binding cassette (ABC) transporter, ABCG2 is responsible for multidrug resistance in some tumours. Detailed knowledge of its activity is crucial for understanding drug transport and resistance in cancer, and has implications …
View article: Analysis of Sequence Divergence in Mammalian ABCGs Predicts a Structural Network of Residues That Underlies Functional Divergence
Analysis of Sequence Divergence in Mammalian ABCGs Predicts a Structural Network of Residues That Underlies Functional Divergence Open
The five members of the mammalian G subfamily of ATP-binding cassette transporters differ greatly in their substrate specificity. Four members of the subfamily are important in lipid transport and the wide substrate specificity of one of t…
View article: Picky ABCG5/G8 and promiscuous ABCG2 ‐ a tale of fatty diets and drug toxicity
Picky ABCG5/G8 and promiscuous ABCG2 ‐ a tale of fatty diets and drug toxicity Open
Structural data on ABCG5/G8 and ABCG2 reveal a unique molecular architecture for subfamily G ATP‐binding cassette (ABCG) transporters and disclose putative substrate‐binding sites. ABCG5/G8 and ABCG2 appear to use several unique structural…
View article: Correction: Comparison of the molecular properties of retinitis pigmentosa P23H and N15S amino acid replacements in rhodopsin
Correction: Comparison of the molecular properties of retinitis pigmentosa P23H and N15S amino acid replacements in rhodopsin Open
[This corrects the article DOI: 10.1371/journal.pone.0214639.].
View article: Comparison of the molecular properties of retinitis pigmentosa P23H and N15S amino acid replacements in rhodopsin
Comparison of the molecular properties of retinitis pigmentosa P23H and N15S amino acid replacements in rhodopsin Open
Mutations in the RHO gene encoding for the visual pigment protein, rhodopsin, are among the most common cause of autosomal dominant retinitis pigmentosa (ADRP). Previous studies of ADRP mutations in different domains of rhodopsin have indi…
View article: Structural and Functional Consequences of the Weak Binding of Chlorin e6 to Bovine Rhodopsin
Structural and Functional Consequences of the Weak Binding of Chlorin e6 to Bovine Rhodopsin Open
The chlorophyll‐derivative chlorin e6 (Ce6) identified in the retinas of deep‐sea ocean fish is proposed to play a functional role in red bioluminescence detection. Fluorescence and 1 H NMR spectroscopy studies with the bovine dim‐light ph…
View article: Structural stability, dynamics and unfolding of 7-transmembrane helical receptors
Structural stability, dynamics and unfolding of 7-transmembrane helical receptors Open
The dynamics of membrane proteins is an understudied area due to the difficulties in production and manipulation of samples. Interactions of the G-protein coupled receptor, rhodopsin, with an allosteric reagent were systematically investig…