about
Augmenting light coverage for photosynthesis through YFP-enhanced charge separation at the Rhodobacter sphaeroides reaction centreIt takes two to tango: two TatA paralogues and two redox enzyme-specific chaperones are involved in the localization of twin-arginine translocase substrates in Campylobacter jejuni.A bioelectrochemical approach to characterize extracellular electron transfer by Synechocystis sp. PCC6803Quantifying Integrated Proteomic Responses to Iron Stress in the Globally Important Marine Diazotroph Trichodesmium.Lateral Segregation of Photosystem I in Cyanobacterial Thylakoids.Evidence for polyploidy in the globally important diazotroph Trichodesmium.Two Unrelated 8-Vinyl Reductases Ensure Production of Mature Chlorophylls in Acaryochloris marina.Reduction of fumarate, mesaconate and crotonate by Mfr, a novel oxygen-regulated periplasmic reductase in Campylobacter jejuni.Roles of the twin-arginine translocase and associated chaperones in the biogenesis of the electron transport chains of the human pathogen Campylobacter jejuni.Hydrogenase activity in the foodborne pathogen Campylobacter jejuni depends upon a novel ABC-type nickel transporter (NikZYXWV) and is SlyD-independent.A Multicopper Oxidase (Cj1516) and a CopA Homologue (Cj1161) Are Major Components of the Copper Homeostasis System of Campylobacter jejuni.Determination of Cell Doubling Times from the Return-on-Investment Time of Photosynthetic Vesicles Based on Atomic Detail Structural Models.Phosphite utilization by the globally important marine diazotroph Trichodesmium.Repurposing a photosynthetic antenna protein as a super-resolution microscopy label.Transcriptome and proteome dynamics in chemostat culture reveal how Campylobacter jejuni modulates metabolism, stress responses and virulence factors upon changes in oxygen availability.The molecular basis of phosphite and hypophosphite recognition by ABC-transporters.Probing the local lipid environment of the Rhodobacter sphaeroides cytochrome bc1 and Synechocystis sp. PCC 6803 cytochrome b6f complexes with styrene maleic acid.Identification of protein W, the elusive sixth subunit of the Rhodopseudomonas palustris reaction center-light harvesting 1 core complex.Desert Dust as a Source of Iron to the Globally Important Diazotroph Trichodesmium.Tapping the Unused Potential of Photosynthesis with a Heterologous Electron Sink.Biosynthesis of Chlorophyll a in a Purple Bacterial Phototroph and Assembly into a Plant Chlorophyll-Protein Complex.Probing the quality control mechanism of the Escherichia coli twin-arginine translocase with folding variants of a de novo-designed heme protein.Plant and algal chlorophyll synthases function in Synechocystis and interact with the YidC/Alb3 membrane insertaseA Rhamnose-Inducible System for Precise and Temporal Control of Gene Expression in CyanobacteriaA photosynthetic antenna complex foregoes unity carotenoid-to-bacteriochlorophyll energy transfer efficiency to ensure photoprotectionCryo-EM structure of the spinach cytochrome b6 f complex at 3.6 Å resolutionAtoms to Phenotypes: Molecular Design Principles of Cellular Energy MetabolismStructural and functional characterization of IdiA/FutA (Tery_3377), an iron-binding protein from the ocean diazotroph Trichodesmium erythraeumPhosphite binding by the HtxB periplasmic binding protein depends on the protonation state of the ligandMembrane organization of photosystem I complexes in the most abundant phototroph on EarthProgress and challenges in engineering cyanobacteria as chassis for light-driven biotechnologyThe ChlD subunit links the motor and porphyrin binding subunits of magnesium chelatase
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P50
description
hulumtues
@sq
researcher
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wetenschapper
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հետազոտող
@hy
name
Andrew Hitchcock
@ast
Andrew Hitchcock
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Andrew Hitchcock
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Andrew Hitchcock
@nl
Andrew Hitchcock
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type
label
Andrew Hitchcock
@ast
Andrew Hitchcock
@en
Andrew Hitchcock
@es
Andrew Hitchcock
@nl
Andrew Hitchcock
@sl
prefLabel
Andrew Hitchcock
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Andrew Hitchcock
@en
Andrew Hitchcock
@es
Andrew Hitchcock
@nl
Andrew Hitchcock
@sl
P106
P21
P2798
P31
P496
0000-0001-6572-434X