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Peter J. F. Henderson

Researcher at University of Leeds

Publications -  184
Citations -  8914

Peter J. F. Henderson is an academic researcher from University of Leeds. The author has contributed to research in topics: GalP & Membrane transport protein. The author has an hindex of 46, co-authored 184 publications receiving 8382 citations. Previous affiliations of Peter J. F. Henderson include University of Sheffield & University of London.

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A linear equation that describes the steady-state kinetics of enzymes and subcellular particles interacting with tightly bound inhibitors.

TL;DR: D dose-response measurements generate a linear plot of inhibitor concentration divided by degree of inhibition against velocity without inhibitor divided by velocity with inhibitor, which indicates that the inhibitors of oxidative phosphorylation, rutamycin and bongkrekic acid, are tightly bound to rat liver mitochondria.
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Mammalian and bacterial sugar transport proteins are homologous.

TL;DR: The sequences of the arabinose-H+ and xylose- H+ membrane transport proteins of Escherichia coli are determined and are homologous with each other and with the glucose transporters of human hepatoma1 and rat brain2 cells.
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The action of certain antibiotics on mitochondrial, erythrocyte and artificial phospholipid membranes. The role of induced proton permeability.

TL;DR: The action of enniatin A, valinomycin, the actin homologues, gramicidin, nigericin and dianemycin on mitochondrial respiration could be accounted for by changes in passive ion permeability of the mitochondrial membrane similar to those induced in erythrocytes and phospholipid membranes, if it is assumed that a membrane potential is present in respiring mitochondria.
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Overcoming barriers to membrane protein structure determination

TL;DR: Rational approaches to overcoming the bottlenecks in the field are urgently required as membrane proteins, which typically comprise ∼30% of the proteomes of organisms, are dramatically under-represented in the structural database of the Protein Data Bank.