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Paul L. Greenhaff
Researcher at University of Nottingham
Publications - 287
Citations - 18095
Paul L. Greenhaff is an academic researcher from University of Nottingham. The author has contributed to research in topics: Skeletal muscle & Creatine. The author has an hindex of 72, co-authored 270 publications receiving 16441 citations. Previous affiliations of Paul L. Greenhaff include The Queen's Medical Center & Loughborough University.
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Journal ArticleDOI
The effects of increasing exercise intensity on muscle fuel utilisation in humans
Luc J. C. van Loon,Paul L. Greenhaff,Dumitru Constantin-Teodosiu,Wim H. M. Saris,Anton J. M. Wagenmakers +4 more
TL;DR: It is concluded that the most likely mechanism for the reduction in fat oxidation during high‐intensity exercise is a downregulation of carnitine palmitoyltransferase I, either by this marked decline in free carnitines availability or by a decrease in intracellular pH.
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Muscle creatine loading in men
TL;DR: A rapid way to "creatine load" human skeletal muscle is to ingest 20 g of creatine for 6 days, which can be maintained by ingestion of 2 g/day thereafter, and the ingestion of 3 g creatine/day is in the long term likely to be as effective at raising tissue levels as this higher dose.
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Effect of oral creatine supplementation on skeletal muscle phosphocreatine resynthesis.
TL;DR: The data suggest that a dietary-induced increase in muscle total Cr concentration can increase PCr resynthesis during the 2nd min of recovery from intense contraction.
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Influence of oral creatine supplementation of muscle torque during repeated bouts- of maximal voluntary exercise in man
TL;DR: Investigation of the influence of oral creatine supplementation on skeletal muscle isokinetic torque and the accumulation of plasma ammonia and blood lactate during five bouts of maximal exercise found muscle peak torque production was greater and plasma ammonia accumulation was lower during and after exercise after creatine ingestion.
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Disassociation between the effects of amino acids and insulin on signaling, ubiquitin ligases, and protein turnover in human muscle.
Paul L. Greenhaff,Leonidas G. Karagounis,Nicholas Peirce,Elizabeth J. Simpson,Michelle Hazell,Robert Layfield,Henning Wackerhage,Kenneth Smith,Philip J. Atherton,Anna Selby,Michael J. Rennie +10 more
TL;DR: Increasing AA and insulin availability causes changes in anabolic signaling and amounts of enzymes of the ubiquitin-proteasome pathway, which cannot be easily reconciled with observed effects on MPS or LPB.