M
Mike Smith
Researcher at University of Oxford
Publications - 14
Citations - 945
Mike Smith is an academic researcher from University of Oxford. The author has contributed to research in topics: Major histocompatibility complex & Phosphocreatine. The author has an hindex of 12, co-authored 14 publications receiving 902 citations.
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The New College Vision and Laser Data Set
TL;DR: A large dataset intended for use in mobile robotics research, gathered from a robot driving several kilometers through a park and campus, contains a five-degree-of-freedom dead-reckoned trajectory, laser range/reflectance data and 20 Hz stereoscopic and omnidirectional imagery.
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Navigating, Recognizing and Describing Urban Spaces With Vision and Lasers
Paul Newman,Gabe Sibley,Mike Smith,Mark Cummins,Alastair Harrison,Christopher Mei,Ingmar Posner,Robbie Shade,Derik Schroeter,Liz Murphy,Winston Churchill,Dave Cole,Ian Reid +12 more
TL;DR: A body of work aimed at extending the reach of mobile navigation and mapping is described, showing how running topological and metric mapping and pose estimation processes concurrently, using vision and laser ranging, has produced a full six-degree-of-freedom outdoor navigation system.
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A sequence pattern for peptides presented to cytotoxic T lymphocytes by HLA B8 revealed by analysis of epitopes and eluted peptides
Julian Sutton,Sarah Rowland-Jones,William Rosenberg,Douglas F. Nixon,Frances M. Gotch,Xiao-Ming Gao,Nicholas Murray,Anna Spoonas,Paul C. Driscoll,Mike Smith,Anthony Willis,Andrew J. McMichael +11 more
TL;DR: HLA B8‐restricted cytotoxic T lymphocytes (CTL) specific for influenza A virus were generated and shown to recognize the nucleoprotein (NP) and one of the predicted epitope peptides was made and showed to be recognized by specific CTL.
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Peptide selection by class I molecules of the major histocompatibility complex.
TL;DR: Comparison of over 100 peptides reveals the importance of the carboxy-terminal residue in selective binding of major histocompatibility complex peptides.
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In vivo functioning of creatine phosphokinase in human forearm muscle, studied by 31P NMR saturation transfer.
TL;DR: 31P nuclear magnetic resonance (NMR) saturation transfer has been used to measure enzymatic flux through the creatine phosphokinase reaction in the direction of ATP synthesis in the human forearm muscle flexor digitorum superficialis, finding a discrepancy contrary to the increase in flux predicted from previous saturation transfer studies.