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- Andrey N. Pravdivtsev
- Section Biomedical Imaging Molecular Imaging North Competence Center (MOIN CC) Department of Radiology and Neuroradiology University Medical Center Schleswig-Holstein (UKSH) Kiel University Am Botanischen Garten 14 24118 Kiel Germany
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- Gerd Buntkowsky
- Technical University Darmstadt Eduard-Zintl-Institute for Inorganic and Physical Chemistry Alarich-Weiss-Strasse 8 64287 Darmstadt Germany
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- Simon B. Duckett
- Department Center for Hyperpolarization in Magnetic Resonance (CHyM) Department of Chemistry University of York, Heslington York YO10 5NY UK
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- Igor V. Koptyug
- International Tomography Center SB RAS 3A Institutskaya st. 630090 Novosibirsk Russia
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- Jan‐Bernd Hövener
- Section Biomedical Imaging Molecular Imaging North Competence Center (MOIN CC) Department of Radiology and Neuroradiology University Medical Center Schleswig-Holstein (UKSH) Kiel University Am Botanischen Garten 14 24118 Kiel Germany
抄録
<jats:title>Abstract</jats:title><jats:p>Nuclear magnetic resonance (NMR) has become a universal method for biochemical and biomedical studies, including metabolomics, proteomics, and magnetic resonance imaging (MRI). By increasing the signal of selected molecules, the hyperpolarization of nuclear spin has expanded the reach of NMR and MRI even further (e.g. hyperpolarized solid‐state NMR and metabolic imaging in vivo). Parahydrogen (pH<jats:sub>2</jats:sub>) offers a fast and cost‐efficient way to achieve hyperpolarization, and the last decade has seen extensive advances, including the synthesis of new tracers, catalysts, and transfer methods. The portfolio of hyperpolarized molecules now includes amino acids, which are of great interest for many applications. Here, we provide an overview of the current literature and developments in the hyperpolarization of amino acids and peptides.</jats:p>
収録刊行物
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- Angewandte Chemie International Edition
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Angewandte Chemie International Edition 60 (44), 23496-23507, 2021-08-13
Wiley