The fast spin-echo (FSE) sequence is frequently used as a fast data-readout technique in conjunction with other pulse sequence elements, such as in fluid-attenuated inversion-recovery (FLAIR) and double inversion-recovery (DIR) sequences. In order to implement those pulse sequences, an understanding is required of how the longitudinal magnetization evolves during the FSE part of the sequence. This evolution has been addressed to a certain extent by previous publications, but the DIR literature in particular appears to be replete with approximations to the exact expression for the longitudinal magnetization, and several papers contain errors. Equations are therefore presented here for the evolution of the longitudinal magnetization for a FSE readout. These are then applied to calculate the magnetization available immediately prior to the 90 degrees imaging pulse for the FLAIR-FSE and DIR-FSE pulse sequences.
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http://dx.doi.org/10.1002/mrm.20541 | DOI Listing |
Sci Transl Med
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Institute for Stroke and Dementia Research (ISD), University Hospital, LMU Munich, 81377 Munich, Germany.
In Alzheimer's disease (AD), amyloid-β (Aβ) triggers the aggregation and spreading of tau pathology, which drives neurodegeneration and cognitive decline. However, the pathophysiological link between Aβ and tau remains unclear, which hinders therapeutic efforts to attenuate Aβ-related tau accumulation. Aβ has been found to trigger neuronal hyperactivity and hyperconnectivity, and preclinical research has shown that tau spreads across connected neurons in an activity-dependent manner.
View Article and Find Full Text PDFJ Phys Chem Lett
January 2025
Department of Chemistry and Applied Biosciences, ETH Zurich, Vladimir Prelog Weg 2, 8093 Zurich, Switzerland.
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View Article and Find Full Text PDFJ Biomol NMR
January 2025
Department of Chemistry "Ugo Schiff" and Magnetic Resonance Center (CERM), University of Florence, Florence, Italy.
Intrinsically disordered proteins and protein regions are central to many biological processes but difficult to characterize at atomic resolution. Nuclear magnetic resonance is particularly well-suited for providing structural and dynamical information on intrinsically disordered proteins, but existing NMR methodologies need to be constantly refined to provide greater sensitivity and resolution, particularly to capitalise on the potential of high magnetic fields to investigate large proteins. In this paper, we describe how N-detected 2D NMR experiments can be optimised for better performance.
View Article and Find Full Text PDFChild Obes
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Department of Pediactrics, The Children's Obesity Clinic, Accredited European Centre for Obesity Management, Copenhagen University Hospital Holbæk, Holbæk, Denmark.
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View Article and Find Full Text PDFEur J Clin Invest
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Department of Clinical Therapeutics, National and Kapodistrian University of Athens, Athens, Greece.
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