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Introduction: Longitudinally extensive spinal cord lesions (LESCL) are characterized by T2-hyperintense signals spanning at least three vertebral body segments, with neuromyelitis optica spectrum disorders (NMOSD) being a significant cause. This study aimed to characterize the clinical, radiological, serological, and cerebrospinal fluid (CSF) features of LESCL and to compare NMOSD and non-NMOSD cases.

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(1) Background: MALDI imaging is a technique that still largely depends on time of flight (TOF)-based instrument such as the Bruker UltrafleXtreme. While capable of performing targeted MS/MS, these instruments are unable to perform fragmentation while imaging a tissue section necessitating the reliance of MS1 values for peptide level identifications. With this premise in mind, we have developed a hybrid bioinformatic/image-based method for the identification and validation of viral biomarkers.

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Objective: The aim of this study was to evaluate the relevance of ultrasonography training by non-experts carrying out quadriceps muscle mass assessment.

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In the last decade, strains of the genera and have been misclassified as first and later Because is a serious foodborne pathogen that affects premature neonates and elderly individuals, such misidentification may not only falsify epidemiological statistics but also lead to tests of powdered infant formula or other foods giving false results. Currently, the main ways of identifying and strains are by biochemical testing or by sequencing of the gene as part of multilocus sequence typing (MLST), but in relation to these strains the former is generally highly difficult and unreliable while the latter remains expensive. To address this, we developed a fast, simple, and most importantly, reliable method for and identification based on intact-cell matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS).

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Mapping protein structural changes by quantitative cross-linking.

Methods

November 2015

Laboratory of Structural Biology and Cell Signaling, Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague, Czech Republic; Department of Biochemistry, Faculty of Science, Charles University, Prague, Czech Republic. Electronic address:

Chemical cross-linking is a promising technology for protein tertiary structure determination. Though the data has low spatial resolution, it is possible to obtain it at physiological conditions on proteins that are not amenable to standard high resolution techniques such as X-ray, NMR analysis and cryo-EM. Here we demonstrate the utilization of isotopically labeled chemical cross-linking to visualize protein conformation rearrangements.

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