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            <title><![CDATA[HIGH RESOLUTION MASS SPECTROMETRY IN LIPIDOMICS]]></title>
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            <link>https://www.novareader.co/book/isbn/10.1002/mas.21627</link>
            <description><![CDATA[<p class="para" id="N65539">The boost of research output in lipidomics during the last decade is tightly linked to improved instrumentation in mass spectrometry. Associated with this trend is the shift from low resolution—toward high‐resolution lipidomics platforms. This review article summarizes the state of the art in the lipidomics field with a particular focus on the merits of high mass resolution. Following some theoretical considerations on the benefits of high mass resolution in lipidomics, it starts with a historical perspective on lipid analysis by sector instruments and moves further to today's instrumental approaches, including shotgun lipidomics, liquid chromatography–mass spectrometry, matrix‐assisted laser desorption ionization‐time‐of‐flight, and imaging lipidomics. Subsequently, several data processing and data analysis software packages are critically evaluated with all their pros and cons. Finally, this article emphasizes the importance and necessity of quality standards as the field evolves from its pioneering phase into a mature and robust omics technology and lists various initiatives for improving the applicability of lipidomics. © 2020 The Authors. <i>Mass Spectrometry Reviews</i> published by John Wiley &amp; Sons Ltd. Mass Spec Rev</p>]]></description>
            <pubDate><![CDATA[2020-03-31T00:00]]></pubDate>
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            <title><![CDATA[THE MAKING OF A FOOTPRINT IN PROTEIN FOOTPRINTING: A REVIEW IN HONOR OF MICHAEL L. GROSS]]></title>
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            <link>https://www.novareader.co/book/isbn/10.1002/mas.21632</link>
            <description><![CDATA[<p class="para" id="N65539">Within the past decade protein footprinting in conjunction with mass spectrometry has become a powerful and versatile means to unravel the higher order structure of proteins. Footprinting‐based approaches has demonstrated the capacity to inform on interaction sites and dynamic regions that participate in conformational changes. These findings when set in a biological perspective inform on protein folding/unfolding, protein–protein interactions, and protein–ligand interactions. In this review, we will look at the contribution of Dr. Michael L. Gross to protein footprinting approaches such as hydrogen deuterium exchange mass spectrometry and hydroxyl radical protein footprinting. This review details the development of novel footprinting methods as well as their applications to study higher order protein structure. © 2020 The Authors. Mass Spectrometry Reviews published by John Wiley &amp; Sons Ltd. Mass Spec Rev</p>]]></description>
            <pubDate><![CDATA[2020-05-12T00:00]]></pubDate>
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