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Cybersecurity and research do not have to be opposed to each other. With increasing cyberattacks, it is more important than ever for cybersecurity and research to corporate. The authors describe how Research Liaisons and Information Assurance: Michigan Medicine (IA:MM) collaborate at Michigan Medicine, an academic medical center subject to strict

Cybersecurity and research do not have to be opposed to each other. With increasing cyberattacks, it is more important than ever for cybersecurity and research to corporate. The authors describe how Research Liaisons and Information Assurance: Michigan Medicine (IA:MM) collaborate at Michigan Medicine, an academic medical center subject to strict HIPAA controls and frequent risk assess- ments. IA:MM provides its own Liaison to work with the Research Liaisons to better understand security process and guide researchers through the process. IA:MM has developed formal risk decision processes and informal engagements with the CISO to provide risk- based cybersecurity instead of controls-based. This collaboration has helped develop mitigating procedures for researchers when standard controls are not feasible.
ContributorsMcCaffrey, Deb (Author) / Kelley, Jessica (Author)
Created2022-07-14
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Description

Background: Cysteine sulfenic acid (Cys-SOH) plays important roles in the redox regulation of numerous proteins. As a relatively unstable posttranslational protein modification it is difficult to quantify the degree to which any particular protein is modified by Cys-SOH within a complex biological environment. The goal of these studies was to move

Background: Cysteine sulfenic acid (Cys-SOH) plays important roles in the redox regulation of numerous proteins. As a relatively unstable posttranslational protein modification it is difficult to quantify the degree to which any particular protein is modified by Cys-SOH within a complex biological environment. The goal of these studies was to move a step beyond detection and into the relative quantification of Cys-SOH within specific proteins found in a complex biological setting--namely, human plasma.

Results: This report describes the possibilities and limitations of performing such analyses based on the use of thionitrobenzoic acid and dimedone-based probes which are commonly employed to trap Cys-SOH. Results obtained by electrospray ionization-based mass spectrometric immunoassay reveal the optimal type of probe for such analyses as well as the reproducible relative quantification of Cys-SOH within albumin and transthyretin extracted from human plasma--the latter as a protein previously unknown to be modified by Cys-SOH.

Conclusions: The relative quantification of Cys-SOH within specific proteins in a complex biological setting can be accomplished, but several analytical precautions related to trapping, detecting, and quantifying Cys-SOH must be taken into account prior to pursuing its study in such matrices.

ContributorsRehder, Douglas (Author) / Borges, Chad (Author) / Biodesign Institute (Contributor)
Created2010-07-01