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40
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Text
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<a href="http://doi.org/10.1016/j.ab.2020.114067" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.ab.2020.114067</a>
Pages
114067
Volume
615
ISSN
1096-0309 0003-2697
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<a href="http://neomed.idm.oclc.org/login?url=http://doi.org/10.1016/j.ab.2020.114067" target="_blank" rel="noreferrer noopener">NEOMED Full-text Holding (if available) - Proxy DOI: 10.1016/j.ab.2020.114067</a>
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Update Year & Number
January 2021 List
NEOMED College
NEOMED College of Pharmacy
NEOMED Department
Department of Pharmaceutical Sciences
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The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
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Measuring acetyl-coa and acetylated histone turnover in vivo: Effect of a high fat diet.
Publisher
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Analytical Biochemistry
Date
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2021
2021-02-15
Subject
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Acetyl-CoA; Acetylation; Heavy water; High resolution mass spectrometry; Histone; Turnover
Creator
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Arias-Alvarado A; Aghayev M; Ilchenko S; Rachdaoui N; Lepp J; Tsai T-H; Zhang G-F; Previs S; Kasumov T
Description
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Cellular availability of acetyl-CoA, a central intermediate of metabolism, regulates histone acetylation. The impact of a high-fat diet (HFD) on the turnover rates of acetyl-CoA and acetylated histones is unknown. We developed a method for simultaneous measurement of acetyl-CoA and acetylated histones kinetics using a single (2)H(2)O tracer, and used it to examine effect of HFD-induced perturbations on hepatic histone acetylation in LDLR(-/-) mice, a mouse model of non-alcoholic fatty liver disease (NAFLD). Mice were given (2)H(2)O in the drinking water and the kinetics of hepatic acetyl-CoA, histones, and acetylated histones were quantified based on their (2)H-labeling. Consumption of a high fat Western-diet (WD) for twelve weeks led to decreased acetylation of hepatic histones (p< 0.05), as compared to a control diet. These changes were associated with 1.5-3-fold increased turnover rates of histones without any change in acetyl-CoA flux. Acetylation significantly reduced the stability of histones and the turnover rates of acetylated peptides were correlated with the number of acetyl groups in neighboring lysine sites. We conclude that (2)H(2)O-method can be used to study metabolically controlled histone acetylation and acetylated histone turnover in vivo.
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<a href="http://doi.org/10.1016/j.ab.2020.114067" target="_blank" rel="noreferrer noopener">10.1016/j.ab.2020.114067</a>
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journalArticle
2021
Acetyl-CoA
Acetylation
Aghayev M
Analytical biochemistry
Arias-Alvarado A
Department of Pharmaceutical Sciences
Heavy water
High resolution mass spectrometry
Histone
Ilchenko S
January 2021 List
journalArticle
Kasumov T
Lepp J
NEOMED College of Pharmacy
Previs S
Rachdaoui N
Tsai T-H
Turnover
Zhang G-F
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1021/acschembio.0c00380" target="_blank" rel="noreferrer noopener">http://doi.org/10.1021/acschembio.0c00380</a>
ISSN
1554-8937
Search for Full-text
Locate full-text within NEOMED Library's e-journal collections
<a href="http://neomed.idm.oclc.org/login?url=http://doi.org/10.1021/acschembio.0c00380" target="_blank" rel="noreferrer noopener">NEOMED Full-text Holding (if available) - Proxy DOI: 10.1021/acschembio.0c00380</a>
<p>Users with a NEOMED Library login can search for full-text journal articles at the following url: <a href="https://libraryguides.neomed.edu/home">https://libraryguides.neomed.edu/home</a></p>
Update Year & Number
September 2020 List
NEOMED College
NEOMED College of Pharmacy
NEOMED Department
Department of Pharmaceutical Sciences
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
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Examining targeted protein degradation from physiological and analytical perspectives: Enabling translation between cells and subjects.
Publisher
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ACS Chemical Biology
Date
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2020
2020-09-30
Creator
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Daurio NA;Zhou H;Chen Y;Sheth PR;Imbriglio JE;McLaren DG;Tawa P;Rachdaoui N;Previs MJ;Kasumov T;O'Neil J;Previs SF
Description
An account of the resource
The ability to target specific proteins for degradation may open a new door toward developing therapeutics. Although effort in chemistry is essential for advancing this modality, i.e., one needs to generate proteolysis targeting chimeras (bifunctional molecules, also referred to as PROTACS) or "molecular glues" to accelerate protein degradation, we suspect that investigations could also benefit by directing attention toward physiological regulation surrounding protein homeostasis, including the methods that can be used to examine changes in protein kinetics. This perspective will first consider some metabolic scenarios that might be of importance when one aims to change protein abundance by increasing protein degradation. Specifically, could protein turnover impact the apparent outcome? We will then outline how to study protein dynamics by coupling stable isotope tracer methods with mass spectrometry-based detection; since the experimental conditions could have a dramatic effect on protein turnover, special attention is directed toward the application of methods for quantifying protein kinetics using in vitro and in vivo models. Our goal is to present key concepts that should enable mechanistically informed studies which test targeted protein degradation strategies.
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<a href="http://doi.org/10.1021/acschembio.0c00380" target="_blank" rel="noreferrer noopener">10.1021/acschembio.0c00380</a>
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
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journalArticle
2020
Acs Chemical Biology
Chen Y
Daurio NA
Department of Pharmaceutical Sciences
Imbriglio JE
journalArticle
Kasumov T
McLaren DG
NEOMED College of Pharmacy
O'Neil J
Previs MJ
Previs SF
Rachdaoui N
September 2020 List
Sheth PR
Tawa P
Zhou H