1
40
3
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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/10.1016/j.freeradbiomed.2012.05.025" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.freeradbiomed.2012.05.025</a>
Pages
962–973
Issue
4
Volume
53
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
A name given to the resource
Protein thiyl radical mediates S-glutathionylation of complex I.
Publisher
An entity responsible for making the resource available
Free radical biology & medicine
Date
A point or period of time associated with an event in the lifecycle of the resource
2012
2012-08
Subject
The topic of the resource
*Oxidative Stress; Amino Acid Motifs; Amino Acid Sequence; Animals; Binding Sites; Cattle; Cell Line; Cyclic N-Oxides/chemistry/pharmacology; Cysteine/chemistry/*metabolism; Electron Transport Complex I/chemistry/*metabolism; Free Radical Scavengers/chemistry/pharmacology; Free Radicals/chemistry/*metabolism; Glutathione/chemistry/*metabolism; Heart/enzymology/metabolism; Mice; Mitochondria; Models; Molecular; Molecular Sequence Data; Muscle Cells/drug effects/metabolism; Onium Compounds/pharmacology; Peptide Fragments/chemistry; Peptide Mapping; Protein; Rats; Rotenone/pharmacology; Structural Homology; Superoxides/metabolism
Creator
An entity primarily responsible for making the resource
Kang Patrick T; Zhang Liwen; Chen Chwen-Lih; Chen Jingfeng; Green Kari B; Chen Yeong-Renn
Description
An account of the resource
Complex I is a critical site of O(2)(*-) production and the major host of reactive protein thiols in mitochondria. In response to oxidative stress, complex I protein thiols at the 51- and 75-kDa subunits are reversibly
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.freeradbiomed.2012.05.025" target="_blank" rel="noreferrer noopener">10.1016/j.freeradbiomed.2012.05.025</a>
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Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Oxidative Stress
2012
Amino Acid Motifs
Amino Acid Sequence
Animals
Binding Sites
Cattle
Cell Line
Chen Chwen-Lih
Chen Jingfeng
Chen Yeong-Renn
Cyclic N-Oxides/chemistry/pharmacology
Cysteine/chemistry/*metabolism
Department of Integrative Medical Sciences
Electron Transport Complex I/chemistry/*metabolism
Free radical biology & medicine
Free Radical Scavengers/chemistry/pharmacology
Free Radicals/chemistry/*metabolism
Glutathione/chemistry/*metabolism
Green Kari B
Heart/enzymology/metabolism
Kang Patrick T
Mice
Mitochondria
Models
Molecular
Molecular Sequence Data
Muscle Cells/drug effects/metabolism
NEOMED College of Medicine
Onium Compounds/pharmacology
Peptide Fragments/chemistry
Peptide Mapping
Protein
Rats
Rotenone/pharmacology
Structural Homology
Superoxides/metabolism
Zhang Liwen
-
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/10.1016/j.freeradbiomed.2017.04.022" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.freeradbiomed.2017.04.022</a>
Pages
595–609
Volume
108
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
A name given to the resource
Differential protein acetylation assists import of excess SOD2 into mitochondria and mediates SOD2 aggregation associated with cardiac hypertrophy in the murine
Publisher
An entity responsible for making the resource available
Free radical biology & medicine
Date
A point or period of time associated with an event in the lifecycle of the resource
2017
2017-07
Subject
The topic of the resource
*Cardiac-specific transgenic mouse; *Mitochondria; *Mitochondrial translocation; *Protein acetylation; *Protein aggregation; *SOD2; Acetylation; Animals; Cardiomegaly/*metabolism; Cytosol/*metabolism; Heart/*physiology; Mice; Mitochondria/*metabolism; Pathological; Post-Translational; Protein Aggregation; Protein Folding; Protein Processing; Protein Transport; Reactive Oxygen Species/metabolism; Sirtuin 3/metabolism; Superoxide Dismutase/genetics/*metabolism; Transgenic
Creator
An entity primarily responsible for making the resource
Zhang Liwen; Chen Chwen-Lih; Kang Patrick T; Jin Zhicheng; Chen Yeong-Renn
Description
An account of the resource
SOD2 is the primary antioxidant enzyme neutralizing (*)O2(-) in mitochondria. Cardiac-specific SOD2 overexpression (SOD2-tg) induces supernormal function and cardiac hypertrophy in the mouse heart. However, the reductive stress imposed by SOD2 overexpression results in protein aggregation of SOD2 pentamers and differential hyperacetylation of SOD2 in the mitochondria and cytosol. Here, we studied SOD2 acetylation in SOD2-tg and wild-type mouse hearts. LC-MS/MS analysis indicated the presence of four acetylated lysines in matrix SOD2 and nine acetylated lysines in cytosolic SOD2 from the SOD2-tg heart. However, only one specific acetylated lysine residue was detected in the mitochondria of the wild-type heart, which was consistent with Sirt3 downregulation in the SOD2-tg heart. LC-MS/MS further detected hyperacetylated SOD2 with a signaling peptide in the mitochondrial inner membrane and matrix of the SOD2-tg heart, indicating partial arrest of the SOD2 precursor in the membrane during translocation into the mitochondria. Upregulation of HSP 70 and cytosolic HSP 60 enabled the translocation of excess SOD2 into mitochondria. In vitro acetylation of matrix SOD2 with Ac2O deaggregated pentameric SOD2, restored the profile of cytosolic SOD2 hyperacetylation, and decreased matrix SOD2 activity. As revealed by 3D structure, acetylation of K89, K134, and K154 of cytosolic SOD2 induces unfolding of the tertiary structure and breaking of the salt bridges that are important for the quaternary structure, suggesting that hyperacetylation and HSP 70 upregulation maintain the unfolded status of SOD2 in the cytosol and mediate the import of SOD2 across the membrane. Downregulation of Sirt3, HSP 60, and presequence protease in the mitochondria of the SOD2-tg heart promoted protein misfolding that led to pentameric aggregation.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.freeradbiomed.2017.04.022" target="_blank" rel="noreferrer noopener">10.1016/j.freeradbiomed.2017.04.022</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
*Cardiac-specific transgenic mouse
*Mitochondria
*Mitochondrial translocation
*Protein acetylation
*Protein aggregation
*SOD2
2017
Acetylation
Animals
Cardiomegaly/*metabolism
Chen Chwen-Lih
Chen Yeong-Renn
Cytosol/*metabolism
Department of Integrative Medical Sciences
Free radical biology & medicine
Heart/*physiology
Jin Zhicheng
Kang Patrick T
Mice
Mitochondria/*metabolism
NEOMED College of Medicine
Pathological
Post-Translational
Protein Aggregation
Protein Folding
Protein Processing
Protein Transport
Reactive Oxygen Species/metabolism
Sirtuin 3/metabolism
Superoxide Dismutase/genetics/*metabolism
Transgenic
Zhang Liwen
-
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/10.1016/j.yjmcc.2018.07.244" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.yjmcc.2018.07.244</a>
Pages
190–204
Volume
121
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
A name given to the resource
Mitochondrial complex I in the post-ischemic heart: reperfusion-mediated oxidative injury and protein cysteine sulfonation.
Publisher
An entity responsible for making the resource available
Journal of molecular and cellular cardiology
Date
A point or period of time associated with an event in the lifecycle of the resource
2018
2018-08
Subject
The topic of the resource
Complex I; Mitochondrial dysfunction; Myocardial ischemia and reperfusion; Protein cysteine sulfonation; Protein structure
Creator
An entity primarily responsible for making the resource
Kang Patrick T; Chen Chwen-Lih; Lin Paul; Zhang Liwen; Zweier Jay L; Chen Yeong-Renn
Description
An account of the resource
A serious consequence of ischemia-reperfusion injury (I/R) is oxidative damage leading to mitochondrial dysfunction. Such I/R-induced mitochondrial dysfunction is observed as impaired state 3 respiration and overproduction of O2(-). The cascading ROS can propagate cysteine oxidation on mitochondrial complex I and add insult to injury. Herein we employed LC-MS/MS to identify protein sulfonation of complex I in mitochondria from the infarct region of rat hearts subjected to
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.yjmcc.2018.07.244" target="_blank" rel="noreferrer noopener">10.1016/j.yjmcc.2018.07.244</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
2018
Chen Chwen-Lih
Chen Yeong-Renn
Complex I
Department of Family & Community Medicine
Department of Integrative Medical Sciences
Journal of molecular and cellular cardiology
Kang Patrick T
Lin Paul
Mitochondrial dysfunction
Myocardial ischemia and reperfusion
NEOMED College of Medicine
Protein cysteine sulfonation
Protein Structure
Zhang Liwen
Zweier Jay L