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/10.1074/jbc.M513420200" target="_blank" rel="noreferrer noopener">http://doi.org/10.1074/jbc.M513420200</a>
Pages
10081–10088
Issue
15
Volume
281
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
A Prospero-related homeodomain protein is a novel co-regulator of hepatocyte nuclear factor 4alpha that regulates the cholesterol 7alpha-hydroxylase gene.
Publisher
An entity responsible for making the resource available
The Journal of biological chemistry
Date
A point or period of time associated with an event in the lifecycle of the resource
2006
2006-04
Subject
The topic of the resource
*Gene Expression Regulation; Aged; Amino Acid Motifs; Bile Acids and Salts/metabolism; Cell Line; Cell Nucleus/metabolism; Cells; Cholesterol 7-alpha-Hydroxylase/*chemistry/*genetics; Cultured/metabolism; Enzymologic; Female; Genes; Genetic; Gluconeogenesis; Glutathione Transferase/metabolism; Hepatocyte Nuclear Factor 4/metabolism/*physiology; Hepatocytes/metabolism; Homeodomain Proteins/metabolism/*physiology; Humans; Immunoprecipitation; Liver/metabolism; Luciferases/metabolism; Male; Messenger/metabolism; Middle Aged; Phosphoenolpyruvate Carboxykinase (ATP)/metabolism; Plasmids/metabolism; Protein Structure; Reporter; Response Elements; Reverse Transcriptase Polymerase Chain Reaction; RNA; Small Interfering/metabolism; Tertiary; Time Factors; Transcription; Transcriptional Activation; Transfection; Tumor Suppressor Proteins; Two-Hybrid System Techniques
Creator
An entity primarily responsible for making the resource
Song Kwang-Hoon; Li Tiangang; Chiang John Y L
Description
An account of the resource
Prox1, an early specific marker for developing liver and pancreas in foregut endoderm has recently been shown to interact with alpha-fetoprotein transcription factor and repress cholesterol 7alpha-hydroxylase (CYP7A1) gene transcription. Using a yeast two-hybrid assay, we found that Prox1 strongly and specifically interacted with hepatocyte nuclear factor (HNF)4alpha, an important transactivator of the human CYP7A1 gene in bile acid synthesis and phosphoenolpyruvate carboxykinase (PEPCK) gene in gluconeogenesis. A real time PCR assay detected Prox1 mRNA expression in human primary hepatocytes and HepG2 cells. Reporter assay, GST pull-down, co-immunoprecipitation, and yeast two-hybrid assays identified a specific interaction between the N-terminal LXXLL motif of Prox1 and the activation function 2 domain of HNF4alpha. Prox1 strongly inhibited HNF4alpha and peroxisome proliferators-activated receptor gamma coactivator-1alpha co-activation of the CYP7A1 and PEPCK genes. Knock down of the endogenous Prox1 by small interfering RNA resulted in significant increase of CYP7A1 and PEPCK mRNA expression and the rate of bile acid synthesis in HepG2 cells. These results suggest that Prox1 is a novel co-regulator of HNF4alpha that may play a key role in the regulation of bile acid synthesis and gluconeogenesis in the liver.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1074/jbc.M513420200" target="_blank" rel="noreferrer noopener">10.1074/jbc.M513420200</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).
*Gene Expression Regulation
2006
Aged
Amino Acid Motifs
Bile Acids and Salts/metabolism
Cell Line
Cell Nucleus/metabolism
Cells
Chiang John Y L
Cholesterol 7-alpha-Hydroxylase/*chemistry/*genetics
Cultured/metabolism
Department of Integrative Medical Sciences
Enzymologic
Female
Genes
Genetic
Gluconeogenesis
Glutathione Transferase/metabolism
Hepatocyte Nuclear Factor 4/metabolism/*physiology
Hepatocytes/metabolism
Homeodomain Proteins/metabolism/*physiology
Humans
Immunoprecipitation
Li Tiangang
Liver/metabolism
Luciferases/metabolism
Male
Messenger/metabolism
Middle Aged
NEOMED College of Medicine
Phosphoenolpyruvate Carboxykinase (ATP)/metabolism
Plasmids/metabolism
Protein Structure
Reporter
Response Elements
Reverse Transcriptase Polymerase Chain Reaction
RNA
Small Interfering/metabolism
Song Kwang-Hoon
Tertiary
The Journal of biological chemistry
Time Factors
Transcription
Transcriptional Activation
Transfection
Tumor Suppressor Proteins
Two-Hybrid System Techniques
-
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>
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).
*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/10.1002/bip.21457" target="_blank" rel="noreferrer noopener">http://doi.org/10.1002/bip.21457</a>
Pages
207–221
Issue
2
Volume
96
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
Design and use of peptide-based antibodies decreasing superoxide production by mitochondrial complex I and complex II.
Publisher
An entity responsible for making the resource available
Biopolymers
Date
A point or period of time associated with an event in the lifecycle of the resource
2011
1905-7
Subject
The topic of the resource
*Electron Transport Complex I/antagonists & inhibitors/chemistry/immunology/metabolism; *Electron Transport Complex II/antagonists & inhibitors/chemistry/immunology/metabolism; *Mitochondria; *Mitochondrial Proteins/antagonists & inhibitors/chemistry/immunology/metabolism; *Peptides/chemistry/immunology/metabolism; Amino Acid Motifs; Animals; Cattle; Female; Heart/chemistry/immunology/metabolism; Protein Structure; Rabbits; Tertiary
Creator
An entity primarily responsible for making the resource
Kang Patrick T; Yun June; Kaumaya Pravin P T; Chen Yeong-Renn
Description
An account of the resource
Mitochondria are the major source of reactive oxygen species. Both complex I and complex II mediate O2*- production in mitochondria and host reactive protein thiols. To explore the functions of the specific domains involved in the redox modifications of complexes I and II, various peptide-based antibodies were generated against these complexes, and their inhibitory effects were subsequently measured. The redox domains involved in S-glutathionylation and nitration, as well as the binding 2011. motif of the iron-sulfur cluster (N1a) of the complexes I and II were utilized to design B-cell epitopes for generating antibodies. The effect of antibody binding on enzyme-mediated O2*- generation was measured by EPR spin trapping. Binding of either antibody AbGSCA206 or AbGSCB367 against glutathione (GS)-binding domain to complex I inhibit its O2*- generation, but does not affect electron transfer efficiency. Binding of antibody (Ab24N1a) against the binding motif of N1a to complex I modestly suppresses both O2*- generation and electron transfer efficiency. Binding of either antibody Ab75 or Ab24 against nonredox domain decreases electron leakage production. In complex II, binding of antibody AbGSC90 against GS-binding domain to complex II marginally decreases both O2*- generation and electron transfer activity. Binding of antibody AbY142 to complex II against the nitrated domain modestly inhibits electron leakage, but does not affect the electron transfer activity of complex II. In conclusion, mediation of O2*- generation by complexes I and II can be regulated by specific redox and nonredox domains.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1002/bip.21457" target="_blank" rel="noreferrer noopener">10.1002/bip.21457</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).
*Electron Transport Complex I/antagonists & inhibitors/chemistry/immunology/metabolism
*Electron Transport Complex II/antagonists & inhibitors/chemistry/immunology/metabolism
*Mitochondria
*Mitochondrial Proteins/antagonists & inhibitors/chemistry/immunology/metabolism
*Peptides/chemistry/immunology/metabolism
2011
Amino Acid Motifs
Animals
Biopolymers
Cattle
Chen Yeong-Renn
Department of Integrative Medical Sciences
Female
Heart/chemistry/immunology/metabolism
Kang Patrick T
Kaumaya Pravin P T
NEOMED College of Medicine
Protein Structure
Rabbits
Tertiary
Yun June