1
40
10
-
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
Articles Published in 2021
Creator
An entity primarily responsible for making the resource
Shelley Harrell
Publisher
An entity responsible for making the resource available
Shelley Harrell
Date
A point or period of time associated with an event in the lifecycle of the resource
2021
Description
An account of the resource
Items published in 2021
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
<table width="91" style="border-collapse:collapse;width:68pt;"><colgroup><col width="91" style="width:68pt;" /></colgroup><tbody><tr style="height:15pt;"><td width="91" height="20" class="xl18" style="width:68pt;height:15pt;"><a href="http://doi.org/10.1016/j.yjmcc.2021.07.008">http://doi.org/10.1016/j.yjmcc.2021.07.008</a></td>
</tr></tbody></table>
NEOMED College
NEOMED College of Medicine
NEOMED Department
Department of Integrative Medical Sciences
Update Year & Number
Jan to Aug list 2021
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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Reperfusion mediates heme impairment with increased protein cysteine sulfonation of mitochondrial complex III in the post-ischemic heart.
Creator
An entity primarily responsible for making the resource
Chen C; Kang PT; Zhang L; Xiao K; Zweier JL; Chilian WM; Chen Y-R
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
2021
2021-08-10
Description
An account of the resource
A serious consequence of myocardial ischemia-reperfusion injury (I/R) is oxidative damage, which causes mitochondrial dysfunction. The cascading ROS can propagate and potentially induce heme bleaching and protein cysteine sulfonation (PrSO3H) of the mitochondrial electron transport chain. Herein we studied the mechanism of I/R-mediated irreversible oxidative injury of complex III in mitochondria from rat hearts subjected to 30-min of ischemia and 24-h of reperfusion in vivo. In the I/R region, the catalytic activity of complex III was significantly impaired. Spectroscopic analysis indicated that I/R mediated the destruction of hemes b and c + c1 in the mitochondria, supporting I/R-mediated complex III impairment. However, no significant impairment of complex III activity and heme damage were observed in mitochondria from the risk region of rat hearts subjected only to 30-min ischemia, despite a decreased state 3 respiration. In the I/R mitochondria, carbamidomethylated C122/C125 of cytochrome c1 via alkylating complex III with a down regulation of HCCS was exclusively detected, supporting I/R-mediated thioether defect of heme c1. LC-MS/MS analysis showed that I/R mitochondria had intensely increased complex III PrSO3H levels at the C236 ligand of the [2Fesingle bond2S] cluster of the Rieske iron‑sulfur protein (uqcrfs1), thus impairing the electron transport activity. MS analysis also indicated increased PrSO3H of the hinge protein at C65 and of cytochrome c1 at C140 and C220, which are confined in the intermembrane space. MS analysis also showed that I/R extensively enhanced the PrSO3H of the core 1 (uqcrc1) and core 2 (uqcrc2) subunits in the matrix compartment, thus supporting the conclusion that complex III releases ROS to both sides of the inner membrane during reperfusion. Analysis of ischemic mitochondria indicated a modest reduction from the basal level of complex III PrSO3H detected in the mitochondria of sham control hearts, suggesting that the physiologic hyperoxygenation and ROS overproduction during reperfusion mediated the enhancement of complex III PrSO3H. In conclusion, reperfusion-mediated heme damage with increased PrSO3H controls oxidative injury to complex III and aggravates mitochondrial dysfunction in the post-ischemic heart.
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<table width="91" style="border-collapse:collapse;width:68pt;"><colgroup><col width="91" style="width:68pt;" /></colgroup><tbody><tr style="height:15pt;"><td width="91" height="20" class="xl18" style="width:68pt;height:15pt;"><a href="http://doi.org/10.1016/j.yjmcc.2021.07.008">http://doi.org/10.1016/j.yjmcc.2021.07.008</a></td>
</tr></tbody></table>
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© 2021 Elsevier Ltd. All rights reserved.
Format
The file format, physical medium, or dimensions of the resource
Journal Article
2021
Complex III
Cysteine sulfonation
Heme damage
Myocardial ischemia and reperfusion
Oxidative Stress
Protein Structure
-
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.2021.07.008" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.yjmcc.2021.07.008</a>
ISSN
1095-8584
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/10.1016/j.yjmcc.2021.07.008" target="_blank" rel="noreferrer noopener">NEOMED Full-text Holding (if available) - Proxy DOI: 10.1016/j.yjmcc.2021.07.008</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
August 2021 List
NEOMED College
NEOMED College of Medicine
NEOMED Department
Department of Integrative Medical 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
A name given to the resource
Reperfusion mediates heme impairment with increased protein cysteine sulfonation of mitochondrial complex III in the post-ischemic heart.
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
2021
2021-07-28
Subject
The topic of the resource
Complex III; Cysteine sulfonation; Heme damage; Myocardial ischemia and reperfusion; Oxidative stress; Protein structure
Creator
An entity primarily responsible for making the resource
Chen C; Kang PT; Zhang L; Xiao K; Zweier JL; Chilian WM; Chen Y-R
Description
An account of the resource
A serious consequence of myocardial ischemia-reperfusion injury (I/R) is oxidative damage, which causes mitochondrial dysfunction. The cascading ROS can propagate and potentially induce heme bleaching and protein cysteine sulfonation (PrSO 3 H) of the mitochondrial electron transport chain. Herein we studied the mechanism of I/R-mediated irreversible oxidative injury of complex III in mitochondria from rat hearts subjected to 30-min of ischemia and 24-h of reperfusion in vivo. In the I/R region, the catalytic activity of complex III was significantly impaired. Spectroscopic analysis indicated that I/R mediated the destruction of hemes b and c + c 1 in the mitochondria, supporting I/R-mediated complex III impairment. However, no significant impairment of complex III activity and heme damage were observed in mitochondria from the risk region of rat hearts subjected only to 30-min ischemia, despite a decreased state 3 respiration. In the I/R mitochondria, carbamidomethylated C 122 /C 125 of cytochrome c 1 via alkylating complex III with a down regulation of HCCS was exclusively detected, supporting I/R-mediated thioether defect of heme c 1 . LC-MS/MS analysis showed that I/R mitochondria had intensely increased complex III PrSO 3 H levels at the C 236 ligand of the [2Fe2S] cluster of the Rieske iron‑sulfur protein (uqcrfs1), thus impairing the electron transport activity. MS analysis also indicated increased PrSO 3 H of the hinge protein at C 65 and of cytochrome c 1 at C 140 and C 220 , which are confined in the intermembrane space. MS analysis also showed that I/R extensively enhanced the PrSO 3 H of the core 1 (uqcrc1) and core 2 (uqcrc2) subunits in the matrix compartment, thus supporting the conclusion that complex III releases ROS to both sides of the inner membrane during reperfusion. Analysis of ischemic mitochondria indicated a modest reduction from the basal level of complex III PrSO 3 H detected in the mitochondria of sham control hearts, suggesting that the physiologic hyperoxygenation and ROS overproduction during reperfusion mediated the enhancement of complex III PrSO 3 H. In conclusion, reperfusion-mediated heme damage with increased PrSO 3 H controls oxidative injury to complex III and aggravates mitochondrial dysfunction in the post-ischemic heart. (Copyright © 2018. Published by Elsevier Ltd.)
Identifier
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<a href="http://doi.org/10.1016/j.yjmcc.2021.07.008" target="_blank" rel="noreferrer noopener">10.1016/j.yjmcc.2021.07.008</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).
Format
The file format, physical medium, or dimensions of the resource
journalArticle
2021
August 2021 List
Chen C
Chen Y-R
Chilian WM
Complex III
Cysteine sulfonation
Department of Integrative Medical Sciences
Heme damage
Journal of molecular and cellular cardiology
journalArticle
Kang PT
Myocardial ischemia and reperfusion
NEOMED College of Medicine
Oxidative Stress
Protein Structure
Xiao K
Zhang L
Zweier JL
-
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.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
-
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.bmcl.2018.03.061" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.bmcl.2018.03.061</a>
Pages
1937–1942
Issue
10
Volume
28
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
Novel compounds that target lipoprotein lipase and mediate growth arrest in acute lymphoblastic leukemia.
Publisher
An entity responsible for making the resource available
Bioorganic & medicinal chemistry letters
Date
A point or period of time associated with an event in the lifecycle of the resource
2018
2018-06
Subject
The topic of the resource
*Acute lymphoblastic leukemia; *Cancer; *Co-culture model; *Lipids; *Lipoprotein lipase; *Metabolism; Amides/chemistry/metabolism/pharmacology; Antineoplastic Agents/*chemistry/metabolism/pharmacology; Binding Sites; Cell Line; Cell Proliferation/drug effects; Coculture Techniques; Dyslipidemias/complications/metabolism/pathology; Humans; Lipoprotein Lipase/antagonists & inhibitors/*metabolism; Mesenchymal Stem Cells/cytology/metabolism; Molecular Docking Simulation; Precursor Cell Lymphoblastic Leukemia-Lymphoma/complications/metabolism/pathology; Protein Binding; Protein Structure; Serum Albumin/chemistry/metabolism; Tertiary; Tumor
Creator
An entity primarily responsible for making the resource
Nair Rajesh R; Geldenhuys Werner J; Piktel Debbie; Sadana Prabodh; Gibson Laura F
Description
An account of the resource
Over the past decade, the therapeutic strategies employed to treat B-precursor acute lymphoblastic leukemia (ALL) have been progressively successful in treating the disease. Unfortunately, the treatment associated dyslipidemia, either acute or chronic, is very prevalent and a cause for decreased quality of life in the surviving patients. To overcome this hurdle, we tested a series of cylopropanecarboxamides, a family demonstrated to target lipid metabolism, for their anti-leukemic activity in ALL. Several of the compounds tested showed anti-proliferative activity, with one, compound 22, inhibiting both Philadelphia chromosome negative REH and Philadelphia chromosome positive SupB15 ALL cell division. The novel advantage of these compounds is the potential synergy with standard chemotherapeutic agents, while concomitantly blunting the emergence of dyslipidemia. Thus, the cylopropanecarboxamides represent a novel class of compounds that can be potentially used in combination with the present standard-of-care to limit treatment associated dyslipidemia in ALL patients.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.bmcl.2018.03.061" target="_blank" rel="noreferrer noopener">10.1016/j.bmcl.2018.03.061</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).
*Acute lymphoblastic leukemia
*Cancer
*Co-culture model
*Lipids
*Lipoprotein lipase
*Metabolism
2018
Amides/chemistry/metabolism/pharmacology
Antineoplastic Agents/*chemistry/metabolism/pharmacology
Binding Sites
Bioorganic & medicinal chemistry letters
Cell Line
Cell Proliferation/drug effects
Coculture Techniques
Department of Pharmaceutical Sciences
Department of Pharmacy Practice
Dyslipidemias/complications/metabolism/pathology
Geldenhuys Werner J
Gibson Laura F
Humans
Lipoprotein Lipase/antagonists & inhibitors/*metabolism
Mesenchymal Stem Cells/cytology/metabolism
Molecular Docking Simulation
Nair Rajesh R
NEOMED College of Graduate Studies
NEOMED College of Pharmacy
Piktel Debbie
Precursor Cell Lymphoblastic Leukemia-Lymphoma/complications/metabolism/pathology
Protein Binding
Protein Structure
Sadana Prabodh
Serum Albumin/chemistry/metabolism
Tertiary
Tumor
-
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.bmcl.2013.01.069" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.bmcl.2013.01.069</a>
Pages
1707–1711
Issue
6
Volume
23
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
3D-QSAR and docking studies of pentacycloundecylamines at the sigma-1 (sigma1) receptor.
Publisher
An entity responsible for making the resource available
Bioorganic & medicinal chemistry letters
Date
A point or period of time associated with an event in the lifecycle of the resource
2013
2013-03
Subject
The topic of the resource
*Quantitative Structure-Activity Relationship; Amines/*chemistry/metabolism; Aza Compounds/chemistry; Binding Sites; Kinetics; Molecular Docking Simulation; Protein Binding; Protein Structure; Receptors; sigma/*chemistry/metabolism; Tertiary
Creator
An entity primarily responsible for making the resource
Geldenhuys Werner J; Novotny Nicholas; Malan Sarel F; Van der Schyf Cornelis J
Description
An account of the resource
Pentacycloundecylamine (PCU) derived compounds have been shown to be promising lead structures for the development of novel drug candidates aimed at a variety of neurodegenerative and psychiatric diseases. Here we show for the first time a 3D quantitative structure-activity relationship (3D-QSAR) for a series of aza-PCU-derived compounds with activity at the sigma-1 (sigma1) receptor. A comparative molecular field analysis (CoMFA) model was developed with a partial least squares cross validated (q(2)) regression value of 0.6, and a non-cross validated r(2) of 0.9. The CoMFA model was effective at predicting the sigma-1 activities of a test set with an r(2) \textgreater0.7. We also describe here the docking of the PCU-derived compounds into a homology model of the sigma-1 (sigma1) receptor, which was developed to gain insight into binding of these cage compounds to the receptor. Based on docking studies we evaluated in a [(3)H]pentazocine binding assay an oxa-PCU, NGP1-01 (IC50=1.78muM) and its phenethyl derivative (IC50=1.54muM). Results from these studies can be used to develop new compounds with specific affinity for the sigma-1(sigma1) receptor.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.bmcl.2013.01.069" target="_blank" rel="noreferrer noopener">10.1016/j.bmcl.2013.01.069</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).
*Quantitative Structure-Activity Relationship
2013
Amines/*chemistry/metabolism
Aza Compounds/chemistry
Binding Sites
Bioorganic & medicinal chemistry letters
Geldenhuys Werner J
Kinetics
Malan Sarel F
Molecular Docking Simulation
Novotny Nicholas
Protein Binding
Protein Structure
Receptors
sigma/*chemistry/metabolism
Tertiary
Van der Schyf Cornelis J
-
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.bmcl.2012.09.056" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.bmcl.2012.09.056</a>
Pages
7183–7188
Issue
23
Volume
22
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
Inhibition of monoamine oxidase by derivatives of piperine, an alkaloid from the pepper plant Piper nigrum, for possible use in Parkinson's disease.
Publisher
An entity responsible for making the resource available
Bioorganic & medicinal chemistry letters
Date
A point or period of time associated with an event in the lifecycle of the resource
2012
2012-12
Subject
The topic of the resource
Alkaloids/*chemistry/isolation & purification/pharmacology; Animals; Benzodioxoles/*chemistry/isolation & purification/pharmacology; Binding Sites; Blood-Brain Barrier/drug effects; Bovine/metabolism; Cattle; Humans; Hydrogen Bonding; Molecular Docking Simulation; Monoamine Oxidase Inhibitors/*chemistry/isolation & purification/pharmacology; Monoamine Oxidase/*chemistry/metabolism; Parkinson Disease/metabolism/pathology; Piper nigrum/*chemistry; Piperidines/*chemistry/isolation & purification/pharmacology; Polyunsaturated Alkamides/*chemistry/isolation & purification/pharmacology; Protein Binding; Protein Structure; Serum Albumin; Tertiary
Creator
An entity primarily responsible for making the resource
Al-Baghdadi Osamah B; Prater Natalie I; Van der Schyf Cornelis J; Geldenhuys Werner J
Description
An account of the resource
A series of compounds related to piperine and antiepilepsirine was screened in a monoamine oxidase A and B assay. Piperine is an alkaloid from the source plant of both black and white pepper grains, Piper nigrum. Piperine has been shown to have a wide range of activity, including MAO inhibitory activity. The z-factor for the screening assay was found to be greater than 0.8 for both assays. Notably, the compounds tested were selective towards MAO-B, with the most potent compound having an IC(50) of 498 nM. To estimate blood-brain barrier (BBB) permeability, we used a PAMPA assay, which suggested that the compounds are likely to penetrate the BBB. A fluorescent bovine serum albumin (BSA) high-throughput screening (HTS) binding assay showed an affinity of 8 muM for piperine, with more modest binding for other test compounds. Taken together, the data described here may be useful in gaining insight towards the design of selective MAO-B inhibitory compounds devoid of MAO-A activity.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.bmcl.2012.09.056" target="_blank" rel="noreferrer noopener">10.1016/j.bmcl.2012.09.056</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).
2012
Al-Baghdadi Osamah B
Alkaloids/*chemistry/isolation & purification/pharmacology
Animals
Benzodioxoles/*chemistry/isolation & purification/pharmacology
Binding Sites
Bioorganic & medicinal chemistry letters
Blood-Brain Barrier/drug effects
Bovine/metabolism
Cattle
Geldenhuys Werner J
Humans
Hydrogen Bonding
Molecular Docking Simulation
Monoamine Oxidase Inhibitors/*chemistry/isolation & purification/pharmacology
Monoamine Oxidase/*chemistry/metabolism
Parkinson Disease/metabolism/pathology
Piper nigrum/*chemistry
Piperidines/*chemistry/isolation & purification/pharmacology
Polyunsaturated Alkamides/*chemistry/isolation & purification/pharmacology
Prater Natalie I
Protein Binding
Protein Structure
Serum Albumin
Tertiary
Van der Schyf Cornelis J
-
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.bmcl.2011.10.014" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.bmcl.2011.10.014</a>
Pages
7405–7411
Issue
24
Volume
21
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
3D-Quantitative structure-activity relationship and docking studies of the tachykinin NK3 receptor.
Publisher
An entity responsible for making the resource available
Bioorganic & medicinal chemistry letters
Date
A point or period of time associated with an event in the lifecycle of the resource
2011
2011-12
Subject
The topic of the resource
*Quantitative Structure-Activity Relationship; Binding Sites; Computer Simulation; Drug Design; Humans; Ligands; Models; Molecular; Neurokinin-3/*chemistry/metabolism; Protein Structure; Quinolines/chemistry; Receptors; Tertiary
Creator
An entity primarily responsible for making the resource
Geldenhuys Werner J; Simmons Mark A
Description
An account of the resource
The tachykinin NK(3) receptor (NK(3)R) is a novel drug target for schizophrenia and drug abuse. Since few non-peptide antagonists of this G protein-coupled receptor are available, we have initiated this study to gain a better understanding of the structure-activity relationships of NK(3) antagonist compounds. We developed a 3D comparative molecular similarity index analysis (CoMSIA) model that gave cross-validated PLS values with q(2) \textgreater0.5 which were validated using a test set. We also describe the development of a homology model of the NK(3)R. The model was then used to develop a pharmacophore for docked ligands. This pharmacophore showed two aromatic, two hydrogen donor and one acceptor/aromatic points. These data will be useful for future structure-based drug discovery of ligands for the NK(3)R.
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<a href="http://doi.org/10.1016/j.bmcl.2011.10.014" target="_blank" rel="noreferrer noopener">10.1016/j.bmcl.2011.10.014</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).
*Quantitative Structure-Activity Relationship
2011
Binding Sites
Bioorganic & medicinal chemistry letters
Computer Simulation
Drug Design
Geldenhuys Werner J
Humans
Ligands
Models
Molecular
Neurokinin-3/*chemistry/metabolism
Protein Structure
Quinolines/chemistry
Receptors
Simmons Mark A
Tertiary
-
Text
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URL Address
<a href="http://doi.org/10.1016/j.bmcl.2009.12.088" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.bmcl.2009.12.088</a>
Pages
819–823
Issue
3
Volume
20
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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Structure-based design of a thiazolidinedione which targets the mitochondrial protein mitoNEET.
Publisher
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Bioorganic & medicinal chemistry letters
Date
A point or period of time associated with an event in the lifecycle of the resource
2010
2010-02
Subject
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*Drug Design; Animals; Binding Sites/drug effects/physiology; Dose-Response Relationship; Drug; Drug Delivery Systems/*methods; Liver/drug effects/metabolism; Mitochondria; Mitochondrial Proteins/*metabolism; Protein Structure; Rats; Secondary; Structure-Activity Relationship; Thiazolidinediones/administration & dosage/*chemical synthesis/*metabolism
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Geldenhuys Werner J; Funk Max O; Barnes Kendra F; Carroll Richard T
Description
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Several PPAR-gamma agonists containing a thiazolidinedione moiety (referred to as glitazones) have been proposed to be neuroprotective and appear to alter mitochondrial function. Recently, a search for mitochondrial proteins that bind pioglitazone identified a novel protein, mitoNEET, which was later shown to regulate the oxidative capacity of the mitochondria. This identified an alternative target for the glitazones suggesting a possible new drug target for the treatment of neurodegenerative diseases. Molecular docking studies employing the reported crystal structure revealed five possible binding pockets on mitoNEET. We focused on two sites based on their physical characteristics. Using binding information gained from the analysis of two glitazones docked in these pockets, we designed and synthesized a ligand (NL-1) that would preferentially bind to site 1. Based on [(3)H]-binding data of the glitazones and comparisons to computer generated K(i)s, we were able to predict that site 1 was likely the target of the glitazones. NL-1 uncoupled isolated mitochondrial complex I respiration with an IC(50) of 2.4 microM and inhibited state III respiration up to 45%. To investigate the ability of NL-1 to block rotenone initiated free radicals from complex I, we found it was able to protect the human neuronal cell line SH-SY5Y against rotenone induced cell death. These data demonstrate that mitoNEET is a viable target for the design and synthesis of novel therapeutic agents aimed at altering mitochondrial function.
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<a href="http://doi.org/10.1016/j.bmcl.2009.12.088" target="_blank" rel="noreferrer noopener">10.1016/j.bmcl.2009.12.088</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).
*Drug Design
2010
Animals
Barnes Kendra F
Binding Sites/drug effects/physiology
Bioorganic & medicinal chemistry letters
Carroll Richard T
Dose-Response Relationship
Drug
Drug Delivery Systems/*methods
Funk Max O
Geldenhuys Werner J
Liver/drug effects/metabolism
Mitochondria
Mitochondrial Proteins/*metabolism
Protein Structure
Rats
Secondary
Structure-Activity Relationship
Thiazolidinediones/administration & dosage/*chemical synthesis/*metabolism
-
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
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Design and use of peptide-based antibodies decreasing superoxide production by mitochondrial complex I and complex II.
Publisher
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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
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Kang Patrick T; Yun June; Kaumaya Pravin P T; Chen Yeong-Renn
Description
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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
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<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