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Institution

Flinders University

EducationAdelaide, South Australia, Australia
About: Flinders University is a education organization based out in Adelaide, South Australia, Australia. It is known for research contribution in the topics: Population & Health care. The organization has 12033 authors who have published 32831 publications receiving 973172 citations. The organization is also known as: Flinders University of South Australia.


Papers
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Journal ArticleDOI
TL;DR: In this article, a questionnaire assessing amount of exercise, reasons for exercise, body satisfaction, and self-esteem was completed by 252 participants between the ages of 16 and 60 years.
Abstract: The study investigated the relationship between amount of exercise and psychological well-being in a broadly based sample. A questionnaire assessing amount of exercise, reasons for exercise, body satisfaction, and self-esteem was completed by 252 participants between the ages of 16 and 60 years. Almost all participants (>95%) were White. Participants were divided into four groups on the basis of gender and age, resulting in 70 young women, 48 young men, 73 mature women, and 61 mature men. Significant negative relationships between amount of exercise and body satisfaction and self-esteem were found for young women, and positive relationships for the remainder of the sample. Women exercised more for reasons of weight control, tone, and mood enhancement than men. For the whole sample, the first two of these reasons were associated with lower body satisfaction, while exercising for health and fitness reasons was associated with increased self-esteem. It was concluded that reasons for exercising did not provide an adequate explanation for the obtained difference in correlations across gender and age.

302 citations

Journal ArticleDOI
TL;DR: This review presents the current understanding of the alternative NAD(P)H dehydrogenases present in plant mitochondria and shows how this provides a mechanism for plants to remove excess reducing power and balance the redox poise of the cell.
Abstract: Plant mitochondria have a highly branched electron transport chain that provides great flexibility for oxidation of cytosolic and matrix NAD(P)H. In addition to the universal electron transport chain found in many organisms, plants have alternative NAD(P)H dehydrogenases in the first part of the chain and a second oxidase, the alternative oxidase, in the latter part. The alternative activities are nonproton pumping and allow for NAD(P)H oxidation with varying levels of energy conservation. This provides a mechanism for plants to, for example, remove excess reducing power and balance the redox poise of the cell. This review presents our current understanding of the alternative NAD(P)H dehydrogenases present in plant mitochondria.

302 citations

Journal ArticleDOI
TL;DR: It is concluded that nitric oxide synthase is located in a sub-population of enteric neurons, amongst which are inhibitory motor neurons that supply the circular muscle layer.

302 citations

Journal ArticleDOI
TL;DR: It is suggested that one physiological function of acetylcholinesterase may be to hydrolyse this neuropeptide, thus terminating its biological activity.

302 citations

Journal Article
TL;DR: A major role for P450IA2 in activation (N-hydroxylation) of aromatic amides and amines in human liver is suggested.
Abstract: The human P-450 CYP1A1 gene and a P450IA2 complementary DNA have been expressed in Cos-1 cells and the expressed proteins were assayed for their capacity to metabolize the carcinogens 2-acetylaminofluorene (AAF), benzo( a )pyrene, 2-amino-3-methylimidazo[4,5- f ]quinoline (IQ), 2-amino-3,4-dimethylimidazo[4,5- f ]quinoline, 2-amino-3,8-dimethylimidazo[4,5- f ]quinoxaline, 2-amino-3,4,8-trimethylimidazo[4,5- f ]quinoxaline, 2-amino-1-methyl-6-phenylimidazo[4,5- b ]pyridine (PhIP) was determined. The expressed human P450IA1 and P450IA2 proteins, when run on a 7.5% sodium dodecyl sulfate-polyacrylamide gel, migrated with different mobilities, with the former displaying the lower molecular weight. In human liver microsomes from 18 subjects, only a protein band corresponding to P450IA2 was detectable. Cos-1 cell-expressed P450IA1 and P450IA2 were capable of N -hydroxylating AAF and these activities were inhibited by α-naphthoflavone. In human liver microsomes, a correlation of r = 0.76 ( P n = 18) was obtained between AAF N -hydroxylase activity and P450IA2 content. AAF N -hydroxylase activity of human liver microsomes was also strongly inhibited by α-naphthoflavone. Except in the case of PhIP, where both proteins exhibited similar activities, P450IA2 was at least an order of magnitude more efficient than P450IA1 in activating IQ, 2-amino-3,4-dimethylimidazo[4,5- f ]quinoline, 2-amino-3,8-dimethylimidazo[4,5- f ]quinoxaline, and 2-amino-3,4,8-trimethylimidazo[4,5- f ]quinoxaline to mutagens as measured in the Ames test. Statistically significant correlations were obtained between IQ activation and P450IA2 content ( r = 0.75, r 2 = 0.56) and PhIP activation and P450IA2 content ( r = 0.71, r 2 = 0.5) in human liver microsomes. The activation of both IQ and PhIP by expressed proteins and human liver microsomes was strongly inhibited by α-naphthoflavone. The above data suggest a major role for P450IA2 in activation ( N -hydroxylation) of aromatic amides and amines in human liver. When benzo( a )pyrene hydroxylase activity was determined, only Cos-1 cell-expressed P450IA1 exhibited appreciable activity. While α-naphthoflavone inhibited Cos-1 cell-expressed P450IA1 benzo( a )pyrene hydroxylase activity, it caused a marked stimulation of this activity in human liver microsomes, which lack P450IA1 protein. The lack of a role for P450IA proteins in benzo( a )pyrene metabolism is further supported by the poor correlation ( r = 0.43, P > 0.05) between this activity and P450IA2 content of human liver microsomes. However, when P450IIIA3 content of the above human liver microsomes was determined by using the Western blot technique and correlated with benzo( a )pyrene metabolism, an r value of 0.70 ( P a )pyrene metabolism.

302 citations


Authors

Showing all 12221 results

NameH-indexPapersCitations
Matthew Jones125116196909
Robert Edwards12177574552
Justin C. McArthur11343347346
Peter Somogyi11223242450
Glenda M. Halliday11167653684
Jonathan C. Craig10887259401
Bruce Neal10856187213
Alan Cooper10874645772
Robert J. Norman10375545147
John B. Furness10359737668
Richard J. Miller10341935669
Michael J. Brownstein10227447929
Craig S. Anderson10165049331
John Chalmers9983155005
Kevin D. Hyde99138246113
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
202368
2022336
20212,761
20202,320
20191,943
20181,806