Institution
University of Aberdeen
Education•Aberdeen, United Kingdom•
About: University of Aberdeen is a education organization based out in Aberdeen, United Kingdom. It is known for research contribution in the topics: Population & Randomized controlled trial. The organization has 21174 authors who have published 49962 publications receiving 2105479 citations. The organization is also known as: Aberdeen University.
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06 Jan 2016
TL;DR: It is concluded that answering key questions on the relationship between Aβ and tau pathology should lead to a better understanding of the nature of secondary tauopathies, especially AD, and open new therapeutic targets and strategies.
Abstract: Abnormal deposition of misprocessed and aggregated proteins is a common final pathway of most neurodegenerative diseases, including Alzheimer's disease (AD). AD is characterized by the extraneuronal deposition of the amyloid β (Aβ) protein in the form of plaques and the intraneuronal aggregation of the microtubule-associated protein tau in the form of filaments. Based on the biochemically diverse range of pathological tau proteins, a number of approaches have been proposed to develop new potential therapeutics. Here we discuss some of the most promising ones: inhibition of tau phosphorylation, proteolysis and aggregation, promotion of intra- and extracellular tau clearance, and stabilization of microtubules. We also emphasize the need to achieve a full understanding of the biological roles and post-translational modifications of normal tau, as well as the molecular events responsible for selective neuronal vulnerability to tau pathology and its propagation. It is concluded that answering key questions on the relationship between Aβ and tau pathology should lead to a better understanding of the nature of secondary tauopathies, especially AD, and open new therapeutic targets and strategies.
492 citations
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TL;DR: Bandurski, R. S., Wilson, L. G. & Squires, G. S. (1956).
Abstract: Bandurski, R. S., Wilson, L. G. & Squires, G. L. (1956). J. Amer. chem. Soc. 78, 6408. Caputto, R., Leloir, L. F., Cardini, C. E. & Paladini, A. C. (1950). J. biol. Chem. 184, 333. Cohen, S. S. & Scott D. B. McNair (1950). Science, 111, 543. Cremer, H. D. & Tiselius, A. (1950). Biochem. Z. 320, 273. D'Abramo, F. &A Lipmann, F. (1957). Biochim. biophys. Acta, 25, 211. DeMeio, R. H. & Tkacz, L. (1950). Arch. Biochem. 27, 242. Gregory, J. D. & Nose, Y. (1957). Fed. Proc. 16, 189. Hanes, C. S. & Isherwood, F. A. (1949). Nature, Lond., 164, 1107. Hilz, H. & Lipmann, F. (1955). Proc. nat. Acad. Sci., Wash., 41, 880. Klemperer, H. (1955). D.Phil. Thesis: University of Oxford. Layton, L. L. & Frankel, D. R. (1951). Arch. Biochem. Biophy8. 31, 161. Loewi, G. & Kent, P. W. (1957). Biochem. J. 65, 550. Markham, R. & Smith, J. D. (1949). Biochem. J. 45, 294. Meyer, K. & Schwartz, D. E. (1950). Helv. chim. Acta, 33, 1651. Paladini, A. C. & Leloir, L. F. (1952). Biochem. J. 51, 426. Partridge, S. M. (1946). Nature, Lond., 158, 270. Partridge, S. M. (1949). Nature, Lond., i164, 443. Pasternak, C. A. & Kent, P. W. (1958). Biochem. J. 68, 452. Pasternak, C. A., Kent, P. W. & Davies, R. E. (1958). Biochem. J. 68, 212. Robbins, P. W. & Lipmann, F. (1956a). J. Amer. chem. Soc. 78, 2652. Robbins, P. W. & Lipmann, F. (1956b). J. Amer. chem. Soc. 78, 6409. Suzuki, S., Takahashi, N. & Egami, F. (1957). Biochim. biophy8. Acta, 24, 444. Werner, I. (1953). Upp8ala Ldkf6ren, F6rh. 58, 1. Williams, R. T. (1947). Detoxication Mechani8ms, p. 70. London: Chapman and Hall. Wilson, L. G. & Bandurski, R. S. (1956). Arch. Biochem. Biophys. 62, 503. Wyatt, G. R. (1951). Biochem. J. 48, 584.
492 citations
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TL;DR: This review summarizes current knowledge about the in vitro pharmacological properties of important CB1 and CB2 receptor ligands and pays particular attention to the binding properties of these ligands, to the efficacies of cannabinoid receptor agonists, as determined using cyclic AMP or [35S]GTPgammaS binding assays, and to selected examples of how these pharmacological Properties can be influenced by chemical structure.
Abstract: Mammalian tissues contain at least two types of cannabinoid receptor, CB 1 and CB 2 , both coupled to G proteins. CB 1 receptors are expressed mainly by neurones of the central and peripheral nervous system whereas CB 2 receptors occur in certain non-neuronal tissues, particularly in immune cells. The existence of endogenous ligands for cannabinoid receptors has also been demonstrated. The discovery of this 'endogenous cannabinoid system' has been paralleled by a renewed interest in possible therapeutic applications of cannabinoids, for example in the management of pain and in the suppression of muscle spasticity/spasm associated with multiple sclerosis or spinal cord injury. It has also prompted the development of a range of novel cannabinoid receptor ligands, including several that show marked selectivity for CB 1 or CB 2 receptors. This review summarizes current knowledge about the in vitro pharmacological properties of important CB 1 and CB 2 receptor ligands. Particular attention is paid to the binding properties of these ligands, to the efficacies of cannabinoid receptor agonists, as determined using cyclic AMP or [ 35 S]GTPγS binding assays, and to selected examples of how these pharmacological properties can be influenced by chemical structure. The in vitro pharmacological properties of ligands that can potently and selectively oppose the actions of CB 1 or CB 2 receptor agonists are also described. When administered by themselves, some of these ligands produce effects in certain tissue preparations that are opposite in direction to those produced by cannabinoid receptor agonists and the possibility that the ligands producing such 'inverse cannabimimetic effects' are inverse agonists rather than pure antagonists is discussed.
492 citations
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TL;DR: The discovery of the system of cannabinoid receptors and endocannabinoids that constitutes the "endocannabinoid system" has prompted the development of CB(1)- and CB(2)-selective agonists and antagonists/inverse agonists.
Abstract: There are at least two types of cannabinoid receptors, CB(1) and CB(2), both coupled to G proteins. CB(1) receptors exist primarily on central and peripheral neurons, one of their functions being to modulate neurotransmitter release. CB(2) receptors are present mainly on immune cells. Their roles are proving more difficult to establish but seem to include the modulation of cytokine release. Endogenous agonists for cannabinoid receptors (endocannabinoids) have also been discovered, the most important being arachidonoyl ethanolamide (anandamide), 2-arachidonoyl glycerol and 2-arachidonyl glyceryl ether. Other endocannabinoids and cannabinoid receptor types may also exist. Although anandamide can act through CB(1) and CB(2) receptors, it is also a vanilloid receptor agonist and some of its metabolites may possess yet other important modes of action. The discovery of the system of cannabinoid receptors and endocannabinoids that constitutes the "endocannabinoid system" has prompted the development of CB(1)- and CB(2)-selective agonists and antagonists/inverse agonists. CB(1)/CB(2) agonists are already used clinically, as anti-emetics or to stimulate appetite. Potential therapeutic uses of cannabinoid receptor agonists include the management of multiple sclerosis/spinal cord injury, pain, inflammatory disorders, glaucoma, bronchial asthma, vasodilation that accompanies advanced cirrhosis, and cancer. Following their release onto cannabinoid receptors, endocannabinoids are removed from the extracellular space by membrane transport and then degraded by intracellular enzymic hydrolysis. Inhibitors of both these processes have been developed. Such inhibitors have therapeutic potential as animal data suggest that released endocannabinoids mediate reductions both in inflammatory pain and in the spasticity and tremor of multiple sclerosis. So too have CB(1) receptor antagonists, for example for the suppression of appetite and the management of cognitive dysfunction or schizophrenia.
491 citations
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Brigham and Women's Hospital1, Houston Methodist Hospital2, University of Colorado Denver3, Memorial Sloan Kettering Cancer Center4, College of American Pathologists5, University of Pittsburgh6, University of Aberdeen7, Temple University8, Roswell Park Cancer Institute9, Peter MacCallum Cancer Centre10, University Health Network11
TL;DR: The 2013 guideline was largely reaffirmed with updated recommendations to allow testing of cytology samples, require improved assay sensitivity, and recommend against the use of immunohistochemistry for EGFR testing.
Abstract: Context.— In 2013, an evidence-based guideline was published by the College of American Pathologists, the International Association for the Study of Lung Cancer, and the Association for Molecular P...
491 citations
Authors
Showing all 21424 results
Name | H-index | Papers | Citations |
---|---|---|---|
Paul M. Thompson | 183 | 2271 | 146736 |
Feng Zhang | 172 | 1278 | 181865 |
Ian J. Deary | 166 | 1795 | 114161 |
Peter A. R. Ade | 162 | 1387 | 138051 |
David W. Johnson | 160 | 2714 | 140778 |
Pete Smith | 156 | 2464 | 138819 |
Naveed Sattar | 155 | 1326 | 116368 |
John R. Hodges | 149 | 812 | 82709 |
Ruth J. F. Loos | 142 | 647 | 92485 |
Alan J. Silman | 141 | 708 | 92864 |
Michael J. Keating | 140 | 1169 | 76353 |
David Price | 138 | 1687 | 93535 |
John D. Scott | 135 | 625 | 83878 |
Aarno Palotie | 129 | 711 | 89975 |
Rajat Gupta | 126 | 1240 | 72881 |