| 1. |
- Boniver, R, et al.
(author)
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Medico-legal in ORL
- 1988
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In: Acta Oto-Rhino-Laryngologica Belgica. - 0001-6497. ; 42:6, s. 722-771
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Journal article (peer-reviewed)
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| 3. |
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| 6. |
- Enbom, L, et al.
(author)
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Occlusal wear in miners.
- 1986
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In: Swedish Dental Journal. - 0347-9994. ; 10:5, s. 165-170
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Journal article (peer-reviewed)
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| 7. |
- Jacobsson, B, et al.
(author)
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Abnormality of adenylate cyclase regulation in human platelet membranes in renal insufficiency.
- 1985
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In: European journal of clinical investigation. - 0014-2972. ; 15:2, s. 75-81
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Journal article (peer-reviewed)abstract
- Adenylate cyclase in human platelets is under dual control of prostaglandins (PGI2 and PGE1) and catecholamines. The adenylate cyclase complex in membranes of platelets from ten patients with uraemia was investigated. The activation of the platelet cyclase by PGE1 is increased in the uraemic state, Vmax 4436 +/- 607 pmol cAMP mg-1 15 min-1. In the normal state Vmax is 2098 +/- 309 pmol cAMP mg-1 15 min-1. The alpha 2-adrenergic receptor was assayed with 3H-yohimbine binding. The density of receptors was equal in the uraemic (175 fmol mg-1 membrane protein) and the normal (170 fmol mg-1 membrane protein) states. Norepinephrine/3H-yohimbine competition binding revealed that catecholamines were bound with normal affinity in platelets in uraemia. Yet the inhibition of adenylate cyclase through the alpha 2-adrenergic receptor was diminished since Vmax values of adenylate cyclase with PGE1 and PGE2 + norepinephrine did not significantly differ. In the normal state, norepinephrine significantly (P less than 0.05) inhibited the PGE1 stimulated cyclase. It is concluded that platelet adenylate cyclase in the uraemia has an increased capacity for activation which is the result of both a sensitized stimulatory mechanism (prostaglandin mediated) and a deficient inhibitory mechanism (catecholamine mediated). It is suggested that a defect exists in the inhibitory nucleotide binding protein (NI) which is the coupling unit between the adenylate cyclase catalytic subunit (C).
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| 8. |
- Magnusson, M, et al.
(author)
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Clinical considerations concerning horizontal optokinetic nystagmus
- 1988
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In: Acta Oto-Laryngologica, Supplement. - 0365-5237. ; 455, s. 7-53
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Journal article (other academic/artistic)abstract
- During recent decades a vast amount of literature concerning horizontal optokinetic nystagmus has emerged, regarding which--and especially as regards our own work--this report is intended to consider the clinical value of optokinetic nystagmus.
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| 9. |
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| 10. |
- Magnusson, Yvonne, 1957, et al.
(author)
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Antigenic analysis of the second extra-cellular loop of the human beta-adrenergic receptors.
- 1989
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In: Clinical and experimental immunology. - 0009-9104. ; 78:1, s. 42-8
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Journal article (peer-reviewed)abstract
- Polyclonal antibodies were raised in rabbits by immunization with free peptides corresponding to positions 197-222 of the human beta 1-adrenergic receptor (beta 1 peptide) and the corresponding sequence (172-197) of the human beta 2-adrenergic receptor (beta 2 peptide). While the beta 2 peptide yielded antibodies that cross-reacted with the beta 1 peptide, the antibodies against the beta 1 peptide did not cross-react with the beta 2 sequence. Cross-reactivity of the anti-beta 2 peptide antibodies and the selectivity of the anti-beta 1 peptide antibodies were also revealed in the recognition by immunoblots of the beta 1- and beta 2-adrenergic receptors of different species or of the receptor gene products expressed in a bacterial vector. These antibodies could be used immunohistochemically to visualize the beta-adrenergic receptors on rabbit heart. The anti-beta 2 peptide antibodies did not show any functional effect on the beta-adrenergic receptors; the anti-beta 1 peptide antibodies were able to displace agonist affinity to higher values. Recognition of truncated peptides by the anti-beta 1 and anti-beta 2 peptide antibodies suggested that the cross-reaction of the anti-beta 2 peptide antibodies was due to the recognition of a common epitope on the C-terminal part of the peptides. The anti-beta 1 peptide antibodies recognized the N-terminal part of the peptide better than the C-terminal part. These results suggest that the second extracellular loop postulated in the structure of the human beta-adrenergic receptor contains the T and B cell epitopes necessary for induction of an immune response. The selectivity and the functional properties of the antibodies raised against that loop in the beta 1 adrenergic receptor could have relevance in induction of auto antibodies in certain cardiomyopathic conditions.
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