Genetic alterations of the BR12 Gene: familial British and Danish dementias.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Standard

Genetic alterations of the BR12 Gene: familial British and Danish dementias. / Ghiso, J.; Rostagno, A.; Tomidokoro, Y.; Lashley, T.; Bojsen-Møller, Marie; Brændgaard, Hans; Plant, G.; Holton, J.; Lal, R.; Revesz, T.; Frangione, B.

I: Brain Pathology, Bind 16, Nr. 1, 2006, s. 71-9.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Ghiso, J, Rostagno, A, Tomidokoro, Y, Lashley, T, Bojsen-Møller, M, Brændgaard, H, Plant, G, Holton, J, Lal, R, Revesz, T & Frangione, B 2006, 'Genetic alterations of the BR12 Gene: familial British and Danish dementias.', Brain Pathology, bind 16, nr. 1, s. 71-9.

APA

Ghiso, J., Rostagno, A., Tomidokoro, Y., Lashley, T., Bojsen-Møller, M., Brændgaard, H., Plant, G., Holton, J., Lal, R., Revesz, T., & Frangione, B. (2006). Genetic alterations of the BR12 Gene: familial British and Danish dementias. Brain Pathology, 16(1), 71-9.

CBE

Ghiso J, Rostagno A, Tomidokoro Y, Lashley T, Bojsen-Møller M, Brændgaard H, Plant G, Holton J, Lal R, Revesz T, Frangione B. 2006. Genetic alterations of the BR12 Gene: familial British and Danish dementias. Brain Pathology. 16(1):71-9.

MLA

Ghiso, J. o.a.. "Genetic alterations of the BR12 Gene: familial British and Danish dementias.". Brain Pathology. 2006, 16(1). 71-9.

Vancouver

Ghiso J, Rostagno A, Tomidokoro Y, Lashley T, Bojsen-Møller M, Brændgaard H o.a. Genetic alterations of the BR12 Gene: familial British and Danish dementias. Brain Pathology. 2006;16(1):71-9.

Author

Ghiso, J. ; Rostagno, A. ; Tomidokoro, Y. ; Lashley, T. ; Bojsen-Møller, Marie ; Brændgaard, Hans ; Plant, G. ; Holton, J. ; Lal, R. ; Revesz, T. ; Frangione, B. / Genetic alterations of the BR12 Gene: familial British and Danish dementias. I: Brain Pathology. 2006 ; Bind 16, Nr. 1. s. 71-9.

Bibtex

@article{e99e4460c27411dbbee902004c4f4f50,
title = "Genetic alterations of the BR12 Gene: familial British and Danish dementias.",
abstract = "Classic arguments sustaining the importance of amyloid in the pathogenesis of dementia are usually centered on amyloid β (Aβ) and its role in neuronal loss characteristic of Alzheimer disease, the most common form of human cerebral amyloidosis. Two non-Aβ cerebral amyloidoses, familial British and Danish dementias, share many aspects of Alzheimer disease, including the presence of neurofibrillary tangles, parenchymal pre-amyloid and amyloid deposits, cerebral amyloid angiopathy, and a widespread inflammatory response. Both early-onset conditions are linked to specific mutations in the BRI2 gene, causing the generation of longer-than-normal protein products and the release of 2 de novo created peptides ABri and ADan, the main components of amyloid fibrils in these inherited dementias. Although the molecular mechanisms and signal transduction pathways elicited by the amyloid deposits and their relation to cognitive impairment remain to be clarified, new evidence indicates that, independent of the differences in their primary structures, Aβ, ABri, and ADan subunits are able to form morphologically compatible ion-channel-like structures and elicit single ion-channel currents in reconstituted lipid membranes. These findings reaffirm the notion that non- Aβ amyloidosis constitute suitable alternative models to study the role of amyloid deposition in the mechanism of neuronal cell death.",
author = "J. Ghiso and A. Rostagno and Y. Tomidokoro and T. Lashley and Marie Bojsen-M{\o}ller and Hans Br{\ae}ndgaard and G. Plant and J. Holton and R. Lal and T. Revesz and B. Frangione",
note = "Paper id:: PMID: 16612984",
year = "2006",
language = "English",
volume = "16",
pages = "71--9",
journal = "Brain Pathology",
issn = "1015-6305",
publisher = "Wiley-Blackwell Publishing, Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Genetic alterations of the BR12 Gene: familial British and Danish dementias.

AU - Ghiso, J.

AU - Rostagno, A.

AU - Tomidokoro, Y.

AU - Lashley, T.

AU - Bojsen-Møller, Marie

AU - Brændgaard, Hans

AU - Plant, G.

AU - Holton, J.

AU - Lal, R.

AU - Revesz, T.

AU - Frangione, B.

N1 - Paper id:: PMID: 16612984

PY - 2006

Y1 - 2006

N2 - Classic arguments sustaining the importance of amyloid in the pathogenesis of dementia are usually centered on amyloid β (Aβ) and its role in neuronal loss characteristic of Alzheimer disease, the most common form of human cerebral amyloidosis. Two non-Aβ cerebral amyloidoses, familial British and Danish dementias, share many aspects of Alzheimer disease, including the presence of neurofibrillary tangles, parenchymal pre-amyloid and amyloid deposits, cerebral amyloid angiopathy, and a widespread inflammatory response. Both early-onset conditions are linked to specific mutations in the BRI2 gene, causing the generation of longer-than-normal protein products and the release of 2 de novo created peptides ABri and ADan, the main components of amyloid fibrils in these inherited dementias. Although the molecular mechanisms and signal transduction pathways elicited by the amyloid deposits and their relation to cognitive impairment remain to be clarified, new evidence indicates that, independent of the differences in their primary structures, Aβ, ABri, and ADan subunits are able to form morphologically compatible ion-channel-like structures and elicit single ion-channel currents in reconstituted lipid membranes. These findings reaffirm the notion that non- Aβ amyloidosis constitute suitable alternative models to study the role of amyloid deposition in the mechanism of neuronal cell death.

AB - Classic arguments sustaining the importance of amyloid in the pathogenesis of dementia are usually centered on amyloid β (Aβ) and its role in neuronal loss characteristic of Alzheimer disease, the most common form of human cerebral amyloidosis. Two non-Aβ cerebral amyloidoses, familial British and Danish dementias, share many aspects of Alzheimer disease, including the presence of neurofibrillary tangles, parenchymal pre-amyloid and amyloid deposits, cerebral amyloid angiopathy, and a widespread inflammatory response. Both early-onset conditions are linked to specific mutations in the BRI2 gene, causing the generation of longer-than-normal protein products and the release of 2 de novo created peptides ABri and ADan, the main components of amyloid fibrils in these inherited dementias. Although the molecular mechanisms and signal transduction pathways elicited by the amyloid deposits and their relation to cognitive impairment remain to be clarified, new evidence indicates that, independent of the differences in their primary structures, Aβ, ABri, and ADan subunits are able to form morphologically compatible ion-channel-like structures and elicit single ion-channel currents in reconstituted lipid membranes. These findings reaffirm the notion that non- Aβ amyloidosis constitute suitable alternative models to study the role of amyloid deposition in the mechanism of neuronal cell death.

M3 - Journal article

VL - 16

SP - 71

EP - 79

JO - Brain Pathology

JF - Brain Pathology

SN - 1015-6305

IS - 1

ER -