Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Timo Sarajärvi"'
Autor:
Teemu Natunen, Mari Takalo, Susanna Kemppainen, Stina Leskelä, Mikael Marttinen, Kaisa M.A. Kurkinen, Juha-Pekka Pursiheimo, Timo Sarajärvi, Jayashree Viswanathan, Sami Gabbouj, Eino Solje, Eveliina Tahvanainen, Tiina Pirttimäki, Mitja Kurki, Jussi Paananen, Tuomas Rauramaa, Pasi Miettinen, Petra Mäkinen, Ville Leinonen, Hilkka Soininen, Kari Airenne, Rudolph E. Tanzi, Heikki Tanila, Annakaisa Haapasalo, Mikko Hiltunen
Publikováno v:
Neurobiology of Disease, Vol 85, Iss , Pp 187-205 (2016)
Accumulation of β-amyloid (Aβ) and phosphorylated tau in the brain are central events underlying Alzheimer's disease (AD) pathogenesis. Aβ is generated from amyloid precursor protein (APP) by β-site APP-cleaving enzyme 1 (BACE1) and γ-secretase-
Externí odkaz:
https://doaj.org/article/fec99dbad77e483d989eaa39ef52f9e5
Autor:
Tiina Laiterä, Timo Sarajärvi, Annakaisa Haapasalo, Lakshman Puli, Tarja Kauppinen, Petra Mäkinen, Tuomas Rauramaa, Heikki Tanila, Juha E Jääskeläinen, Irina Alafuzoff, Hilkka Soininen, Ville Leinonen, Mikko Hiltunen
Publikováno v:
PLoS ONE, Vol 9, Iss 4, p e93717 (2014)
The potential similarity between the brain pathology of idiopathic normal pressure hydrocephalus (iNPH) and Alzheimer disease (AD) is intriguing and thus further studies focusing on the underlying molecular mechanisms may offer valuable information f
Externí odkaz:
https://doaj.org/article/bad24f4c426749caa7432b273f68074c
Autor:
Teemu Natunen, Henna Martiskainen, Timo Sarajärvi, Seppo Helisalmi, Juha-Pekka Pursiheimo, Jayashree Viswanathan, Marjo Laitinen, Petra Mäkinen, Tarja Kauppinen, Tuomas Rauramaa, Ville Leinonen, Irina Alafuzoff, Annakaisa Haapasalo, Hilkka Soininen, Mikko Hiltunen
Publikováno v:
PLoS ONE, Vol 8, Iss 11, p e80700 (2013)
Alzheimer's disease (AD) has been postulated to involve defects in the clearance of amyloid-β (Aβ). Activation of liver X receptor α (LXRα) increases the expression of apolipoprotein E (ApoE) as well as cholesterol transporters ABCA1 and ABCG1, l
Externí odkaz:
https://doaj.org/article/bd432ea45efc4cffa22cd97a2a5a43d8
Autor:
Mari Takalo, Juha-Pekka Pursiheimo, Jussi Paananen, Tiina Pirttimäki, Eino Solje, Heikki Tanila, Tuomas Rauramaa, Pasi Miettinen, Sami Gabbouj, Rudolph E. Tanzi, Ville Leinonen, Stina Leskelä, Timo Sarajärvi, Teemu Natunen, Mitja I. Kurki, Mikko Hiltunen, Jayashree Viswanathan, Susanna Kemppainen, Annakaisa Haapasalo, Mikael Marttinen, Eveliina Tahvanainen, Kaisa M.A. Kurkinen, Kari J. Airenne, Hilkka Soininen, Petra Mäkinen
Publikováno v:
Neurobiology of Disease, Vol 85, Iss, Pp 187-205 (2016)
Accumulation of β-amyloid (Aβ) and phosphorylated tau in the brain are central events underlying Alzheimer's disease (AD) pathogenesis. Aβ is generated from amyloid precursor protein (APP) by β-site APP-cleaving enzyme 1 (BACE1) and γ-secretase-
Autor:
Maria Jäntti, Virpi Talman, Raimo K. Tuominen, Kaisa M. A. Paldanius, Teemu Natunen, Mikko Hiltunen, Petra Mäkinen, J.C. Wu, Timo Sarajärvi, Ilari Tarvainen
Publikováno v:
Neuropharmacology. 141
Abnormal protein kinase C (PKC) function contributes to many pathophysiological processes relevant for Alzheimer's disease (AD), such as amyloid precursor protein (APP) processing. Phorbol esters and other PKC activators have been demonstrated to enh
Autor:
Mitja I. Kurki, Anne M. Remes, Anette Hall, Henna Martiskainen, Ville Leinonen, Terho Lehtimäki, Mikko Hiltunen, Anne M. Koivisto, Kari M. Mattila, Hilkka Soininen, Timo Sarajärvi, Marjo Laitinen, Seppo Helisalmi, Petra Mäkinen, Teemu Natunen, Jayashree Viswanathan, Kaisa M.A. Kurkinen, Sanna-Kaisa Herukka, Annakaisa Haapasalo, Jaakko Huovinen
Publikováno v:
Journal of Alzheimer's Disease. 43:565-573
BACKGROUND Several risk loci for Alzheimer's disease (AD) have been identified during recent years in large-scale genome-wide association studies. However, little is known about the mechanisms by which these loci influence AD pathogenesis. OBJECTIVE
Autor:
Marjo Laitinen, Jussi Paananen, Seppo Helisalmi, Tuomas Rauramaa, Juha E. Jääskeläinen, Ville Leinonen, Joel Huovinen, Annakaisa Haapasalo, Mikko Hiltunen, Anne M. Remes, Irina Alafuzoff, Timo Sarajärvi, Tiina Laiterä, Hilkka Soininen
Publikováno v:
Journal of Alzheimer's disease : JAD. 55(3)
Background Idiopathic normal pressure hydrocephalus (iNPH) is a dementing condition featuring characteristic symptoms, ventriculomegaly, and normal or slightly elevated cerebrospinal fluid pressure. In Alzheimer's disease (AD) patients, diffuse aggre
Autor:
Annakaisa Haapasalo, Kaisa M.A. Kurkinen, Seppo Helisalmi, Timo Sarajärvi, Kristina Mullin, Rudolph E. Tanzi, Antonio R. Parrado, Teemu Natunen, Hilkka Soininen, Lars Bertram, Petra Mäkinen, Juha-Pekka Pursiheimo, Mikko Hiltunen, Irina Alafuzoff
Publikováno v:
Journal of Alzheimer's Disease. 37:217-232
Golgi-localized gamma-ear-containing ADP-ribosylation factor-binding protein (GGA3) is a central regulator of trafficking and degradation of BACE1 (beta-site A beta PP-cleaving enzyme), the rate-limiting enzyme in the production of amyloid-beta (A be
Autor:
Anu Lipsanen, Timo Sarajärvi, Jukka Jolkkonen, Mikko Hiltunen, Sirpa Peräniemi, Hilkka Soininen, Petra Mäkinen, Annakaisa Haapasalo
Publikováno v:
Journal of Cellular and Molecular Medicine
Alzheimer's disease (AD) and cerebral ischaemia share similar features in terms of altered amyloid precursor protein (APP) processing and β-amyloid (Aβ) accumulation. We have previously shown that Aβ and calcium deposition, and β-secretase activi
SEPT8 modulates β-amyloidogenic processing of APP by affecting the sorting and accumulation of BACE1
Autor:
Petra Mäkinen, Heikki Tanila, Tuomas Rauramaa, Hilkka Soininen, Mikko Hiltunen, Ville Leinonen, Sami Gabbouj, Kaisa M.A. Kurkinen, Fanni Haapalinna, Timo Sarajärvi, Laura J. Turner, Teemu Natunen, Mitja I. Kurki, Annakaisa Haapasalo, Jussi Paananen, Mikael Marttinen, Anne M. Koivisto, Fiona R. Lucas
Publikováno v:
Journal of cell science. 129(11)
Dysfunction and loss of synapses are early pathogenic events in Alzheimer's disease. A central step in the generation of toxic amyloid-β (Aβ) peptides is the cleavage of amyloid precursor protein (APP) by β-site APP-cleaving enzyme (BACE1). Here,