Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Teemu Natunen"'
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:
Lars Bertram, Kaisa M.A. Kurkinen, Rudolph E. Tanzi, Annakaisa Haapasalo, Jayashree Viswanathan, Petra Mäkinen, Teemu Natunen, Hilkka Soininen, Mikko Hiltunen
Publikováno v:
Biochemistry. 52:3899-3912
Ubiquilin-1 is an Alzheimer's disease-associated protein, which is known to modulate amyloid precursor protein (APP) processing, amyloid-β (Aβ) secretion, and presenilin-1 (PS1) accumulation. Here, we aim to elucidate the molecular mechanisms by wh
Autor:
Mari Takalo, Hilkka Soininen, Rudolph E. Tanzi, Teemu Natunen, Mikko Hiltunen, Annakaisa Haapasalo, Jayashree Viswanathan, Kaisa M.A. Kurkinen
Publikováno v:
Expert Opinion on Therapeutic Targets. 17:795-810
Alzheimer's disease (AD) is a common neurodegenerative disorder affecting an increasing number of people worldwide as the population ages. Currently, there are no drugs available that could prevent AD pathogenesis or slow down its progression. Increa
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,
Autor:
Mari Takalo, Hilkka Soininen, Heikki Tanila, Jayashree Viswanathan, Mikko Hiltunen, Annakaisa Haapasalo, Teemu Natunen, Kaisa M.A. Kurkinen, Rudolph E. Tanzi
Publikováno v:
Molecular Neurodegeneration
Background Ubiquilin-1 is a ubiquitin-like protein involved in the pathogenesis of Alzheimer’s disease (AD) and other neurodegenerative disorders via different mechanisms. UBQLN1 UBQ-8i genetic variation associates with increased AD risk. Ubiquilin