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Susi Keck
Humboldt University of Berlin
4Publications
2H-index
427Citations
Publications 4
Newest
Published on Dec 15, 2006in Biochemical Journal 4.33
Diana Poppek4
Estimated H-index: 4
(HHU: University of Düsseldorf),
Susi Keck2
Estimated H-index: 2
(Humboldt University of Berlin)
+ 5 AuthorsTilman Grune67
Estimated H-index: 67
(Humboldt University of Berlin)
Hyperphosphorylated tau proteins accumulate in the paired helical filaments of neurofibrillary tangles seen in such tauopathies as Alzheimer9s disease. In the present paper we show that tau turnover is dependent on degradation by the proteasome (inhibited by MG132) in HT22 neuronal cells. Recombinant human tau was rapidly degraded by the 20 S proteasome in vitro , but tau phosphorylation by GSK3β (glycogen synthase kinase 3β) significantly inhibited proteolysis. Tau phosphorylation was increased...
Published on Apr 1, 2005
Diana Poppek4
Estimated H-index: 4
,
Susi Keck2
Estimated H-index: 2
+ 2 AuthorsTilman Grune67
Estimated H-index: 67
Published on Jul 1, 2004in Neurobiology of Aging 4.40
Susi Keck2
Estimated H-index: 2
,
Anja Gräfe + 1 AuthorsTilman Grune67
Estimated H-index: 67
Published on Feb 28, 2003in Journal of Neurochemistry 4.87
Susi Keck2
Estimated H-index: 2
,
Robert Nitsch57
Estimated H-index: 57
+ 1 AuthorsOliver Ullrich33
Estimated H-index: 33
Alzheimer's disease (AD) is characterized neuropathologically by intracellular neurofibrillary tangles (NFTs) formed of tau-based paired helical filaments (PHFs) and extracellular β-amyloid plaques. The degree of Alzheimer dementia correlates with the severity of PHFs and NFTs. As an intraneuronal accumulation of oxidatively damaged proteins has been found in the brains of patients with AD, a dysfunction of the proteasomal system, which degrades damaged proteins, has been assumed to cause protei...
1