Results 51 to 60 of about 243,600 (356)

Polarization‐resolved femtosecond Vis/IR spectroscopy tailored for resolving weak signals in biological samples using minimal sample volume

FEBS Open Bio, EarlyView.
Unique biological samples, such as site‐specific mutant proteins, are available only in limited quantities. Here, we present a polarization‐resolved transient infrared spectroscopy setup with referencing to improve signal‐to‐noise tailored towards tracing small signals. We provide an overview of characterizing the excitation conditions for polarization‐
Clark Zahn, Karsten Heyne
wiley   +1 more source

Targeting tauopathy with engineered tau-degrading intrabodies [PDF]

, 2019
BACKGROUND: The accumulation of pathological tau is the main component of neurofibrillary tangles and other tau aggregates in several neurodegenerative diseases, referred to as tauopathies.
Gallardo, Gilbert, Holtzman, David M, Jiang, Hong, Leyns, Cheryl E G, Lin, Kent H, Mann, Carolyn N, Ricardez, Sara M, Wong, Connie H   +7 more
core   +1 more source

Microtubules gate tau condensation to spatially regulate microtubule functions. [PDF]

, 2019
Tau is an abundant microtubule-associated protein in neurons. Tau aggregation into insoluble fibrils is a hallmark of Alzheimer's disease and other types of dementia1, yet the physiological state of tau molecules within cells remains unclear.
A Ettinger, A Hernandez-Vega, A Kremer, A Seitz, Aileen J. Lam, AR Duan, B Niewidok, BY Monroy, Dan W. Nowakowski, DP McVicker, DP McVicker, EH Kellogg, H Hagiwara, H Zempel, HT Hoang, J Baumbach, JA Garcia-Leon, Jisoo Han, K Tepper, Kassandra M. Ori-McKenney, KM Ori-McKenney, KS Hubbard, L Qiang, L Urnavicius, LC Kapitein, M Goedert, M Vershinin, M Vershinin, MH Hinrichs, Michael Vershinin, PA Gutierrez, R Dixit, R Zhang, RD Vale, Richard J. McKenney, RJ McKenney, RJ McKenney, Ruensern Tan, S Ambadipudi, S Konzack, S Wegmann, S Wegmann, Sergi Simó, SR White, Tracy Tan, V Makrides, W Yu, XH Li   +47 more
core   +1 more source

Proteasomal degradation of tau protein [PDF]

Journal of Neurochemistry, 2002
AbstractFilamentous inclusions composed of the microtubule‐associated protein tau are a defining characteristic of a large number of neurodegenerative diseases. Here we show that tau degradation in stably transfected and non‐transfected SH‐SY5Y cells is blocked by the irreversible proteasome inhibitor lactacystin.
Della C, David, Robert, Layfield, Louise, Serpell, Yolanda, Narain, Michel, Goedert, Maria Grazia, Spillantini   +5 more
openaire   +2 more sources

The role of lipid metabolism in neuronal senescence

FEBS Open Bio, EarlyView.
Disrupted lipid metabolism, through alterations in lipid species or lipid droplet accumulation, can drive neuronal senescence. However, lipid dyshomeostasis can also occur alongside neuronal senescence, further amplifying tissue damage. Delineating how lipid‐induced senescence emerges in neurons and glial cells, and how it contributes to ageing and ...
Dikaia Tsagkari, Eleftheria Panagiotidou, Nektarios Tavernarakis   +2 more
wiley   +1 more source

Pathological progression induced by the frontotemporal dementia-associated R406W tau mutation in patient-derived iPSCs [PDF]

, 2019
Mutations in the microtubule-associated protein tau (MAPT) gene are known to cause familial frontotemporal dementia (FTD). The R406W tau mutation is a unique missense mutation whose patients have been reported to exhibit Alzheimer\u27s disease (AD)-like ...
et al,, Karch, Celeste M, Nakamura, Mari
core   +1 more source

In vivo microdialysis reveals age-dependent decrease of brain interstitial fluid tau levels in P301S human tau transgenic mice [PDF]

, 2011
Although tau is a cytoplasmic protein, it is also found in brain extracellular fluids, e.g., CSF. Recent findings suggest that aggregated tau can be transferred between cells and extracellular tau aggregates might mediate spread of tau pathology. Despite
Binder, Lester I, Cirrito, John R, Diamond, Marc I, Finn, Mary Beth, Holmes, Brandon B, Holtzman, David M, Jiang, Hong, Lee, Virginia M.-Y., Mandelkow, Eva-Maria, Stewart, Floy R, Yamada, Kaoru   +10 more
core   +2 more sources

Microglial dynamics and ferroptosis induction in human iPSC‐derived neuron–astrocyte–microglia tri‐cultures

FEBS Open Bio, EarlyView.
A tri‐culture of iPSC‐derived neurons, astrocytes, and microglia treated with ferroptosis inducers as an Induced ferroptosis model was characterized by scRNA‐seq, cell survival, and cytokine release assays. This analysis revealed diverse microglial transcriptomic changes, indicating that the system captures key aspects of the complex cellular ...
Hongmei Lisa Li, Hiroko Ohmiya, Sou Sakamoto, Masato Yugami, Akiko Oki, Makoto Furusawa, Yan Ling   +6 more
wiley   +1 more source

Tau phosphorylation at Alzheimer\u27s disease-related Ser356 contributes to tau stabilization when PAR-1/MARK activity is elevated. [PDF]

, 2016
Abnormal phosphorylation of the microtubule-associated protein tau is observed in many neurodegenerative diseases, including Alzheimer\u27s disease (AD).
Ando, Kanae, Hayashishita, Motoki, Hisanaga, Shin-Ichi, Iijima, Koichi M., Ohtake, Yosuke, Oka, Mikiko, Shimizu, Sawako   +6 more
core   +1 more source

Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau. [PDF]

, 2018
Small heat shock proteins (sHSPs) are a class of oligomeric molecular chaperones that limit protein aggregation. However, it is often not clear where sHSPs bind on their client proteins or how these protein-protein interactions (PPIs) are regulated. Here,
Agard, David A, Betegon, Miguel, Freilich, Rebecca, Gestwicki, Jason E, Julien, Olivier, Mok, Sue-Ann, Southworth, Daniel R, Takeuchi, Koh, Tse, Eric   +8 more
core   +2 more sources