Results 61 to 70 of about 1,790,741 (301)

The Ca2+ sensor protein Swiprosin-1/EFhd2 is present in neurites and involved in kinesin-mediated transport in neurons [PDF]

, 2014
This work was supported by grants from the German Science Foundation (Deutsche Forschungsgemeinschaft, DFG; FOR832, to DM), the German Federal Ministry of Education and Research (01GQ113; to BW), the Bavarian Ministry of Sciences, Research and the Arts ...
Oliver Welzel, Böhm, Konrad J., Fritsch, K, Regensburger, M, Winner, B, Dirk Mielenz, Brachs, Sebastian, Regensburger, Martin, Francesc Perez-Branguli, Iryna Prots, Perez-Branguli , F, Eva Borger, Loy, Kristina, Brachs, S, Buslei, R, Wenzel, EM, Borger, Eva, Gromer, TW, Mielenz, Dirk, Max Holzer, Beate Winner, Kristina Loy, Holzer, M, Purohit, Pavitra, Holzer, Max, Purohit, P, Buslei, Rolf, Welzel, Oliver, Gunn-Moore, Frank J, Kristin Fritsch, Eva Maria Wenzel, Frank Gunn-Moore, Mielenz, D, Konrad J Böhm, Rolf Buslei, Loy, K, Teja W Grömer, Bohm, KJ, Fritsch, Kristin, Pavitra Purohit, Wenzel, Eva Maria, Prots, I, Perez-Branguli, Francesc, Gunn-Moore, Frank, Welzel, O, Prots, Iryna, Grömer, Teja W., Winner, Beate, Sebastian Brachs, Martin Regensburger   +49 more
core   +2 more sources

Treatment with KCL‐286, a first‐in‐class retinoic acid receptor‐β (RARβ) agonist, ameliorates neuronal DNA damage and inflammation in a mouse model of Alzheimer's disease

FEBS Open Bio, EarlyView.
Repair of neuronal DNA damage in Alzheimer's disease by KCL‐286. (A) Amyloid‐β oligomers and plaques impair neuronal DNA repair pathways, leading to DNA double‐strand breaks and glial activation. (B) KCL‐286 activates RARβ/RXR signalling via retinoic acid response elements (RAREs), associated with increased BRCA1 expression, enhanced DNA repair and ...
Natasha Hill, Hassan Yousef Othman AlMuallim, Elouisa Maddock, Carl Hobbs, Earl Clarke, Maria B. Goncalves, Jonathan P. T. Corcoran   +6 more
wiley   +1 more source

Interactions and Cytotoxicity of Human Neurodegeneration- Associated Proteins Tau and α-Synuclein in the Simple Model Dictyostelium discoideum

Frontiers in Cell and Developmental Biology, 2021
The abnormal accumulation of the tau protein into aggregates is a hallmark in neurodegenerative diseases collectively known as tauopathies. In normal conditions, tau binds off and on microtubules aiding in their assembly and stability dependent on the ...
Katelyn Mroczek, Sanjanie Fernando, Paul R. Fisher, Sarah J. Annesley   +3 more
doaj   +1 more source

Optimizing photoexcitation conditions for time‐resolved X‐ray solution scattering experiments

FEBS Open Bio, EarlyView.
Time‐resolved X‐ray solution scattering (TR‐XSS) is a powerful technique to visualize how proteins change their structure in real time after light activation. Selecting the right laser photoexcitation conditions—fluence, excitation geometry, and sample refresh rate—is critical to maximize the experimental signal while avoiding unwanted side effects ...
Matteo Levantino
wiley   +1 more source

α-Synuclein Aggregated with Tau and β-Amyloid in Human Platelets from Healthy Subjects: Correlation with Physical Exercise

Frontiers in Aging Neuroscience, 2018
The loss of protein homeostasis that has been associated with aging leads to altered levels and conformational instability of proteins, which tend to form toxic aggregates.
Simona Daniele, Deborah Pietrobono, Jonathan Fusi, Annalisa Lo Gerfo, Eugenio Cerri, Lucia Chico, Caterina Iofrida, Lucia Petrozzi, Filippo Baldacci, Chiara Giacomelli, Fabio Galetta, Gabriele Siciliano, Ubaldo Bonuccelli, Maria L. Trincavelli, Ferdinando Franzoni, Claudia Martini   +15 more
doaj   +1 more source

Adenosine triphosphate as a modulator of protein interactions and stability

FEBS Open Bio, EarlyView.
ATP is best known as the cell's energy currency, but it also shapes how proteins fold, interact, aggregate and form biomolecular condensates. This review explains the emerging physical principles behind these effects, including weak binding to charged protein regions, magnesium‐dependent behaviour and concentration‐dependent control of protein ...
Shuyuan Tan, Robin Curtis
wiley   +1 more source

Alterations in iron content, iron-regulatory proteins and behaviour without tau pathology at one year following repetitive mild traumatic brain injury

Acta Neuropathologica Communications, 2023
Repetitive mild traumatic brain injury (r-mTBI) has increasingly become recognised as a risk factor for the development of neurodegenerative diseases, many of which are characterised by tau pathology, metal dyshomeostasis and behavioural impairments.
Sydney M. A. Juan, Maria Daglas, Phan H. Truong, Celeste Mawal, Paul A. Adlard   +4 more
doaj   +1 more source

Is Tau a Prion-Like Protein?

Journal of Alzheimer's Disease, 2014
It has been over a quarter century since the discovery in the mid-1980s that the paired helical filaments of neurofibrillary tangles were made up of abnormally hyperphosphorylated tau. A decade earlier tau had been first isolated from porcine brain as a heat stable protein essential for microtubule assembly.
Miguel, Medina, Jesús, Avila
openaire   +2 more sources

Tau binding protein CAPON induces tau aggregation and neurodegeneration [PDF]

Nature Communications, 2019
AbstractTo understand the molecular processes that link Aβ amyloidosis, tauopathy and neurodegeneration, we screened for tau-interacting proteins by immunoprecipitation/LC-MS. We identified the carboxy-terminal PDZ ligand of nNOS (CAPON) as a novel tau-binding protein.
Shoko Hashimoto, Yukio Matsuba, Naoko Kamano, Naomi Mihira, Naruhiko Sahara, Jiro Takano, Shin-ichi Muramatsu, Takaomi C. Saido, Takashi Saito   +8 more
openaire   +3 more sources

The Calcium-Binding Protein EFhd2 Modulates Synapse Formation In Vitro and Is Linked to Human Dementia [PDF]

, 2014
EFhd2 is a calcium-binding adaptor protein that has been found to be associated with pathologically aggregated tau in the brain in Alzheimer disease and in a mouse model of frontotemporal dementia.
Gunn-Moore, Frank J, Mann, David, Spires-Jones, Tara, Borger, Eva, Herrmann, Abigail, Gunn-Moore, Frank, Spires-Jones , Tara, Mann, David A   +7 more
core   +1 more source