PAPER Bohid S, Ali LK, Romero-Leguizamón CR, Langkilde AE, Dos Santos AB, Kohlmeier KA
SEARCH RESULTS
18663 RESULTS
PAPER Holfeld A, Schuster D, Sesterhenn F, Gillingham AK, Stalder P, Haenseler W, Barrio-Hernandez I, Ghosh D, Vowles J, Cowley SA, Nagel L, Khanppnavar B, Serdiuk T, Beltrao P, Korkhov VM, Munro S, Riek R, de Souza N, Picotti P
Systematic identification of structure-specific protein-protein interactions.
Mol Syst Biol. 2024 May 3; PubMed.PAPER Maltseva S, Kerr D, Turke M, Adams EJ, Lee KY
Parkinson's disease-associated mutations in α-synuclein alters its lipid-bound state.
Biophys J. 2024 May 3; PubMed.Jennifer Rauch on Might SORL1 Bind Tau in Glia, Fuel Its Aggregation?
COMMENT This is an interesting mechanistic study by Cooper et al., looking at the interactions between tau and SORL1, a protein with known associations to AD. This new study expands on the authors’ prior biochemical work looking at the tau-LRP1 interaction and it
Sam Gandy on Might SORL1 Bind Tau in Glia, Fuel Its Aggregation?
COMMENT SORL1 is best known as a modulator of APP sorting, metabolism, and amyloidogenesis. This new data extends the action of SORL1 to tauopathy, providing an unexpected convergence of two key pathways in Alzheimer pathogenesis. Tau aggregates form in neurons a
Might SORL1 Bind Tau in Glia, Fuel Its Aggregation?
RESEARCH NEWS 2024-05-04 Research News Over the last few decades, evidence has emerged to peg the sortilin-related receptor, SORL1, as a risk factor for Alzheimer’s disease and even as the fourth gene for familial AD. SORL1 helps traffic amyloid precursor protein through the endo
Marc Diamond on Might SORL1 Bind Tau in Glia, Fuel Its Aggregation?
COMMENT The take-home message for me is that any assertion of a single protein “receptor” for tau at the surface should be taken with a grain of salt. This paper purports to show that SORL1 is a “receptor” for tau. However, one of the final figures indicates that
Gregory Petsko on Might SORL1 Bind Tau in Glia, Fuel Its Aggregation?
COMMENT The paper is interesting and potentially important. That retromer-regulated trafficking is important in tauopathies, including Alzheimer’s disease, is well-established (e.g., Mishra et al., 2023). However, the direct binding of tau to SORL1 is a new findi
Kenneth Kosik on Might SORL1 Bind Tau in Glia, Fuel Its Aggregation?
COMMENT This paper by J.M. Cooper et al. is a well-executed study that advances our thinking about the route tau travels once internalized. In essence, the problem we face is that, internalized via LRP1 through which it enters endosomes, tau must escape the endos
George King
Atlanta, United States
PAPER Jacobsen L, Madsen P, Jacobsen C, Nielsen MS, Gliemann J, Petersen CM
Activation and functional characterization of the mosaic receptor SorLA/LR11.
J Biol Chem. 2001 Jun 22;276(25):22788-96. Epub 2001 Apr 9 PubMed.PAPER Alzghool OM, Aarnio R, Helin JS, Wahlroos S, Keller T, Matilainen M, Solis J, Danon JJ, Kassiou M, Snellman A, Solin O, Rinne JO, Haaparanta-Solin M
Correction: Glial reactivity in a mouse model of beta-amyloid deposition assessed by PET imaging of P2X7 receptor and TSPO using [11C]SMW139 and [18F]F-DPA.
EJNMMI Res. 2024 May 3;14(1):44. PubMed.PAPER Espay AJ, Herrup K, Imbimbo BP, Kepp KP, Daly T
Recalibrating the Risk-Benefit Profiles of Lecanemab and Donanemab: Scales, Immunoreactivity, and Changes in Amyloid-β42.
J Alzheimers Dis. 2024 May 2; PubMed.PAPER Shen FS, Liu C, Sun HZ, Chen XY, Xue Y, Chen L
Emerging evidence of context-dependent synapse elimination by phagocytes in the CNS.
J Leukoc Biol. 2024 May 3; PubMed.PAPER Meng X, Cui W, Liang Q, Zhang B, Wei Y
Trends and hotspots in tea and Alzheimer's disease research from 2014 to 2023: A bibliometric and visual analysis.
Heliyon. 2024 May 15;10(9):e30063. Epub 2024 Apr 23 PubMed.Current Filters
- Date Range : May 2023 to May 2024 x