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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3148223 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0019491 | PLOS |
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Basic Science and Pathogenesis.
Alzheimers Dement
December 2024
Oregon Health & Science University, Portland, OR, USA.
Background: Dementia with Lewy Bodies (DLB) is one of the most common Alzheimer's Disease (AD)-related dementias and it is defined by the presence of abnormal cytoplasmic inclusions composed of aggregated α-synuclein (αsyn) in neuronal soma, known as Lewy bodies (LB). LB often coexists with AD type pathology such as amyloid-β (Aβ) plaques and neurofibrillary tangles containing hyperphosphorylated tau in several LB dementias, including Parkinson's Disease Dementia and Lewy Body variant AD. These co-pathologies likely represent a spectrum of various contributions of shared mechanisms that underlie these diseases.
View Article and Find Full Text PDFBasic Science and Pathogenesis.
Alzheimers Dement
December 2024
USC Keck School of Medicine, Los Angeles, CA, USA.
Background: Human Apolipoprotein (APOE) has three isoforms, ε2, ε3, and ε4 among which ε4 (APOE4) confers the highest risk for late-onset Alzheimer's disease (AD). APOE4 is also the most prone to aggregate among APOE isoforms. Current evidence strongly suggests that APOE aggregation leads to neuronal dysfunction and eventually to AD.
View Article and Find Full Text PDFTMEM106B C-terminal fragments aggregate and drive neurodegenerative proteinopathy in transgenic Caenorhabditis elegans.
Alzheimers Dement
December 2024
Geriatrics Research Education and Clinical Center, Veterans Affairs Puget Sound Health Care System, Seattle, Washington, USA.
Introduction: Genetic variation in the lysosomal and transmembrane protein 106B (TMEM106B) modifies risk for several neurodegenerative disorders, especially frontotemporal lobar degeneration (FTLD). The C-terminal (CT) domain of TMEM106B occurs as fibrillar protein deposits in the brains of dementia patients.
Methods: To determine the TMEM CT aggregation propensity and neurodegenerative potential, we generated transgenic Caenorhabditis elegans expressing the human TMEM CT fragment aggregating in FTLD cases.
Facile synthesis of silver nanoclusters for promoting highly sensitive surface-enhanced Raman scattering detection of alkyne-tagged biomolecules.
Chem Commun (Camb)
December 2024
School of Chemical and Printing Dyeing Engineering, Henan University of Engineering, Zhengzhou, 451191, P. R. China.
We synthesized two novel silver-based nanocluster materials (TOS-Ag NCs and TNS-Ag NCs) that were used as SERS substrates, combining the powerful adsorption capability and aggregation effect of silver-sulfur clusters to achieve a highly sensitive identification and detection of alkyne-tagged molecules in the Raman-silent region. This work provides new insights for designing novel nanoclusters as SERS substrates displaying ultrahigh sensitive detection of alkyne-tagged molecules.
View Article and Find Full Text PDFSite-Specific Glyco-Tagging of Native Proteins for the Development of Biologicals.
J Am Chem Soc
December 2024
Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, and Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, CG 3584, The Netherlands.
Glycosylation is an attractive approach to enhance biological properties of pharmaceutical proteins; however, the precise installation of glycans for structure-function studies remains challenging. Here, we describe a chemoenzymatic methodology for glyco-tagging of proteins by peptidoligase catalyzed modification of the -terminus of a protein with a synthetic glycopeptide ester having an -acetyl-glucosamine (GlcNAc) moiety to generate an -GlcNAc modified protein. The GlcNAc moiety can be elaborated into complex glycans by -glycosylation using well-defined sugar oxazolines and mutant forms of endo β--acetylglucosaminidases (ENGases).
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