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Journal: The Journal of Prevention of Alzheimer's Disease
Article Title: Evaluation of plasma p-tau217 biomarkers in detecting amyloid pathology and predicting cognitive outcomes: Observations from Japanese Alzheimer’s disease neuroimaging initiative cohort
doi: 10.1016/j.tjpad.2026.100502
Figure Lengend Snippet: Diagnostic performance and cutoff points of plasma p-tau217 biomarkers for detecting amyloid pathology ( A ) ROC curves showing the AUCs of each plasma biomarker in discriminating amyloid pathology, as defined by the CSF Aβ42/Aβ40 ratio. ( B ) Simoa p-tau217, ( C ) Lumipulse p-tau217, and ( D ) Lumipulse p-tau217/Aβ42 × 10³ plots are shown. The red solid lines indicate the single-point cutoffs determined by the maximum Youden index. The red dashed lines represent the two-point cutoffs achieving >95% sensitivity and >95% specificity, with the intermediate zones shaded in red. For Lumipulse p-tau217, only one cutoff is shown as it meets both criteria using a single threshold. For Lumipulse p-tau217/Aβ42, the single-point and two-point cutoffs were identical, and thus only the red solid line is displayed. FDA-approved two-point cutoffs are indicated by blue dashed lines, with the intermediate zones shaded in blue.
Article Snippet:
Techniques: Diagnostic Assay, Clinical Proteomics, Biomarker Discovery
Journal: The Journal of Prevention of Alzheimer's Disease
Article Title: Evaluation of plasma p-tau217 biomarkers in detecting amyloid pathology and predicting cognitive outcomes: Observations from Japanese Alzheimer’s disease neuroimaging initiative cohort
doi: 10.1016/j.tjpad.2026.100502
Figure Lengend Snippet: Kaplan–Meier curves showing risk of conversion to AD dementia based on plasma p-tau217 biomarkers Participants were stratified into high (above cutoff) and low (below cutoff) groups using cutoff values determined by the maximum Youden index. ( A ) Simoa p-tau217, ( B ) Lumipulse p-tau217, and ( C ) Lumipulse p-tau217/Aβ42 ratio. Participants in the high-biomarker group exhibited significantly higher rates of conversion to AD dementia during follow-up. Log-rank test p-values were as follows: Simoa p-tau217 (p = 0.002), Lumipulse p-tau217 (p < 0.001), and Lumipulse p-tau217/Aβ42 (p < 0.001). Numbers at risk are shown in the bottom.
Article Snippet:
Techniques: Clinical Proteomics, Biomarker Discovery
Journal: International Journal of Molecular Sciences
Article Title: Integrated Symbiotic Pleiotropy: Long Non-Coding RNAs and Disordered Proteins Interweaving the Functional Layers of the Eukaryotic Cell
doi: 10.3390/ijms27083478
Figure Lengend Snippet: Evolutionary trajectory of TERT: from rigid catalyst to liquid-state driver. ( A ) Structural stability in invertebrates: The TERT ortholog from T. castaneum (PDB ID: 7QKM) represents the ancestral, predominantly ordered state. FuzDrop profiling reveals a low droplet-promoting probability (p LLPS : 0.11), where the protein acts as a rigid enzymatic unit. ( B ) LLPS expansion in mammals: Human TERT exhibits a significant rise in intrinsic disorder (31.43%) and p LLPS (0.62). Domain mapping shows that liquidity peaks coincide with RNA-interacting motifs (GQ, CP, and QFP) and the Nuclear Localization Signal (NLS), suggesting that in higher eukaryotes, TERT functions as an active organizer of telomeric condensates. ( C ) The “L-paradox” across taxa: Large-scale analysis reveals that while intrinsic disorder remains relatively conserved (28–38% across vertebrates), the propensity for phase separation (pLLPS) exhibits sharp, lineage-specific oscillations. This “L-paradox” (liquidity paradox) indicates that phase behavior acts as an evolutionary “switch” or rheostat, with outliers like the lamprey and domestic cat (marked with red stars) showing extreme spikes in liquidity. This variability likely reflects lineage-specific adaptations in genomic maintenance, metabolic rate, and cellular longevity.
Article Snippet:
Techniques:
Journal: International Journal of Molecular Sciences
Article Title: Integrated Symbiotic Pleiotropy: Long Non-Coding RNAs and Disordered Proteins Interweaving the Functional Layers of the Eukaryotic Cell
doi: 10.3390/ijms27083478
Figure Lengend Snippet: Biophysical landscapes of Arc orthologs and Gag-related proteins. (Top) 3D structures (PDB), residue-based droplet-promoting probabilities (p DP ), predicted regions of disorder, aggregation, and context-dependent binding (FuzDrop/FuzPred), and UniProt domains/features aligned with the p DP graph of ( A ) D. melanogaster (dArc2) and ( B ) H. sapiens (Arc), illustrating the evolutionary transition from rigid invertebrate architecture to high-disorder and LLPS propensity mammalian condensates. (Bottom) ( C ) Comparative analysis of p LLPS propensity, protein disorder, and amyloidogenic potential across 30+ species. Left Y-axis: p LLPS and disorder scores (0.0–1.0). Right Y-axis: Number of amyloidogenic segments (PASTA 2.0). Yellow/Pink bars: Evolutionary benchmarks (HIV-1 Gag, PERV Gag, and PEG10) revealing the high ancestral propensity for phase separation and aggregation. Light-blue bars: Drosophila convergent homologs (dArc1, dArc2); dark-blue bars: vertebrate orthologs, highlighting the significant “mammalian shift” in p LLPS . Red dots: Amyloidogenic potential, showing discrete “quantal” plateaus (7–8 for Sauropsids vs. 38 for Eutherians). Stars: Red and blue stars denote significant outliers in amyloidogenic potential (notably the Indian elephant) and p LLPS propensity, respectively. Note: The proposed evolutionary trajectories and “quantum leaps” of these biophysical parameters are discussed in detail within the main text .
Article Snippet:
Techniques: Residue, Binding Assay