ArticleBiophysical journal2025
Unraveling the conformational landscape of amyloid precursor protein intracellular domain.
Article in Biophysical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amyloid precursor protein intracellular domain (AICD), a cleavage product of amyloid precursor protein implicated in Alzheimer disease and amyloid lateral sclerosis, is a functionally important but structurally elusive intrinsically disordered protein. In this study, we investigate the conformational ensemble of a 35-residue AICD segment encompassing the conserved YENPTY motif using molecular dynamics simulations, small-angle x-ray scattering, circular dichroism, and nuclear magnetic resonance data. Our results reveal that AICD fluctuates between compact and extended states, exhibiting dynamic secondary structure elements and heterogeneous solvent accessibility. Small-angle x-ray scattering and circular dichroism analyses support a partially compact, flexible ensemble, whereas time-lagged independent component analysis uncovers metastable conformational states. Residue-specific solvent accessibility and hydrogen bonding patterns highlight transient structural stabilization, particularly within the YENPTY motif. These findings highlight the structural plasticity of AICD and offer insights into its potential for interaction and regulatory roles in nuclear signaling and neurodegeneration.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.