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Record W7132876170

Analysis of beta-amyloid aggregation and amyloid precursor protein dimerization

2006· dissertation· W7132876170 on OpenAlexfundno aff
Paul M. Gorman

Bibliographic record

VenueTSpace · 2006
Typedissertation
Language
FieldMedicine
TopicAlzheimer's disease research and treatments
Canadian institutionsnot available
FundersCanadian Institutes of Health ResearchAlzheimer SocietyMuscular Dystrophy AssociationNational Institutes of HealthAlzheimer's Association
KeywordsFibrillogenesisFibrilNeurodegenerationSenile plaquesProtein aggregationAmyloid (mycology)Transmembrane proteinProtein–protein interactionProtein folding
DOInot available

Abstract

fetched live from OpenAlex

Alzheimer's Disease (AD) is a neuropathological disorder characterized by the progressive deposition of insoluble amyloid plaques and vascular deposits consisting primarily of 4.5 kDa amyloid beta peptides (Abeta). There is increasing evidence that the deposition of Abeta fibrils in the brain, an invariable feature of AD, and/or prefibrillar aggregates likely cause neurodegeneration in AD. While Abeta fibrils were a previous research focus, recent experiments implicate prefibrillar aggregates as the toxic species. The identification and characterization of prefibrillar aggregates is of great importance to understanding AD and the development of therapeutic strategies. Biophysical and spectroscopic techniques were used to examine the effects of electrostatic interactions on Abeta oligomerization. Experimental work demonstrated that, while salt bridges likely provide stability to preformed Abeta aggregates, these interactions are not essential for the early stages of aggregation. Abeta oligomerization is driven by the formation of pH-independent interactions and is impeded by electrostatic repulsion at pH values away from the isoelectric point. Diffuse plaques, containing only the 42-residue form of Abeta, are unstructured and non-toxic; they appear before toxic senile plaques containing both 40 and 42-residue forms. Through incubation, Abeta40 and Abeta42 were shown to co-incorporate into unstructured aggregates early during fibrillogenesis later leading to tightly packed aggregates with secondary structure. Previously, the stage at which the Abeta variants co-incorporated during the fibrillogenic process was unknown. After observing that the amyloid precursor protein transmembrane (APP-TM) domain contains two known dimerization motifs (GXXXG/A), oligomerization of the APP-TM domain was examined. A model system was developed to investigate the effects of familial AD mutations on the dimerization propensity of APP-TM domains. This work culminated in the first experimentally supported mechanism to explain how genetic mutations within the APP gene lead to the observed phenotype and predisposition to AD. Further experimentation led to the discovery of non-denaturing detergents that stabilize suspected on-pathway spherical Abeta aggregates. These detergent-stabilized Abeta oligomers share many of the structural features and biological activities of both membrane bound Abeta and spherical oligomers of Abeta formed in solution. Thus, these stabilizing detergents may prove useful in high-resolution structural analysis of spherical oligomers.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame machine prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. The Gemma side is a direct model label for every work in the frame, read from the title-only record. The Codex side is a classifier learned from the 10,348 direct Codex labels and calibrated to design-weighted sample rates; fields without enough sample support carry no Codex call. Candidate is the union of the two sides; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: metacan-v3-hybrid-931329e0061cValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.001
Threshold uncertainty score0.002

Distilled classifier scores by category (both heads)

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0010.001
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0010.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.021
GPT teacher head0.341
Teacher spread0.320 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one source (direct Gemma or distilled Codex), not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations0
Published2006
Admission routes1
Has abstractyes

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