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Record W2085337366 · doi:10.1001/archneurol.2009.29

Brain Traffic

2009· letter· en· W2085337366 on OpenAlexfundno aff
Richard Mayeux, Peter St George‐Hyslop

Bibliographic record

VenueArchives of Neurology · 2009
Typeletter
Languageen
FieldMedicine
TopicAlzheimer's disease research and treatments
Canadian institutionsnot available
FundersCanadian Institutes of Health ResearchNational Institute on AgingNational Institutes of HealthWellcome TrustHoward Hughes Medical Institute
KeywordsMedicineNeurologyOtorhinolaryngologyFamily medicinePsychiatry

Abstract

fetched live from OpenAlex

The progression from proteolysis of the amyloid precursor protein (APP) to the formation of aggregated amyloid- peptide (A) deposits forms the basis of the amyloid hypothesis for the pathogenesis of Alzheimer disease. 1 Key steps in APP processing occur in subcellular compartments. Amyloid- is one of several end products that originate from the sequential proteolysis by -secretase and -secretase cleavage of the transmembrane APP. While A can range in size from 37 to 43 amino acids, it is the A 42 peptide that appears to be the foundation of fibrillar plaque formation in the brains of patients with Alzheimer disease. Alterations in the intracellular transport of APP can directly influence whether APP undergoes -secretase enzymatic activity, releasing a nontoxic peptide, -secretase-cleaved soluble APP (sAPP), or follows -secretase and -secretase enzymatic pathways, leading to generation of the neurotoxic forms of A. While the -secretase enzymes are found at the cell surface, -secretase lies within the Golgi apparatus and endosomes, the -secretase complex in the endoplasmic reticulum, lysosomes, and the cell surface. When APP is moved into the endosome, it is cleaved by -secretase and then transported either to the cell surface or to the lysosome to be further processed by -secretase to form A. However, when APP accumulates at the cell surface, it has a greater chance of interacting with -secretase to form nonamyloid-forming sAPP. SORL1 (also known as LR11 and SorLA) is 1 of several members of the low-density lipoprotein receptor family that interact and influence the cellular localization and processing of APP. SORL1 is a highly conserved type 1 receptor with vacuolar protein sorting and lowdensity lipoprotein-receptor class A and fibronectin domains. The low-density lipoproteinreceptor domain also serves as a binding site for apolipoprotein E. A single transmembrane domain carries a motif that specifically mediates SORL1 interaction with proteins involved in Golgi apparatus and endosome sorting of proteins, such as APP. An inherent modification in SORL1 enables it to control the clearance of some glycoproteins, modulate interactions with other proteins, and influence intracellular trafficking. 1 SORL1 and APP are colocalized within the perinuclear region of neurons and, when coexpressed in vitro, result in a complex formation in which there is SORL1-dependent translocation of APP.2 The active receptors for SORL1 are in the Golgi network as well as the endosome, further supporting an influential role in intracellular trafficking of APP. It has been suggested that SORL1 acts as a regulatory gate keeper for the amyloidogenic and nonamyloidogenic pathways, determining the ultimate destination for APP.2 , 3 When SORL1 effectively binds with APP, there is a reduction in sAPP and A, but when deficient, as in SORL1-knockout mice, the result is high levels of sAPP and A. 2 In a cell culture, Anderson et al 2 demonstrated that by increasing SORL1

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 distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Not applicable · Consensus signal: Not applicable
GenreCandidate signal: Commentary · Consensus signal: Commentary
Teacher disagreement score0.043
Threshold uncertainty score0.820

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0010.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.001
Insufficient payload (model declined to judge)0.0000.000

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 head0.022
GPT teacher head0.295
Teacher spread0.273 · 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 teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designNot applicable
Domainnot available
GenreCommentary

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

Citations7
Published2009
Admission routes1
Has abstractyes

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