Evidence map›Paper›PMID 28637867›Full record

ArticleThe Journal of biological chemistry2017

Full-length cellular β-secretase has a trimeric subunit stoichiometry, and its sulfur-rich transmembrane interaction site modulates cytosolic copper compartmentalization.

Filip Liebsch, Mark R P Aurousseau, Tobias Bethge, Hugo McGuire, Silvia Scolari, Andreas Herrmann, Rikard Blunck, Derek Bowie, Gerd Multhaup

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 24 citations in OpenAlex.

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  5. Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Filip LiebschFrom the Integrated Program in Neuroscience, McGill University, Montreal, Quebec H3G 0B1, Canada.ORCID 0000-0002-0955-8065
Mark R P Aurousseauthe Department of Pharmacology & Therapeutics, McGill University, Montreal, Quebec H3G 1Y6, Canada.
Tobias Bethgethe Institut für Chemie und Biochemie, Freie Universität Berlin, 14195 Berlin, Germany.
Hugo McGuirethe Department of Physics, Université de Montréal, Montreal, Quebec H3C 3J7, Canada, and.
Silvia Scolarithe Institut für Biologie, Humboldt Universität zu Berlin, 10115 Berlin, Germany.
Andreas Herrmannthe Institut für Biologie, Humboldt Universität zu Berlin, 10115 Berlin, Germany.
Rikard Blunckthe Department of Physics, Université de Montréal, Montreal, Quebec H3C 3J7, Canada, and.
Derek BowieFrom the Integrated Program in Neuroscience, McGill University, Montreal, Quebec H3G 0B1, Canada.
Gerd MulthaupFrom the Integrated Program in Neuroscience, McGill University, Montreal, Quebec H3G 0B1, Canada, gerhard.multhaup@mcgill.ca.
McGill University · CAHumboldt-Universität zu Berlin · DEUniversité de Montréal · CAFreie Universität Berlin · DE

Funding

CIHR MOP 136894
6 · The paper itself

Abstract

The β-secretase (BACE1) initiates processing of the amyloid precursor protein (APP) into Aβ peptides, which have been implicated as central players in the pathology of Alzheimer disease. BACE1 has been described as a copper-binding protein and its oligomeric state as being monomeric, dimeric, and/or multimeric, but the native cellular stoichiometry has remained elusive. Here, by using single-molecule fluorescence and

Indexed as

Models, MolecularAlanineAmino Acid SubstitutionAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBacterial ProteinsBiological TransportCopperCysteineCytosolFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHEK293 CellsHumansLuminescent ProteinsMicroscopy, FluorescenceAlanineAmyloid Precursor Protein SecretasesAspartic Acid EndopeptidasesBACE1 protein, humanBacterial ProteinsCopperCyan Fluorescent ProteinCysteineGreen Fluorescent ProteinsLuminescent ProteinsRecombinant Fusion Proteinsyellow fluorescent protein, Bacteriabeta-secretase 1 (BACE1)copper transportprotein cross-linkingsingle-molecule biophysicsstoichiometry

Identifiers

PMID28637867
PMCPMC5555187
OpenAlexW2690315019

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.