Implications of the Orb2 Amyloid Structure in Huntington's Disease.

Rubén Hervás, Alexey G Murzin, Kausik Si

Open access · goldAbstract readReview

In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

0.3field-weighted citation impact, top 48% 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

0 citing papers in PubMed, 4 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 2 institutions in 2 countries.

Rubén HervásStowers Institute for Medical Research, Kansas City, MO 64110, USA.ORCID 0000-0001-6393-6058

Alexey G MurzinMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.

Kausik SiStowers Institute for Medical Research, Kansas City, MO 64110, USA.

Stowers Institute for Medical Research · USMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105192716

6 · The paper itself

Abstract

Huntington's disease is a progressive, autosomal dominant, neurodegenerative disorder caused by an expanded CAG repeat in the huntingtin gene. As a result, the translated protein, huntingtin, contains an abnormally long polyglutamine stretch that makes it prone to misfold and aggregating. Aggregation of huntingtin is believed to be the cause of Huntington's disease. However, understanding on how, and why, huntingtin aggregates are deleterious has been hampered by lack of enough relevant structural data. In this review, we discuss our recent findings on a glutamine-based functional amyloid isolated from

Indexed as

AmyloidAnimalsDrosophila melanogasterDrosophila ProteinsHumansHuntington DiseasemRNA Cleavage and Polyadenylation FactorsTranscription FactorsAmyloidDrosophila ProteinsmRNA Cleavage and Polyadenylation FactorsOrb2 protein, DrosophilaTranscription FactorsCPEBCryo-EMfunctional amyloidshuntingtinHuntington’s diseaseOrb2polyglutamine

Identifiers

PMID32967102

DOI10.3390/ijms21186910

PMCPMC7555547

OpenAlexW3087154063

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.