Evidence map›Paper›PMID 28869595›Full record

ArticleNature chemical biology2017

A toxic mutant huntingtin species is resistant to selective autophagy.

Yuhua Fu, Peng Wu, Yuyin Pan, Xiaoli Sun, Huiya Yang, Marian Difiglia, Boxun Lu

Abstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Autophagy-NADFrontiers in molecular biosciences · 2025
    Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Emerging New Concepts of Degrader Technologies.Trends in pharmacological sciences · 2020
    Review
  18. Autophagy in Neurodegenerative Diseases: A Hunter for Aggregates.International journal of molecular sciences · 2020
    Review
  19. Review
  20. Article
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

7 authors at 2 institutions in 2 countries.

Yuhua FuState Key Laboratory of Medical Neurobiology, Neurology Department at Huashan Hospital, School of Life Sciences, Fudan University, Shanghai, China.
Peng WuState Key Laboratory of Medical Neurobiology, Neurology Department at Huashan Hospital, School of Life Sciences, Fudan University, Shanghai, China.
Yuyin PanState Key Laboratory of Medical Neurobiology, Neurology Department at Huashan Hospital, School of Life Sciences, Fudan University, Shanghai, China.
Xiaoli SunState Key Laboratory of Medical Neurobiology, Neurology Department at Huashan Hospital, School of Life Sciences, Fudan University, Shanghai, China.
Huiya YangState Key Laboratory of Medical Neurobiology, Neurology Department at Huashan Hospital, School of Life Sciences, Fudan University, Shanghai, China.
Marian DifigliaMassGeneral Institute for Neurodegenerative Diseases, Massachusetts General Hospital, Boston, USA.
Boxun LuState Key Laboratory of Medical Neurobiology, Neurology Department at Huashan Hospital, School of Life Sciences, Fudan University, Shanghai, China.ORCID http://orcid.org/0000-0002-1675-9340
Fudan University · CNMassachusetts General Hospital · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein misfolding is a common theme in neurodegenerative disorders including Huntington's disease (HD). The HD-causing mutant huntingtin protein (mHTT) has an expanded polyglutamine (polyQ) stretch that may adopt multiple conformations, and the most toxic of these is the one recognized by antibody 3B5H10. Here we show that the 3B5H10-recognized mHTT species has a slower degradation rate due to its resistance to selective autophagy in human cells and brains, revealing mechanisms of its higher toxicity.

Indexed as

AutophagyMutationBrainCells, CulturedFibroblastsHumansHuntingtin ProteinHuntington DiseasePeptidesPolyubiquitinProtein ConformationProteolysisRepetitive Sequences, Nucleic AcidUbiquitinationHuntingtin ProteinPeptidespolyglutaminePolyubiquitin

Identifiers

PMID28869595
OpenAlexW2752458922

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.