Evidence map›Paper›PMID 28000086›Full record

ArticleCell stress & chaperones2017

Interaction of small heat shock proteins with light component of neurofilaments (NFL).

Victoria V Nefedova, Maria V Sudnitsyna, Nikolai B Gusev

Open access · bronzeAbstract read
In one paragraph

Article in Cell stress & chaperones, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.9field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Heat Shock Proteins in Tooth Development and Injury Repair.International journal of molecular sciences · 2023
    Review
  3. Neurofilaments in health and Charcot-Marie-Tooth disease.Frontiers in cell and developmental biology · 2023
    Review
  4. The J Domain of Sacsin Disrupts Intermediate Filament Assembly.International journal of molecular sciences · 2022
    Article
  5. Review
  6. Review
  7. Article
  8. Mutations in HspB1 and hereditary neuropathies.Cell stress & chaperones · 2020
    Review
  9. Review
  10. Article
  11. Homeostatic Roles of the Proteostasis Network in Dendrites.Frontiers in cellular neuroscience · 2020
    Review
  12. Article
  13. Article
  14. Review
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 1 institution in 1 country.

Victoria V NefedovaDepartment of Biochemistry, School of Biology, Moscow State University, Moscow, Russian Federation, 119991.
Maria V SudnitsynaDepartment of Biochemistry, School of Biology, Moscow State University, Moscow, Russian Federation, 119991.
Nikolai B GusevDepartment of Biochemistry, School of Biology, Moscow State University, Moscow, Russian Federation, 119991. NBGusev@mail.ru.
Lomonosov Moscow State University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction of human small heat shock protein HspB1, its point mutants associated with distal hereditary motor neuropathy, and three other small heat shock proteins (HspB5, HspB6, HspB8) with the light component of neurofilaments (NFL) was analyzed by differential centrifugation, analytical ultracentrifugation, and fluorescent spectroscopy. The wild-type HspB1 decreased the quantity of NFL in pellets obtained after low- and high-speed centrifugation and increased the quantity of NFL remaining in the supernatant after high-speed centrifugation. Part of HspB1 was detected in the pellet of NFL after high-speed centrifugation, and at saturation, 1 mol of HspB1 monomer was bound per 2 mol of NFL. Point mutants of HspB1 associated with distal hereditary motor neuropathy (G84R, L99M, R140G, K141Q, and P182S) were almost as effective as the wild-type HspB1 in modulation of NFL assembly. At low ionic strength, HspB1 weakly interacted with NFL tetramers, and this interaction was increased upon salt-induced polymerization of NFL. HspB1 and HspB5 (αB-crystallin) decreased the rate of NFL polymerization measured by fluorescent spectroscopy. HspB6 (Hsp20) and HspB8 (Hsp22) were less effective than HspB1 (or HspB5) in modulation of NFL assembly. The data presented indicate that the small heat shock proteins affect NFL transition from tetramers to filaments, hydrodynamic properties of filaments, and their bundling and therefore probably modulate the formation of intermediate filament networks in neurons.

Indexed as

Heat-Shock ProteinsHeat-Shock Proteins, SmallHSP27 Heat-Shock ProteinsHumansIntermediate FilamentsMolecular ChaperonesMuscular Atrophy, SpinalNeuronsPoint MutationProtein Interaction MapsHeat-Shock ProteinsHeat-Shock Proteins, SmallHSP27 Heat-Shock ProteinsHSPB1 protein, humanMolecular ChaperonesCytoskeletonIntermediate filamentsNeurodegenerative diseasesNeurofilamentsSmall heat shock proteins

Identifiers

PMID28000086
PMCPMC5465025
OpenAlexW2567439893

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.