Evidence map›Paper›PMID 2925792›Full record

ArticleThe Journal of cell biology1989

Assembly and exchange of intermediate filament proteins of neurons: neurofilaments are dynamic structures.

K J Angelides, K E Smith, M Takeda

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

29 citing papers in PubMed, 127 citations in OpenAlex.

  1. Vimentin Intermediate Filaments: A Paradigm Shift From Static Structure to Dynamic Cytoplasmic Network.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Review
  3. Article
  4. Neurofilaments and Neurofilament Proteins in Health and Disease.Cold Spring Harbor perspectives in biology · 2017
    Review
  5. Review
  6. Flow birefringence property of desmin filaments.Biophysics (Nagoya-shi, Japan) · 2012
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

3 authors at 1 institution in 1 country.

K J AngelidesDepartment of Physiology and Molecular Biophysics, Baylor College of Medicine, Houston, Texas 77030.
K E Smith
M Takeda
Baylor College of Medicine · US

Funding

STRUCTURAL/KINETIC/CELLULAR MAPPING--NA+ CHANNELK04NS001218 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI ANGELIDES, KIMON J · 1987 to 1991
–
STRUCTURAL, KINETIC, AND CELLULAR MAPPING OF THE NAT+ CHR01NS024606 · NINDS · BAYLOR COLLEGE OF MEDICINE · PI ANGELIDES, KIMON J · 1986 to 1990
–
NINDS NIH HHS NS 01218NINDS NIH HHS NS 24606
6 · The paper itself

Abstract

We have explored the dynamics of intermediate filament assembly and subunit exchange using fluorescently labeled neurofilament proteins and a fluorescence resonance energy transfer assay. Neurofilaments (NFs) are assembled from three highly phosphorylated proteins with molecular masses of 180 (NF-H), 130 (NF-M), and 66 kD (NF-L) of which NF-L forms the structural core. The core component, NF-L, was stoichiometrically labeled at cysteine 321 with fluorescein, coumarin, or biotin-maleimide to produce assembly-competent fluorescent or biotinylated derivatives, respectively. Using coumarin-labeled NF-L as fluorescence donor and fluorescein-labeled NF-L as the fluorescence acceptor, assembly of NF filaments was induced by rapidly raising the NaCl concentration to 170 mM, and the kinetics was followed by the decrease in the donor fluorescence. Assembly of NF-L subunits into filaments does not require nucleotide binding or hydrolysis but is strongly dependent on ionic strength, pH, and temperature. The critical concentration of NF-L, that concentration that remains unassembled at equilibrium with fully formed filaments, is 38 micrograms/ml or 0.6 microM. Under physiological salt conditions NF-L filaments also undergo extensive subunit exchange. Kinetic analysis and evaluation of several possible mechanisms indicate that subunit exchange is preceded by dissociation of subunits from the filament and generation of a kinetically active pool of soluble subunits. Given the concentration of NF-L found in nerve cells and the possibility of regulating this pool, these results provide the first information that intermediate filaments are dynamic structures and that NF-L within the NF complex is in dynamic equilibrium with a small but kinetically active pool of unassembled NF-L units.

Indexed as

AnimalsCattleCytoskeletonIntermediate Filament ProteinsIntermediate FilamentsKineticsMacromolecular SubstancesMicroscopy, ElectronPhosphoproteinsSpinal CordIntermediate Filament ProteinsMacromolecular SubstancesPhosphoproteins

Identifiers

PMID2925792
PMCPMC2115529
OpenAlexW2004086215

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.