Evidence map›Paper›PMID 8253847›Full record

ArticleThe Journal of cell biology1993

The rod domain of NF-L determines neurofilament architecture, whereas the end domains specify filament assembly and network formation.

S Heins, P C Wong, S Müller, K Goldie, D W Cleveland, U Aebi

Abstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Intramolecular structural heterogeneity altered by long-range contacts in an intrinsically disordered protein.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Genetic and clinical characteristics ofJournal of neurology, neurosurgery, and psychiatry · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. MSC p43 required for axonal development in motor neurons.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  18. Article
  19. Article
  20. 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

6 authors.

S HeinsM.E. Müller Institute at the Biocenter, University of Basel, Switzerland.
P C Wong
S Müller
K Goldie
D W Cleveland
U Aebi

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neurofilaments, assembled from NF-L, NF-M, and NF-H subunits, are the most abundant structural elements in myelinated axons. Although all three subunits contain a central, alpha-helical rod domain thought to mediate filament assembly, only NF-L self-assembles into 10-nm filaments in vitro. To explore the roles of the central rod, the NH2-terminal head and the COOH-terminal tail domain in filament assembly, full-length, headless, tailless, and rod only fragments of mouse NF-L were expressed in bacteria, purified, and their structure and assembly properties examined by conventional and scanning transmission electron microscopy (TEM and STEM). These experiments revealed that in vitro assembly of NF-L into bona fide 10-nm filaments requires both end domains: whereas the NH2-terminal head domain promotes lateral association of protofilaments into protofibrils and ultimately 10-nm filaments, the COOH-terminal tail domain controls lateral assembly of protofilaments so that it terminates at the 10-nm filament level. Hence, the two end domains of NF-L have antagonistic effects on the lateral association of protofilaments into higher-order structures, with the effect of the COOH-terminal tail domain being dominant over that of the NH2-terminal head domain. Consideration of the 21-nm axial beading commonly observed with 10-nm filaments, the approximate 21-nm axial periodicity measured on paracrystals, and recent cross-linking data combine to support a molecular model for intermediate filament architecture in which the 44-46-nm long dimer rods overlap by 1-3-nm head-to-tail, whereas laterally they align antiparallel both unstaggered and approximately half-staggered.

Indexed as

AnimalsCattleIntermediate FilamentsIn Vitro TechniquesMacromolecular SubstancesMiceMicroscopy, ElectronNeurofilament ProteinsProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsStructure-Activity RelationshipMacromolecular SubstancesNeurofilament ProteinsRecombinant Proteins

Identifiers

PMID8253847
PMCPMC2290863

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Registered trials

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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.