Evidence map›Paper›PMID 1379729›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats.

J Way, M R Hellmich, H Jaffe, B Szaro, H C Pant, H Gainer, J Battey

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

12 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
  2. Article
  3. Squid Giant Axons Synthesize NF Proteins.Molecular neurobiology · 2018
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Active polysomes are present in the large presynaptic endings of the synaptosomal fraction from squid brain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1997
    Article
  9. Phosphorylation and subunit organization of axonal neurofilaments determined by scanning transmission electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 1997
    Article
  10. Article
  11. Article
  12. 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 3 institutions in 1 country.

J WayLaboratory of Neurochemistry, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
M R Hellmich
H Jaffe
B Szaro
H C Pant
H Gainer
J Battey
National Institute of Neurological Disorders and Stroke · USMarine Biological Laboratory · USNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Previous studies have shown that two low molecular-weight neurofilament (NF) proteins (NF-60 and NF-70) from the squid Loligo pealei are translated from mRNAs that are splice variants of a single squid NF gene. In this study, we report the isolation and characterization of cDNA clones encoding a high-molecular-weight squid NF protein (NF-220), the mRNA of which derives from the same squid NF gene. All three proteins are identical in their amino-terminal and lamin-like rod domains but differ in their carboxyl-terminal tail regions. In contrast to the short tail domains of NF-60 and NF-70, the NF-220 protein has a longer tail domain containing an acidic cluster of amino acids immediately followed by repeated copies of the sequence motif Lys-Ser-Pro. The Lys-Ser-Pro domain is similar to that of mammalian medium NF (NF-M) and high NF (NF-H) proteins, where the serines are highly phosphorylated. Except for these Lys-Ser-Pro motifs, there is surprisingly little structural similarity between the squid NF-220 protein and mammalian NF-M and NF-H proteins. Furthermore, the location of introns in squid NF-220 protein shows that it is more closely related to nuclear lamins and type III intermediate-filament proteins than to vertebrate NF proteins.

Indexed as

Amino Acid SequenceAnimalsDecapodiformesDNAGenomic LibraryHumansIntronsLaminsMammalsMolecular Sequence DataMolecular WeightMusclesNervous System Physiological PhenomenaNeurofilament ProteinsNuclear ProteinsRepetitive Sequences, Nucleic AcidDNALaminsNeurofilament ProteinsNuclear ProteinsRNARNA, Messenger

Identifiers

PMID1379729
PMCPMC49625
OpenAlexW2032169912

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.