Evidence map›Paper›PMID 7800122›Full record

ReviewNeurochemical research1994

Expression and biological functions of sulfoglucuronyl glycolipids (SGGLs) in the nervous system--a review.

F B Jungalwala

Abstract readReview
PubMed Publisher
In one paragraph

Review in Neurochemical research, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-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

23 citing papers in PubMed, 114 citations in OpenAlex.

  1. Analysis of Lacto/Neolacto-Series Glycolipids and Gangliosides.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  2. Review
  3. Article
  4. Review
  5. Proteins Binding to the Carbohydrate HNK-1: Common Origins?International journal of molecular sciences · 2021
    Article
  6. Article
  7. Review
  8. Glycosylation Changes in Brain Cancer.ACS chemical neuroscience · 2018
    Review
  9. Article
  10. Article
  11. Article
  12. Detection and characterization of a novel subset of CD8⁺CD57⁺ T cells in metastatic melanoma with an incompletely differentiated phenotype.Clinical cancer research : an official journal of the American Association for Cancer Research · 2012
    Article
  13. Review
  14. Article
  15. Biomarkers in Acute Kidney Injury.Biomarker insights · 2008
    Article
  16. Article
  17. Article
  18. Paraproteinaemic neuropathies.Brain pathology (Zurich, Switzerland) · 1999
    Review
  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

1 author at 1 institution in 1 country.

F B JungalwalaDepartment of Biomedical Sciences, Eunice Kennedy Shriver Center, Waltham, MA 02254.
Eunice Kennedy Shriver Center · US

Funding

NEUROBIOLOGY OF SULFATED GLUCURONYL GLYCOCONJUGATESR01NS024405 · NINDS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI JUNGALWALA, FIROZE B · 1987 to 2000
$262k
REGULATION OF LIMB CHONDROGENESISR01HD005505 · NICHD · UNIVERSITY OF IOWA · PI DANIELS, KARLA J · 1985 to 1993
–
NICHD NIH HHS P01 HD 05505NINDS NIH HHS R01 NS 24405
6 · The paper itself

Abstract

Sulfoglucuronyl carbohydrate linked to neolactotetraose reacts with HNK-1 antibody. The HNK-1 carbohydrate epitope is found in two major glycolipids, several glycoproteins and in some proteoglycans of the nervous system. Most of the HNK-1 reactive glycoproteins so far identified are neural cell adhesion molecules and/or are involved in cell-cell interactions. HNK-1 carbohydrate is highly immunogenic. Several HNK-1-like antibodies, including IgM of some patients with plasma cell abnormalities and having peripheral neuropathy, have been described. This article summarizes published work mainly on sulfoglucuronyl glycolipids, SGGLs and covers: structural requirements of the carbohydrate epitope for binding to HNK-1 and human antibodies, expression of the lipids in various neural areas, stage and region specific developmental expression in CNS and PNS, immunocytochemical localization, loss of expression in Purkinje cell abnormality murine mutations, biosynthetic regulation of expression by a single enzyme N-acetylglucosaminyl transferase, identification of receptor-like carbohydrate binding neural proteins (lectins), and perceived role of the carbohydrate in physiological functions. The latter includes role in: pathogenesis of certain peripheral neuropathies, in migration of neural crest cells, as a ligand in cell-cell adhesion/interaction and as a promoter of neurite outgrowth for motor neurons. Multiple expression of HNK-1 carbohydrate in several molecules and in various neural cell types at specific stages of nervous system development has puzzled investigators as to its specific biological function, but this may also suggest its importance in multiple systems during cell differentiation and migration processes.

Indexed as

AnimalsCarbohydrate SequenceCarrier ProteinsGlucuronatesGlycolipidsMiceMolecular Sequence DataMolecular StructureMutationNervous SystemSulfoglycosphingolipidsCarrier ProteinsGlucuronatesGlycolipidssulfoglycolipidsSulfoglycosphingolipids

Identifiers

PMID7800122
OpenAlexW2034740945

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.