Evidence map›Paper›PMID 26203194›Full record

ArticleThe Journal of biological chemistry2015

Structural Aspects of N-Glycosylations and the C-terminal Region in Human Glypican-1.

Wael Awad, Barbara Adamczyk, Jessica Örnros, Niclas G Karlsson, Katrin Mani, Derek T Logan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.3field-weighted citation impact, top 39% 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

22 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
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  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. The function of glypicans in the mammalian embryo.American journal of physiology. Cell physiology · 2022
    Review
  12. Role of glypican-1 in regulating multiple cellular signaling pathways.American journal of physiology. Cell physiology · 2021
    Review
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Extracellular Vesicles and Glycosylation.Advances in experimental medicine and biology · 2021
    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

6 authors at 2 institutions in 1 country.

Wael AwadFrom the Department of Biochemistry and Structural Biology, Centre for Molecular Protein Science, Lund University, Box 124, SE-221 00 Lund.
Barbara Adamczykthe Department of Biochemistry and Cell Biology, University of Gothenburg, Box 440, SE-40530 Gothenburg, and.
Jessica Örnrosthe Department of Biochemistry and Cell Biology, University of Gothenburg, Box 440, SE-40530 Gothenburg, and.
Niclas G Karlssonthe Department of Biochemistry and Cell Biology, University of Gothenburg, Box 440, SE-40530 Gothenburg, and.
Katrin Manithe Department of Experimental Medical Science, Lund University, SE-221 84, Lund, Sweden.
Derek T LoganFrom the Department of Biochemistry and Structural Biology, Centre for Molecular Protein Science, Lund University, Box 124, SE-221 00 Lund, derek.logan@biochemistry.lu.se.ORCID http://orcid.org/0000-0002-0098-8560
Lund University · SEUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glypicans are multifunctional cell surface proteoglycans involved in several important cellular signaling pathways. Glypican-1 (Gpc1) is the predominant heparan sulfate proteoglycan in the developing and adult human brain. The two N-linked glycans and the C-terminal domain that attach the core protein to the cell membrane are not resolved in the Gpc1 crystal structure. Therefore, we have studied Gpc1 using crystallography, small angle x-ray scattering, and chromatographic approaches to elucidate the composition, structure, and function of the N-glycans and the C terminus and also the topology of Gpc1 with respect to the membrane. The C terminus is shown to be highly flexible in solution, but it orients the core protein transverse to the membrane, directing a surface evolutionarily conserved in Gpc1 orthologs toward the membrane, where it may interact with signaling molecules and/or membrane receptors on the cell surface, or even the enzymes involved in heparan sulfate substitution in the Golgi apparatus. Furthermore, the N-glycans are shown to extend the protein stability and lifetime by protection against proteolysis and aggregation.

Indexed as

AdultCrystallography, X-RayGlycosylationGlypicansHEK293 CellsHumansProtein Structure, TertiaryGlypicansglypican-1glypicansmass spectrometry (MS)membrane-anchored proteinN-linked glycosylationproteoglycansmall angle x-ray scattering (SAXS)structure-function

Identifiers

PMID26203194
PMCPMC4645609
OpenAlexW1055306509

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.