Evidence map›Paper›PMID 8425897›Full record

ArticleThe Journal of cell biology1993

Breaching the diffusion barrier that compartmentalizes the transmembrane glycoprotein CE9 to the posterior-tail plasma membrane domain of the rat spermatozoon.

C L Nehme, M M Cesario, D G Myles, D E Koppel, J R Bartles

Open access · bronzeAbstract read
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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
5.4field-weighted citation impact, top 5% 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

19 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Importance of N-glycosylation on CD147 for its biological functions.International journal of molecular sciences · 2014
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Basigin-2 is a cell surface receptor for soluble basigin ligand.The Journal of biological chemistry · 2008
    Article
  13. Review
  14. Review
  15. Article
  16. Article
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  18. Article
  19. 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

5 authors at 1 institution in 1 country.

C L NehmeDepartment of Cell, Molecular and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.
M M Cesario
D G Myles
D E Koppel
J R Bartles
Northwestern University · US

Funding

REGULATION OF CE 9 PROTEIN BY PEROXISOME PROLIFERATORSR01CA053997 · NCI · NORTHWESTERN UNIVERSITY · PI BARTLES, JAMES R · 1991 to 1993
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MEMBRANE DYNAMICS OF LOCOMOTING TISSUE CELLSR01GM023585 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI KOPPEL, DENNIS E · 1985 to 1995
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REMODELING OF SPERMATOZOA PLASMA MEMBRANE DOMAINSR01HD028977 · NICHD · NORTHWESTERN UNIVERSITY · PI BARTLES, JAMES R · 1992 to 1994
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NCI NIH HHS CA 53997NICHD NIH HHS HD 28977NIGMS NIH HHS GM 23585
6 · The paper itself

Abstract

CE9 is a posterior-tail domain-specific integral plasma membrane glycoprotein of the rat testicular spermatozoon. During epididymal maturation, CE9 undergoes endoproteolytic processing and then redistributes into the anterior-tail plasma membrane domain of the spermatozoon (Petruszak, J. A. M., C. L. Nehme, and J. R. Bartles. 1991. J. Cell. Biol. 114:917-927). We have determined the sequence of CE9 and found it to be a Type Ia transmembrane protein identical to the MRC OX-47 T-cell activation antigen, a member of the immunoglobulin superfamily predicted to have two immunoglobulin-related loops and three asparagine-linked glycans disposed extracellularly. Although encoded by a single gene and mRNA in the rat, the majority of spermatozoal CE9 is of smaller apparent molecular mass than its hepatocytic counterpart due to the under-utilization of sites for asparagine-linked glycosylation. By fluorescence recovery after photobleaching, CE9 was determined to be mobile within the posterior-tail plasma membrane domain of the living rat testicular spermatozoon, thus implying the existence of a regional barrier to lateral diffusion that is presumed to operate at the level of the annulus. Through the development of an in vitro system, the modification of this diffusion barrier to allow for the subsequent redistribution of CE9 into the anterior-tail domain was found to be a time-, temperature-, and energy-dependent process.

Indexed as

Antigens, SurfaceAmino Acid SequenceAnimalsBase SequenceBasiginBlood ProteinsDiffusionDNAFluorescent Antibody TechniqueGlycosylationKineticsMaleMembrane GlycoproteinsMolecular Sequence DataRatsRats, Inbred F344Antigens, SurfaceBasiginBlood ProteinsBsg protein, ratDNAMembrane Glycoproteins

Identifiers

PMID8425897
PMCPMC2119531
OpenAlexW2147656241

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.