Evidence map›Paper›PMID 1452459›Full record

ArticleJapanese journal of cancer research : Gann1992

Altered glycosylation of membrane glycoproteins associated with human mammary carcinoma.

S Hiraizumi, S Takasaki, N Ohuchi, Y Harada, M Nose, S Mori, A Kobata

Abstract readComparative Study
In one paragraph

Article in Japanese journal of cancer research : Gann, 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
0.3field-weighted citation impact, top 49% 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, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Glycosylation Changes in Brain Cancer.ACS chemical neuroscience · 2018
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
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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 2 institutions in 1 country.

S HiraizumiDepartment of Biochemistry, University of Tokyo.
S Takasaki
N Ohuchi
Y Harada
M Nose
S Mori
A Kobata
Tohoku University · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-Linked sugar chains of normal mammary gland, mammary carcinomas (primary lesion), and axillary lymph node metastases of mammary carcinomas were released from their membrane preparations by hydrazinolysis and their structures were analyzed. Fractionation using a Datura stramonium agglutinin (DSA)-Sepharose column revealed that the metastasized carcinomas contain more than twice as much DSA-binding oligosaccharides as the normal gland, and the primary carcinomas contain an intermediate amount. These oligosaccharides were elucidated to have tri- and tetraantennary structures containing the GlcNAc beta 1-->6(GlcNAc beta 1-->2)Man group with and without N-acetyllactosamine repeating units. Lectin blot analysis of membrane glycoproteins and histochemical staining of tissues using biotinylated DSA indicated that these glycosylation changes predominantly occur in a limited number of glycoproteins with apparent molecular weights of 90, 160, and 210 kilodaltons, and mammary carcinomas are distinguishable from normal gland by their intense intracytoplasmic staining.

Indexed as

Plant LectinsAcrylic ResinsBreastBreast NeoplasmsCarbohydrate ConformationCarbohydrate SequenceCell MembraneChromatographyElectrophoresis, PaperFemaleGlycosylationHistocytochemistryHumansLectinsLymphatic MetastasisMembrane GlycoproteinsAcrylic ResinsBio-Gel P-4Datura stramonium lectinLectinsMembrane GlycoproteinsPlant LectinsPolysaccharides

Identifiers

PMID1452459
PMCPMC5918672
OpenAlexW2031615787

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.