Evidence map›Paper›PMID 9335273›Full record

ArticleJournal of bacteriology1997

Altered extent of cross-linking of beta1,6-glucosylated mannoproteins to chitin in Saccharomyces cerevisiae mutants with reduced cell wall beta1,3-glucan content.

J C Kapteyn, A F Ram, E M Groos, R Kollar, R C Montijn, H Van Den Ende, A Llobell, E Cabib, F M Klis

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
15.9field-weighted citation impact, top 1% 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

53 citing papers in PubMed, 183 citations in OpenAlex.

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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

9 authors at 1 institution in 1 country.

J C KapteynInstitute of Molecular Cell Biology, University of Amsterdam, The Netherlands. kapteyn@bio.uva.nl
A F Ram
E M Groos
R Kollar
R C Montijn
H Van Den Ende
A Llobell
E Cabib
F M Klis
University of Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast cell wall contains beta1,3-glucanase-extractable and beta1,3-glucanase-resistant mannoproteins. The beta1,3-glucanase-extractable proteins are retained in the cell wall by attachment to a beta1,6-glucan moiety, which in its turn is linked to beta1,3-glucan (J. C. Kapteyn, R. C. Montijn, E. Vink, J. De La Cruz, A. Llobell, J. E. Douwes, H. Shimoi, P. N. Lipke, and F. M. Klis, Glycobiology 6:337-345, 1996). The beta1,3-glucanase-resistant protein fraction could be largely released by exochitinase treatment and contained the same set of beta1,6-glucosylated proteins, including Cwp1p, as the B1,3-glucanase-extractable fraction. Chitin was linked to the proteins in the beta1,3-glucanase-resistant fraction through a beta1,6-glucan moiety. In wild-type cell walls, the beta1,3-glucanase-resistant protein fraction represented only 1 to 2% of the covalently linked cell wall proteins, whereas in cell walls of fks1 and gas1 deletion strains, which contain much less beta1,3-glucan but more chitin, beta1,3-glucanase-resistant proteins represented about 40% of the total. We propose that the increased cross-linking of cell wall proteins via beta1,6-glucan to chitin represents a cell wall repair mechanism in yeast, which is activated in response to cell wall weakening.

Indexed as

beta-GlucansGlucosyltransferasesSaccharomyces cerevisiae Proteinsbeta-GlucosidaseCell WallChitinEchinocandinsFungal ProteinsGlucan 1,3-beta-GlucosidaseGlucansGlycoside HydrolasesGlycosylationHexosaminidasesMembrane GlycoproteinsMembrane ProteinsSaccharomyces cerevisiaebeta-1,3-glucanbeta-1,6-glucanbeta-Glucansbeta-GlucosidaseChitinCWP1 protein, S cerevisiaeEchinocandinsendo-1,6-beta-glucanaseFKS1 protein, S cerevisiaeFungal ProteinsGAS1 protein, S cerevisiaeGlucan 1,3-beta-GlucosidaseGlucansGlucosyltransferasesGlycoside HydrolasesHexosaminidasesmannoproteinsMembrane GlycoproteinsMembrane ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID9335273
PMCPMC179540
OpenAlexW1875868434

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.