Evidence map›Paper›PMID 14676317›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

Genetic, biochemical, and morphological evidence for the involvement of N-glycosylation in biosynthesis of the cell wall beta1,6-glucan of Saccharomyces cerevisiae.

Manasi Chavan, Tadashi Suzuki, Magdalena Rekowicz, William Lennarz

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

13 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Candida albicans cell wall proteins.Microbiology and molecular biology reviews : MMBR · 2008
    Review
  10. Article
  11. Article
  12. Cell wall assembly in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2006
    Review
  13. 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

4 authors at 1 institution in 1 country.

Manasi ChavanDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794, USA.
Tadashi Suzuki
Magdalena Rekowicz
William Lennarz
Stony Brook University · US

Funding

ENZYMATIC CONVERSION OF PROTEINS TO GLYCOPROTEINSR01GM033185 · NIGMS · UNIVERSITY OF TEXAS MD ANDERSON CAN CTR · PI LENNARZ, WILLIAM J · 1985 to 2007
$1.5M
ENZYMATIC CONVERSION OF PROTEINS TO GLYCOPROTEINSR37GM033185 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI LENNARZ, WILLIAM J · 1990 to 1999
–
NIGMS NIH HHS GM33185NIGMS NIH HHS R01 GM033185NIGMS NIH HHS R37 GM033185
6 · The paper itself

Abstract

Recent evidence indicates that Stt3p plays a central role in the recognition and/or catalytic step in N-glycosylation (asparagine-linked glycosylation) in the lumen of the endoplasmic reticulum. It is known that stt3 mutants exhibit certain phenotypic features that are suggestive of a cell wall defect. To understand the basis of these phenotypes, we devised a genetic screen to isolate strains bearing mutations that lead to synthetic lethality in combination with the stt3-1 mutation. Using this screen, we were surprised to identify two KRE genes (KRE5 and KRE9) that are involved in the biosynthesis of the cell wall beta1,6-glucan. This finding led us to propose that the N-glycosylation process is essential in the biosynthesis of cell wall beta1,6-glucan. This proposal was supported by the observation that several stt3 mutants exhibited a 60-70% reduction in the content of cell wall beta1,6-glucan as compared with WT cells. Transmission electron microscopy revealed that the stt3 mutant strains exhibit a diffused cell wall with loss of the outer mannoprotein layer as compared with the WT cells. Thus, we provide genetic, morphological, and biochemical evidence for the critical involvement of N-glycosylation in some step in assembly of the cell wall beta1,6-glucan in Saccharomyces cerevisiae.

Indexed as

beta-GlucansBase SequenceCell WallCloning, MolecularDNA PrimersEscherichia coliGenes, LethalGlucansGlycoproteinsGlycosylationMutationPhenotypePolymerase Chain ReactionSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsbeta-1,6-glucanbeta-GlucansDNA PrimersGlucansGlycoproteinsKRE5 protein, S cerevisiaeKRE9 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID14676317
PMCPMC307576
OpenAlexW1969043041

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.