Evidence map›Paper›PMID 19129246›Full record

ArticleGlycobiology2009

Hetero-oligomeric interactions between early glycosyltransferases of the dolichol cycle.

Christine Noffz, Sabine Keppler-Ross, Neta Dean

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

33 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Functions ofJournal of fungi (Basel, Switzerland) · 2025
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. AAQSP increases mapping resolution of stable QTLs through applying NGS-BSA in multiple genetic backgrounds.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2022
    Article
  11. Article
  12. AnFrontiers in cell and developmental biology · 2022
    Article
  13. Article
  14. Frontiers in plant science · 2021
    Article
  15. N-Glycosylation.Advances in experimental medicine and biology · 2021
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Christine NoffzDepartment of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215, USA.
Sabine Keppler-Ross
Neta Dean
Stony Brook University · US

Funding

PROTEIN TARGETING TO THE YEAST GOLGIR01GM048467 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI DEAN, NETA · 1995 to 2006
$2.3M
NIGMS NIH HHS R01-GM048467
6 · The paper itself

Abstract

N-Linked glycosylation begins with the formation of a dolichol-linked oligosaccharide in the endoplasmic reticulum (ER). The first two steps of this pathway lead to the formation of GlcNAc(2)-PP-dolichol, whose synthesis is sequentially catalyzed by the Alg7p GlcNAc phosphotransferase and by the dimeric Alg13p/Alg14p UDP-GlcNAc transferase on the cytosolic face of the endoplasmic reticulum. Here, we show that the Alg7p, Alg13p, and Alg14p glycosyltransferases form a functional multienzyme complex. Coimmunoprecipitation and gel filtration assays demonstrate that the Alg7p/Alg13p/Alg14p complex is a hexamer with a native molecular weight of approximately 200 kDa and an Alg7p:Alg13:Alg14p stoichiometry of 1:1:1. These results highlight and extend the striking parallels that exist between these eukaryotic UDP-GlcNAc transferases and their bacterial MraY and MurG homologs that catalyze the first two steps of the lipid-linked peptidoglycan precursor. In addition to their preferred substrate and lipid acceptors, these enzymes are similar in their structure, chemistry, temporal, and spatial organization. These similarities point to an evolutionary link between the early steps of N-linked glycosylation and those of peptidoglycan synthesis.

Indexed as

DolicholsEndoplasmic ReticulumGlycosylationGlycosyltransferasesN-AcetylglucosaminyltransferasesProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDolicholsGlycosyltransferasesN-AcetylglucosaminyltransferasesSaccharomyces cerevisiae ProteinsUDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase

Identifiers

PMID19129246
PMCPMC2667158
OpenAlexW2139932029

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.