Evidence map›Paper›PMID 16754853›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Dimeric organization of the yeast oligosaccharyl transferase complex.

Manasi Chavan, Zhiqiang Chen, Guangtao Li, Hermann Schindelin, William J Lennarz, Huilin Li

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Generation and degradation of free asparagine-linked glycans.Cellular and molecular life sciences : CMLS · 2015
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  13. Article
  14. Article
  15. Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  16. Article
  17. 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

6 authors at 3 institutions in 2 countries.

Manasi ChavanDepartment of Biochemistry and Cell Biology and Institute for Cell and Developmental Biology, Stony Brook University, Stony Brook, NY 11794, USA.
Zhiqiang Chen
Guangtao Li
Hermann Schindelin
William J Lennarz
Huilin Li
Stony Brook University · USUniversity of Würzburg · DEBrookhaven National Laboratory · US

Funding

The Structural Basis of Eukaryotic Replication Origin Licensing by Cryo-EMR01GM074985 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI LI, HUILIN · 2006 to 2010
$1.7M
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

The enzyme complex oligosaccharyl transferase (OT) catalyzes N-glycosylation in the lumen of the endoplasmic reticulum. The yeast OT complex is composed of nine subunits, all of which are transmembrane proteins. Several lines of evidence, including our previous split-ubiquitin studies, have suggested an oligomeric organization of the OT complex, but the exact oligomeric nature has been unclear. By FLAG epitope tagging the Ost4p subunit of the OT complex, we purified the OT enzyme complex by using the nondenaturing detergent digitonin and a one-step immunoaffinity technique. The digitonin-solubilized OT complex was catalytically active, and all nine subunits were present in the enzyme complex. The purified OT complex had an apparent mass of approximately 500 kDa, suggesting a dimeric configuration, which was confirmed by biochemical studies. EM showed homogenous individual particles and revealed a dimeric structure of the OT complexes that was consistent with our biochemical studies. A 3D structure of the dimeric OT complex at 25-A resolution was reconstructed from EM images. We suggest that the dimeric structure of OT might be required for effective association with the translocon dimer and for its allosteric regulation during cotranslational glycosylation.

Indexed as

Protein Structure, QuaternaryAnimalsDimerizationHexosyltransferasesImage Processing, Computer-AssistedMembrane ProteinsMicroscopy, ElectronModels, MolecularMultiprotein ComplexesProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsdolichyl-diphosphooligosaccharide - protein glycotransferaseHexosyltransferasesMembrane ProteinsMultiprotein ComplexesProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID16754853
PMCPMC1482546
OpenAlexW2069888921

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.