Evidence map›Paper›PMID 1824724›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1991

Molecular cloning and expression of cDNA encoding the enzyme that controls conversion of high-mannose to hybrid and complex N-glycans: UDP-N-acetylglucosamine: alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.

M Sarkar, E Hull, Y Nishikawa, R J Simpson, R L Moritz, R Dunn, H Schachter

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 121 citations in OpenAlex.

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  6. Mouse models for congenital disorders of glycosylation.Journal of inherited metabolic disease · 2011
    Review
  7. Article
  8. Influenza virus entry and infection require host cell N-linked glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  9. 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 1 institution in 1 country.

M SarkarResearch Institute, Hospital for Sick Children, Toronto, ON, Canada.
E Hull
Y Nishikawa
R J Simpson
R L Moritz
R Dunn
H Schachter
Hospital for Sick Children · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

UDP-GlcNAc:alpha-3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I (GnT I; EC 2.4.1.101) catalyzes an essential first step in the conversion of high-mannose N-glycans to hybrid and complex N-glycans. Cloning of the gene encoding this enzyme was carried out by mixed oligonucleotide-primed polymerase chain reaction amplification of rabbit liver single-stranded cDNA using sense and antisense 20- to 24-base-pair (bp) primers. A rabbit liver library in phage lambda gt10 yielded a 2.5-kilobase (kb) cDNA with a 447-amino acid coding sequence. None of the nine asparagine residues were in an Asn-Xaa-(Ser or Thr) sequence, indicating that the protein is not N-glycosylated. There is no sequence homology to other previously cloned glycosyltransferases, but GnT I appears to have a domain structure typical of these enzymes--i.e., a short amino-terminal domain, a transmembrane domain, a "neck" region, and a large carboxyl-terminal catalytic domain. RNA was transcribed off the 2.5-kb cDNA, and in vitro translation with rabbit reticulocyte lysate yielded a 52-kDa protein with GnT I activity.

Indexed as

GenesN-AcetylglucosaminyltransferasesAmino Acid SequenceAnimalsBase SequenceChromatography, High Pressure LiquidCloning, MolecularGene LibraryGlucosyltransferasesLiverMolecular Sequence DataOligonucleotide ProbesPeptide FragmentsPolymerase Chain ReactionProtein BiosynthesisRabbitsalpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase IGlucosyltransferasesN-AcetylglucosaminyltransferasesOligonucleotide ProbesPeptide FragmentsRNA, Messenger

Identifiers

PMID1824724
PMCPMC50784
OpenAlexW2059373310

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.