Evidence map›Paper›PMID 27856750›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Substrate recognition and catalysis by GH47 α-mannosidases involved in Asn-linked glycan maturation in the mammalian secretory pathway.

Yong Xiang, Khanita Karaveg, Kelley W Moremen

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

28 citing papers in PubMed, 38 citations in OpenAlex.

  1. Iterative Bump-and-Hole Engineering Creates a Bioorthogonal Reporter forJournal of the American Chemical Society · 2026
    Article
  2. Article
  3. From a single C-mannose to multiple C-mannosyltransferases.The Journal of biological chemistry · 2026
    Review
  4. Iterative Bump-and-hole engineering creates a bioorthogonal reporter forbioRxiv : the preprint server for biology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
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  16. Article
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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

3 authors at 1 institution in 1 country.

Yong XiangComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.
Khanita KaravegComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602.
Kelley W MoremenComplex Carbohydrate Research Center, University of Georgia, Athens, GA 30602; moremen@uga.edu.
University of Georgia · US

Funding

TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
Recombinant Production of Glycosylation Enzymes for Biochem/Structural StudiesP01GM107012 · NIGMS · UNIVERSITY OF GEORGIA · PI PRESTEGARD, JAMES H. · 2013 to 2017
$7.5M
Mannosidases in Glycoprotein Biosynthesis &CatabolismR01GM047533 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI MOREMEN, KELLEY W. · 1992 to 2008
$2.6M
Mannosidase inhibitors as therapeutics for glycoprotein misfolding diseasesR01DK075322 · NIDDK · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2006 to 2010
$2.6M
NIDDK NIH HHS R01 DK075322NIGMS NIH HHS P01 GM107012NIGMS NIH HHS P41 GM103390NIGMS NIH HHS R01 GM047533
6 · The paper itself

Abstract

Maturation of Asn-linked oligosaccharides in the eukaryotic secretory pathway requires the trimming of nascent glycan chains to remove all glucose and several mannose residues before extension into complex-type structures on the cell surface and secreted glycoproteins. Multiple glycoside hydrolase family 47 (GH47) α-mannosidases, including endoplasmic reticulum (ER) α-mannosidase I (ERManI) and Golgi α-mannosidase IA (GMIA), are responsible for cleavage of terminal α1,2-linked mannose residues to produce uniquely trimmed oligomannose isomers that are necessary for ER glycoprotein quality control and glycan maturation. ERManI and GMIA have similar catalytic domain structures, but each enzyme cleaves distinct residues from tribranched oligomannose glycan substrates. The structural basis for branch-specific cleavage by ERManI and GMIA was explored by replacing an essential enzyme-bound Ca

Indexed as

Secretory PathwayAnimalsCalciumCatalysisCatalytic DomainHumansKineticsMannosidasesMiceMutationPolysaccharidesCalciumMan1a protein, mouseMAN1B1 protein, humanMannosidasesPolysaccharidesAsn-linked glycan processingbioinorganic chemistryglycosidase mechanismglycoside hydrolaseα-mannosidase

Identifiers

PMID27856750
PMCPMC5150396
OpenAlexW2554344115

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.