Evidence map›Paper›PMID 22722607›Full record

ReviewNature reviews. Molecular cell biology2012

Vertebrate protein glycosylation: diversity, synthesis and function.

Kelley W Moremen, Michael Tiemeyer, Alison V Nairn

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 845 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
845citing papers in PubMed, 1 pooled it
29.8field-weighted citation impact, top 1% 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

845 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,664 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Article
  4. ADAR RNA editing for cardiovascular disease: TargetingMolecular therapy. Nucleic acids · 2026
    Article
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785 more citing papers are in PubMed but not listed here.

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.

Kelley W MoremenComplex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30602, USA. moremen@uga.edu
Michael Tiemeyer
Alison V Nairn
University of Georgia · US

Funding

ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR005351 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI VENOT, ANDRE · 1989 to 2011
$18.4M
UNDERSTANDING MECHANISMS OF hESC SELF-RENEWAL AND CELL FATE COMMITMENTP01GM085354 · NIGMS · UNIVERSITY OF GEORGIA · PI DALTON, STEPHEN · 2008 to 2018
$18.3M
TR&D3. Approaches to Proteoglycan Function at Biochemical and Cellular LevelsP41GM103390 · NIGMS · UNIVERSITY OF GEORGIA · PI MOREMEN, KELLEY W. · 2012 to 2019
$14.5M
TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
ZINC DEFICIENCY &PROTEIN EXPRESSION IN RAT OLFACTORY BULBSP41RR018502 · NCRR · UNIVERSITY OF GEORGIA (UGA) · PI AZADI, PARASTOO · 2003 to 2011
$13.1M
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
Mechanisms regulating glycan expression and functionR01GM072839 · NIGMS · UNIVERSITY OF GEORGIA (UGA) · PI TIEMEYER, MICHAEL · 2005 to 2008
$1.1M
NCRR NIH HHS P41 RR005351NCRR NIH HHS P41RR005351NCRR NIH HHS P41 RR018502NCRR NIH HHS P41RR018502NIDDK NIH HHS R01 DK075322NIDDK NIH HHS R01DK075322NIGMS NIH HHS P01 GM085354NIGMS NIH HHS P01GM085354NIGMS NIH HHS P41 GM103390NIGMS NIH HHS P41GM103390NIGMS NIH HHS P41 GM103490NIGMS NIH HHS P41GM103490NIGMS NIH HHS R01 GM047533NIGMS NIH HHS R01GM047533NIGMS NIH HHS R01 GM072839NIGMS NIH HHS R01GM072839
6 · The paper itself

Abstract

Protein glycosylation is a ubiquitous post-translational modification found in all domains of life. Despite their significant complexity in animal systems, glycan structures have crucial biological and physiological roles, from contributions in protein folding and quality control to involvement in a large number of biological recognition events. As a result, they impart an additional level of 'information content' to underlying polypeptide structures. Improvements in analytical methodologies for dissecting glycan structural diversity, along with recent developments in biochemical and genetic approaches for studying glycan biosynthesis and catabolism, have provided a greater understanding of the biological contributions of these complex structures in vertebrates.

Indexed as

GlycosylationAnimalsCell MembraneCytosolEndoplasmic ReticulumGlycoproteinsGolgi ApparatusHumansMetabolismModels, BiologicalPolysaccharidesProtein ConformationProtein DenaturationProtein FoldingProtein Processing, Post-TranslationalProteinsGlycoproteinsPolysaccharidesProteins

Identifiers

PMID22722607
PMCPMC3934011
OpenAlexW2018042261

What OpenQuestion holds

Textmetadata
LicenceTDM
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.