Evidence map›Paper›PMID 33445129›Full record

ReviewCurrent opinion in structural biology2021

Protein N-glycosylation and O-mannosylation are catalyzed by two evolutionarily related GT-C glycosyltransferases.

Lin Bai, Huilin Li

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. The Role of Glycans in Human Immunity-A Sweet Code.Molecules (Basel, Switzerland) · 2025
    Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. 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

2 authors at 2 institutions in 2 countries.

Lin BaiDepartment of Biochemistry and Biophysics, School of Basic Medical Sciences, Peking University, Beijing 100083, PR China. Electronic address: lbai@bjmu.edu.cn.
Huilin LiDepartment of Structural Biology, Van Andel Institute, Grand Rapids, MI 49503, United States. Electronic address: Huilin.Li@vai.org.
Peking University · CNVan Andel Institute · US

Funding

The structure and function of eukaryotic protein glycosylation enzymesR01CA231466 · NCI · VAN ANDEL RESEARCH INSTITUTE · PI Huilin Li · 2018 to 2026
$4.0M
NCI NIH HHS R01 CA231466
6 · The paper itself

Abstract

The structural folds of glycosyltransferases are categorized into three superfamilies: GT-A, GT-B, and GT-C. Few structures of GT-C fold existed in the Protein Data Bank prior to the recent advent of high-resolution cryo-EM, because the glycosyltransferases are large membrane proteins that are difficult to crystallize. The use of cryo-EM has resulted in the structures of several key GT-C glycosyltransferases. Here we summarize the latest structural features of and mechanistic insights into these membrane enzyme complexes.

Indexed as

GlycosyltransferasesMembrane ProteinsCatalysisDatabases, ProteinGlycosylationGlycosyltransferasesMembrane Proteins

Identifiers

PMID33445129
PMCPMC8222153
OpenAlexW3120298832

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.