Evidence map›Paper›PMID 31003021›Full record

ReviewCurrent opinion in structural biology2019

Structural and mechanistic themes in glycoconjugate biosynthesis at membrane interfaces.

Karen N Allen, Barbara Imperiali

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
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

13 citing papers in PubMed.

  1. Article
  2. Article
  3. LipoproteinmBio · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Nucleotide Sugars in Chemistry and Biology.Molecules (Basel, Switzerland) · 2020
    Review
  13. Lipopolysaccharide O-antigens-bacterial glycans made to measure.The Journal of biological chemistry · 2020
    Review
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.

Karen N AllenDepartment of Chemistry, Boston University, Boston, MA 02215, United States; Program in Biomolecular Pharmacology, Boston University School of Medicine, Boston, MA 02118, United States. Electronic address: drkallen@bu.edu.
Barbara ImperialiDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, United States; Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, United States. Electronic address: imper@mit.edu.

Funding

SPECIFICITY IN CO- AND POST-TRANSLATIONAL MODIFICATIONR01GM039334 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N., IMPERIALI, BARBARA · 1993 to 2025
$8.0M
Structure and function of the monotopic phosphoglycosyl transferase superfamily: Initiators of biosynthesis of complex bacterial glycoconjugatesR01GM131627 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI ALLEN, KAREN N. · 2019 to 2025
$3.1M
NIGMS NIH HHS R01 GM039334NIGMS NIH HHS R01 GM131627
6 · The paper itself

Abstract

Peripheral and integral membrane proteins feature in stepwise assembly of complex glycans and glycoconjugates. Catalysis on membrane-bound substrates features challenges with substrate solubility and active-site accessibility. However, advantages in enzyme and substrate orientation and control of lateral membrane diffusion provide order to the multistep processes. Recent glycosyltransferase (GT) studies show that substrate diversity is met by the selection of folds which do not converge upon a common mechanism. Examples of polyprenol phosphate phosphoglycosyl transferases (PGTs) highlight that divergent fold families catalyze the same reaction with different mechanisms. Lipid A biosynthesis enzymes illustrate that variations on the robust Rossmann fold allow substrate diversity. Improved understanding of GT and PGT structure and function holds promise for better function prediction and improvement of therapeutic inhibitory ligands.

Indexed as

Binding SitesCarbohydrate MetabolismCatalysisCatalytic DomainCell MembraneCelluloseGlucosyltransferasesGlycoconjugatesGlycosyltransferasesLipid APolyprenolsPolysaccharidesQuantitative Structure-Activity RelationshipSubstrate SpecificityCellulosecellulose synthaseGlucosyltransferasesGlycoconjugatesGlycosyltransferasesLipid APolyprenolsPolysaccharides

Identifiers

PMID31003021
PMCPMC6885101

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.