Evidence map›Paper›PMID 20832292›Full record

ReviewCurrent opinion in structural biology2010

Biosynthetic enzymes of unusual microbial sugars.

Hazel M Holden, Paul D Cook, James B Thoden

Abstract readReview
In one paragraph

Review in Current opinion in structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Biochemical investigation of an N-acetyltransferase from Helicobacter pullorum.Protein science : a publication of the Protein Society · 2021
    Article
  2. Review
  3. Bacterial carbohydrate diversity - a Brave New World.Current opinion in chemical biology · 2019
    Review
  4. Structural investigation on WlaRG from Campylobacter jejuni: A sugar aminotransferase.Protein science : a publication of the Protein Society · 2017
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. 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

3 authors at 2 institutions in 1 country.

Hazel M HoldenDepartment of Biochemistry, University of Wisconsin, Madison, WI 53706, USA. hazel_holden@biochem.wisc.edu
Paul D Cook
James B Thoden
University of Wisconsin–Madison · USVanderbilt University Medical Center · US

Funding

X-ray Studies of Sugar-Modifying EnzymesR01DK047814 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI HOLDEN, HAZEL M. · 1994 to 2015
$4.3M
X-ray Studies of Sugar-Modifying EnzymesR56DK047814 · NIDDK · UNIVERSITY OF WISCONSIN-MADISON · PI HOLDEN, HAZEL · 2006 to 2006
$88k
NIDDK NIH HHS DK47814NIDDK NIH HHS R01 DK047814NIDDK NIH HHS R56 DK047814
6 · The paper itself

Abstract

The biological importance of proteins and nucleic acids in the natural world is undeniable, and research efforts on these macromolecules have often overshadowed those directed at carbohydrates. It is now known, however, that carbohydrates not only play roles in energy storage and plant cell wall structure, but are also intimately involved in such processes as fertilization, the immune response, and cell adhesion. Indeed, recent years have seen an explosion in research efforts directed at uncovering and understanding new sugar moieties. The dideoxysugars and trideoxysugars, which are synthesized by a variety of bacteria, fungi, and plants, represent an especially intriguing class of carbohydrates. They are found, for example, on the lipopolysaccharides of some Gram-negative bacteria or on antibacterial agents such as erythromycin. Many of them are formed from simple monosaccharides such as glucose-6-phosphate or fructose-6-phosphate via a myriad of enzymatic reactions including acetylations, aminations, dehydrations, epimerizations, reductions, and methylations. In this review we focus on the recent structural investigations of the bacterial N-acetyltransferases and the PLP-dependent aminotransferases that function on nucleotide-linked sugar substrates.

Indexed as

AcetyltransferasesBacteriaCarbohydratesHumansHydro-LyasesTransaminasesAcetyltransferasesCarbohydratesHydro-LyasesTransaminases

Identifiers

PMID20832292
PMCPMC4254661
OpenAlexW2154892059

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.