Evidence map›Paper›PMID 8379930›Full record

ArticleThe Biochemical journal1993

Analysis of the structural requirements of sugar binding to the liver, brain and insulin-responsive glucose transporters expressed in oocytes.

C A Colville, M J Seatter, G W Gould

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.3field-weighted citation impact, top 46% 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

9 citing papers in PubMed, 35 citations in OpenAlex.

  1. Fluorinated carbohydrates forChemical Society reviews · 2023
    Review
  2. Article
  3. Review
  4. Article
  5. Regional distribution of SGLT activity in rat brain in vivo.American journal of physiology. Cell physiology · 2013
    Article
  6. Review
  7. Functional expression of SGLTs in rat brain.American journal of physiology. Cell physiology · 2010
    Article
  8. Article
  9. Role of glucose regulatory mechanisms in diabetic retinopathy.The British journal of ophthalmology · 1995
    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 1 institution in 1 country.

C A ColvilleDepartment of Biochemistry, University of Glasgow, Scotland, UK.
M J Seatter
G W Gould
University of Glasgow · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have expressed the liver (GLUT 2), brain (GLUT 3) and insulin-responsive (GLUT 4) glucose transporters in oocytes from Xenopus laevis by microinjection of in vitro-transcribed mRNA. Using a range of halogeno- and deoxy-glucose analogues, and other hexoses, we have studied the structural basis of sugar binding to these different isoforms. We show that a hydrogen bond to the C-3 position is involved in sugar binding for all three isoforms, but that the direction of this hydrogen bond is different in GLUT 2 from either GLUT 1, 3 or 4. Hydrogen-bonding at the C-4 position is also involved in sugar recognition by all three isoforms, but we propose that in GLUT 3 this hydrogen bond plays a less significant role than in GLUT 2 and 4. In all transporters we propose that the C-4 position is directed out of the sugar-binding pocket. The role of the C-6 position is also discussed. In addition, we have analysed the ability of fructopyranose and fructofuranose analogues to inhibit the transport mediated by GLUT2. We show that fructofuranose analogues, but not fructopyranose analogues, are efficient inhibitors of transport mediated by GLUT 2, and therefore suggest that GLUT 2 accommodates D-glucose as a pyranose ring, but D-fructose as a furanose ring. Models for the binding sites of GLUT 2, 3 and 4 are presented.

Indexed as

AnimalsBinding SitesBrainDeoxyglucoseHydrogen BondingInsulinIn Vitro TechniquesKineticsLiverMonosaccharide Transport ProteinsOocytesProtein BindingRecombinant ProteinsStructure-Activity RelationshipXenopus laevisDeoxyglucoseInsulinMonosaccharide Transport ProteinsRecombinant Proteins

Identifiers

PMID8379930
PMCPMC1134526
OpenAlexW2217817978

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.