Evidence map›Paper›PMID 31511322›Full record

ArticleThe Journal of biological chemistry2019

Unexpected roles for ADH1 and SORD in catalyzing the final step of erythritol biosynthesis.

Lisa Schlicker, Doletha M E Szebenyi, Semira R Ortiz, Alexander Heinz, Karsten Hiller, Martha S Field

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

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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

6 authors at 3 institutions in 2 countries.

Lisa SchlickerDepartment of Bioinformatics and Biochemistry, BRICS, Technische Universität Braunschweig, 38106 Braunschweig, Germany.
Doletha M E SzebenyiMacCHESS, Cornell University, Ithaca, New York 14853.
Semira R OrtizDivision of Nutritional Sciences, Cornell University, Ithaca, New York 14853.
Alexander HeinzDepartment of Bioinformatics and Biochemistry, BRICS, Technische Universität Braunschweig, 38106 Braunschweig, Germany.
Karsten HillerDepartment of Bioinformatics and Biochemistry, BRICS, Technische Universität Braunschweig, 38106 Braunschweig, Germany.
Martha S FieldDivision of Nutritional Sciences, Cornell University, Ithaca, New York 14853 mas246@cornell.edu.ORCID 0000-0001-7547-5180
Cornell University · USTechnische Universität Braunschweig · DEHelmholtz Centre for Infection Research · DE

Funding

Acquisition of a Hybrid Quadrupole Time of Flight LC-MS/MS System for the CornellS10OD017992 · OD · CORNELL UNIVERSITY · PI ZHANG, SHENG · 2014 to 2014
$600k
NIH HHS S10 OD017992
6 · The paper itself

Abstract

The low-calorie sweetener erythritol is endogenously produced from glucose through the pentose phosphate pathway in humans. Erythritol is of medical interest because elevated plasma levels of this polyol are predictive for visceral adiposity gain and development of type 2 diabetes. However, the mechanisms behind these associations remain unknown because the erythritol biosynthesis pathway, particularly the enzyme catalyzing the final step of erythritol synthesis (reduction of erythrose to erythritol), is not characterized. In this study, we purified two enzymes from rabbit liver capable of catalyzing the conversion of erythrose to erythritol: alcohol dehydrogenase 1 (ADH1) and sorbitol dehydrogenase (SORD). Both recombinant human ADH1 and SORD reduce erythrose to erythritol, using NADPH as a co-factor, and cell culture studies indicate that this activity is primarily NADPH-dependent. We found that

Indexed as

A549 CellsAlcohol DehydrogenaseAnimalsErythritolHumansL-Iditol 2-DehydrogenaseLiverRabbitsTetrosesAlcohol DehydrogenaseErythritolerythroseL-Iditol 2-DehydrogenaseTetrosesalcohol dehydrogenase (ADH)biomarkerenzyme catalysisenzyme kineticserythritolglucose metabolismsorbitol dehydrogenase

Identifiers

PMID31511322
PMCPMC6827307
OpenAlexW2973043833

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.