Evidence map›Paper›PMID 23914137›Full record

ArticleJournal of molecular catalysis. B, Enzymatic2013

Calculation of substrate binding affinities for a bacterial GH78 rhamnosidase through molecular dynamics simulations.

Melanie Grandits, Herbert Michlmayr, Christoph Sygmund, Chris Oostenbrink

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular catalysis. B, Enzymatic, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

3 citing papers in PubMed, 11 citations in OpenAlex.

  1. Probiotics-Mediated Bioconversion and Periodontitis.Food science of animal resources · 2021
    Review
  2. Article
  3. 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

4 authors at 1 institution in 1 country.

Melanie GranditsDepartment of Material Sciences and Process Engineering, Institute of Molecular Modeling and Simulation, University of Natural Resources and Life Sciences Vienna, Muthgasse 18, A-1190 Vienna, Austria.
Herbert Michlmayr
Christoph Sygmund
Chris Oostenbrink
BOKU University · AT

Funding

Austrian Science Fund FWF P 20246
6 · The paper itself

Abstract

Ram2 from

Indexed as

Binding thermodynamicsFree energy calculationsGH78, glycoside hydrolase family 78Glycoside hydrolaseGROMOSp-NPR, para-nitrophenyl-alpha-l-rhamnopyranosideRutinose

Identifiers

PMID23914137
PMCPMC3663046
OpenAlexW2004031021

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.