Evidence map›Paper›PMID 29718100›Full record

ArticleBioinformatics (Oxford, England)2018

TMCrys: predict propensity of success for transmembrane protein crystallization.

Julia K Varga, Gábor E Tusnády

Abstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Sequence-Based Prediction of Transmembrane Protein Crystallization Propensity.Interdisciplinary sciences, computational life sciences · 2021
    Article
  3. Article
  4. 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

2 authors.

Julia K Varga'Momentum' Membrane Protein Bioinformatics Research Group, Institute of Enzymology, Research Center of Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.
Gábor E Tusnády'Momentum' Membrane Protein Bioinformatics Research Group, Institute of Enzymology, Research Center of Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Motivation: Transmembrane proteins (TMPs) are crucial in the life of the cells. As they have special properties, their structure is hard to determine--the PDB database consists of 2% TMPs, despite the fact that they are predicted to make up to 25% of the human proteome. Crystallization prediction methods were developed to aid the target selection for structure determination, however, there is a need for a TMP specific service. Results: Here, we present TMCrys, a crystallization prediction method that surpasses existing prediction methods in performance thanks to its specialization for TMPs. We expect TMCrys to improve target selection of TMPs. Availability and implementation: https://github.com/brgenzim/tmcrys. Supplementary information: Supplementary data are available at Bioinformatics online.

Indexed as

CrystallizationHumansMembrane ProteinsProteomeSoftwareMembrane ProteinsProteome

Identifiers

PMID29718100
PMCPMC6137969

What OpenQuestion holds

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LicenceCC BY-NC
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Registered trials

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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.