Evidence map›Paper›PMID 30881304›Full record

ArticleFrontiers in pharmacology2019

Cell-Free Expression and Photo-Crosslinking of the Human Neuropeptide Y

Lisa Maria Kögler, Jan Stichel, Anette Kaiser, Annette G Beck-Sickinger

Open access · goldAbstract read
In one paragraph

Article in Frontiers in pharmacology, 2019. 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
0.5field-weighted citation impact, top 36% 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, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

4 authors at 1 institution in 1 country.

Lisa Maria KöglerInstitute of Biochemistry, Faculty of Life Sciences, Leipzig University, Leipzig, Germany.
Jan StichelInstitute of Biochemistry, Faculty of Life Sciences, Leipzig University, Leipzig, Germany.
Anette KaiserInstitute of Biochemistry, Faculty of Life Sciences, Leipzig University, Leipzig, Germany.
Annette G Beck-SickingerInstitute of Biochemistry, Faculty of Life Sciences, Leipzig University, Leipzig, Germany.
Leipzig University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) represent a large family of different proteins, which are involved in physiological processes throughout the entire body. Furthermore, they represent important drug targets. For rational drug design, it is important to get further insights into the binding mode of endogenous ligands as well as of therapeutic agents at the respective target receptors. However, structural investigations usually require homogenous, solubilized and functional receptors, which is still challenging. Cell-free expression methods have emerged in the last years and many different proteins are successfully expressed, including hydrophobic membrane proteins like GPCRs. In this work, an

Indexed as

cell-freeG protein-coupled receptorshuman Y2 receptorneuropeptide Yphoto-crosslinking

Identifiers

PMID30881304
PMCPMC6405639
OpenAlexW2920407076

What OpenQuestion holds

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LicenceCC BY
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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.