Evidence map›Paper›PMID 30213860›Full record

ArticleThe Journal of biological chemistry2018

A versatile insulin analog with high potency for both insulin and insulin-like growth factor 1 receptors: Structural implications for receptor binding.

Martina Chrudinová, Lenka Žáková, Aleš Marek, Ondřej Socha, Miloš Buděšínský, Martin Hubálek, Jan Pícha, Kateřina Macháčková, Jiří Jiráček, Irena Selicharová

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. 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

10 authors.

Martina ChrudinováFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic.
Lenka ŽákováFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic.
Aleš MarekFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic.ORCID 0000-0001-9031-8263
Ondřej SochaFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic.
Miloš BuděšínskýFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic.
Martin HubálekFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic.
Jan PíchaFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic.
Kateřina MacháčkováFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic.
Jiří JiráčekFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic.
Irena SelicharováFrom the Institute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo n. 2, 166 10 Prague 6, Czech Republic selicharova@uochb.cas.cz.ORCID 0000-0002-0180-6781

Funding

Medical Research Council MR/K000179/1Medical Research Council MR/R009066/1
6 · The paper itself

Abstract

Insulin and insulin-like growth factor 1 (IGF-1) are closely related hormones involved in the regulation of metabolism and growth. They elicit their functions through activation of tyrosine kinase-type receptors: insulin receptors (IR-A and IR-B) and IGF-1 receptor (IGF-1R). Despite similarity in primary and three-dimensional structures, insulin and IGF-1 bind the noncognate receptor with substantially reduced affinity. We prepared [d-His

Indexed as

Amino Acid SequenceCrystallography, X-RayHumansInsulinInsulin-Like Growth Factor IKineticsProtein BindingReceptor, IGF Type 1Receptor, InsulinReceptors, SomatomedinIGF1R protein, humanInsulinInsulin-Like Growth Factor IReceptor, IGF Type 1Receptor, InsulinReceptors, Somatomedinbindinginsulininsulin-like growth factor (IGF)insulin receptorkineticsprotein designSite 1structure-function

Identifiers

PMID30213860
PMCPMC6204900

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.