Evidence map›Paper›PMID 26057800›Full record

ArticleActa crystallographica. Section F, Structural biology communications2015

Crystallization of interleukin-18 for structure-based inhibitor design.

Brian Krumm, Xiangzhi Meng, Yan Xiang, Junpeng Deng

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 95% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Role of Non-Binding T63 Alteration in IL-18 Binding.International journal of molecular sciences · 2024
    Article
  2. 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 2 institutions in 1 country.

Brian KrummDepartment of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
Xiangzhi MengDepartment of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA.
Yan XiangDepartment of Microbiology and Immunology, University of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78229, USA.
Junpeng DengDepartment of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
Oklahoma State University · USThe University of Texas Health Science Center at San Antonio · US

Funding

Poxvirus Immune Evasion MechanismsR01AI079217 · NIAID · UNIVERSITY OF TEXAS HLTH SCIENCE CENTER · PI XIANG, YAN · 2008 to 2018
$3.3M
Structure-function studies on a key signaling module from interleukin 17 receptorR21AI113539 · NIAID · OKLAHOMA STATE UNIVERSITY STILLWATER · PI DENG, JUNPENG · 2014 to 2015
$395k
NIAID NIH HHS AI079217NIAID NIH HHS AI113539NIAID NIH HHS R01 AI079217NIAID NIH HHS R21 AI113539
6 · The paper itself

Abstract

Interleukin-18 (IL-18) is a pleiotropic pro-inflammatory cytokine belonging to the IL-1 superfamily. IL-18 plays an important role in host innate and acquired immune defense, with its activity being modulated in vivo by its naturally occurring antagonist IL-18 binding protein (IL-18BP). Recent crystal structures of human IL-18 (hIL-18) in complex with its antagonist or cognate receptor(s) have revealed a conserved binding interface on hIL-18 representing a promising drug target. An important step in this process is obtaining crystals of apo hIL-18 or hIL-18 in complex with small-molecule inhibitors, preferably under low ionic strength conditions. In this study, surface-entropy reduction (SER) and rational protein design were employed to facilitate the crystallization of hIL-18. The results provide an excellent platform for structure-based drug design.

Indexed as

Protein EngineeringAmino Acid MotifsCrystallizationCrystallography, X-RayEscherichia coliGene ExpressionHumansIntercellular Signaling Peptides and ProteinsInterleukin-18LigandsModels, MolecularMolecular Sequence DataMutationOsmolar ConcentrationProtein BindingProtein Structure, SecondaryIL18 protein, humanIntercellular Signaling Peptides and ProteinsInterleukin-18interleukin-18 binding proteinLigandsRecombinant Fusion Proteinscytokinesimmune defenseinterleukin-18surface-entropy reduction

Identifiers

PMID26057800
PMCPMC4461335
OpenAlexW2120491053

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.