Evidence map›Paper›PMID 20889969›Full record

ArticleThe Journal of biological chemistry2010

Cobra CRISP functions as an inflammatory modulator via a novel Zn2+- and heparan sulfate-dependent transcriptional regulation of endothelial cell adhesion molecules.

Yu-Ling Wang, Je-Hung Kuo, Shao-Chen Lee, Jai-Shin Liu, Yin-Cheng Hsieh, Yu-Tsung Shih, Chun-Jung Chen, Jeng-Jiann Chiu, Wen-Guey Wu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

46 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
  2. Review
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  4. Histopathological characterization of skin and muscle lesions induced by lionfish (The journal of venomous animals and toxins including tropical diseases · 2025
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  5. Review
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  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. CRISPs Function to Boost Sperm Power Output and Motility.Frontiers in cell and developmental biology · 2021
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Frontiers in chemistry · 2020
    Article
  20. 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

9 authors at 4 institutions in 1 country.

Yu-Ling WangFrom the Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 30013, Taiwan.
Je-Hung Kuo
Shao-Chen Lee
Jai-Shin Liu
Yin-Cheng Hsieh
Yu-Tsung Shih
Chun-Jung Chen
Jeng-Jiann Chiu
Wen-Guey Wu
National Health Research Institutes · TWNational Tsing Hua University · TWNational Synchrotron Radiation Research Center · TWFu Jen Catholic University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cysteine-rich secretory proteins (CRISPs) have been identified as a toxin family in most animal venoms with biological functions mainly associated with the ion channel activity of cysteine-rich domain (CRD). CRISPs also bind to Zn(2+) at their N-terminal pathogenesis-related (PR-1) domain, but their function remains unknown. Interestingly, similar the Zn(2+)-binding site exists in all CRISP family, including those identified in a wide range of organisms. Here, we report that the CRISP from Naja atra (natrin) could induce expression of vascular endothelial cell adhesion molecules, i.e. intercellular adhesion molecule-1, vascular adhesion molecule-1, and E-selectin, to promote monocytic cell adhesion in a heparan sulfate (HS)- and Zn(2+)-dependent manner. Using specific inhibitors and small interfering RNAs, the activation mechanisms are shown to involve both mitogen-activated protein kinases and nuclear factor-κB. Biophysical characterization of natrin by using fluorescence, circular dichroism, and x-ray crystallographic methods further reveals the presence of two Zn(2+)-binding sites for natrin. The strong binding site is located near the putative Ser-His-Glu catalytic triad of the N-terminal domain. The weak binding site remains to be characterized, but it may modulate HS binding by enhancing its interaction with long chain HS. Our results strongly suggest that natrin may serve as an inflammatory modulator that could perturb the wound-healing process of the bitten victim by regulating adhesion molecule expression in endothelial cells. Our finding uncovers a new aspect of the biological role of CRISP family in immune response and is expected to facilitate future development of new therapeutic strategy for the envenomed victims.

Indexed as

ElapidaeAnimalsBinding SitesCell AdhesionCell Adhesion MoleculesCell LineCells, CulturedElapid VenomsEndothelial CellsGene ExpressionHeparan SulfateHumansInflammation MediatorsMolecular ConformationProtein BindingProtein Structure, TertiaryCell Adhesion MoleculesElapid VenomsHeparan SulfateInflammation Mediatorsnatrin protein, Naja atraZinc

Identifiers

PMID20889969
PMCPMC2988390
OpenAlexW2041344655

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.