Evidence map›Paper›PMID 20060974›Full record

ArticleAtherosclerosis2010

Caspase-1 recognizes extended cleavage sites in its natural substrates.

Jerry Shen, Ying Yin, Jietang Mai, Xinyu Xiong, Meghana Pansuria, Jingshan Liu, Erin Maley, Najam Us Saqib, Hong Wang, Xiao-Feng Yang

Abstract read
In one paragraph

Article in Atherosclerosis, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

34 citing papers in PubMed, 53 citations in OpenAlex.

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  15. Review
  16. Co-signaling receptors regulate T-cell plasticity and immune tolerance.Frontiers in bioscience (Landmark edition) · 2019
    Article
  17. Caspase-1 regulates cellular trafficking via cleavage of the Rab7 adaptor protein RILP.Biochemical and biophysical research communications · 2018
    Article
  18. Article
  19. 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

10 authors at 1 institution in 1 country.

Jerry ShenDepartment of Pharmacology, Cardiovascular Research Center, Temple University School of Medicine, Philadelphia, PA 19140, United States.
Ying Yin
Jietang Mai
Xinyu Xiong
Meghana Pansuria
Jingshan Liu
Erin Maley
Najam Us Saqib
Hong Wang
Xiao-Feng Yang
Temple University · US

Funding

Atherogenic mechanisms with homocysteineR01HL077288 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI WANG, HONG · 2004 to 2014
$3.8M
Inhibition of Endothelial Growth by HomocysteineR01HL067033 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI WANG, HONG · 2002 to 2011
$3.0M
Suppression of vascular endothelial cell inflammationR01HL094451 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI YANG, XIAOFENG · 2009 to 2013
$1.8M
Role of HHcy in diabetic vascular diseaseR01HL082774 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI WANG, HONG · 2006 to 2010
$1.8M
NHLBI NIH HHS HL094451NHLBI NIH HHS HL67033NHLBI NIH HHS HL77288NHLBI NIH HHS HL82774NHLBI NIH HHS R01 HL067033NHLBI NIH HHS R01 HL077288NHLBI NIH HHS R01 HL082774NHLBI NIH HHS R01 HL094451
6 · The paper itself

Abstract

objectiveThe preferred amino acids in the proteolytic sites have been considered to be similar between caspase-1 and caspase-9, which do not support their differential functions in inflammatory pyroptosis and apoptosis. We attempted to solve this problem.

methodsWe analyzed the flanking 20 amino acid residues in the cleavage sites in 34 caspase-1 and 11 capase-9 experimentally identified substrates.

resultsThis study has made the following findings: first, we verified that caspase-1 and caspase-9 shared 100% aspartic acid in the P1 position. However, the structures in the cleavage sites of most caspase-1 substrates are different from that of caspase-9 substrates in the following three aspects, (a) the amino acid residues with the statistically high frequencies; (b) the hydrophobic amino acid occurrence frequencies; and (c) the charged amino acid occurrence frequencies; second, the amino acid pairs P1-P1' are different; third, our identified cleavage site patterns are useful in the prediction for the 91.4% cleavage sites of 35 new caspase-1 substrates.

conclusionSince most caspase-1 substrates are involved in vascular function, inflammation and atherogenesis, our novel structural patterns for the caspases' substrates are significant in developing new diagnostics and therapeutics.

Indexed as

ApoptosisAmino AcidsBinding SitesCaspase 1Caspase 9CaspasesCell DeathGene Expression Regulation, EnzymologicHumansInflammationModels, BiologicalProtein BindingSubstrate SpecificityAmino AcidsCaspase 1Caspase 9Caspases

Identifiers

PMID20060974
PMCPMC2917068
OpenAlexW1996910863

What OpenQuestion holds

Textmetadata
LicenceTDM
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.