Evidence map›Paper›PMID 19117953›Full record

ArticleThe Journal of biological chemistry2009

Crystal structure of procaspase-1 zymogen domain reveals insight into inflammatory caspase autoactivation.

J Michael Elliott, Lionel Rouge, Christian Wiesmann, Justin M Scheer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

55 citing papers in PubMed, 88 citations in OpenAlex.

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  20. The intricate biophysical puzzle of caspase-1 activation.Archives of biochemistry and biophysics · 2021
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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.

J Michael ElliottDepartment of Protein Chemistry, Genentech, Inc., South San Francisco, California 94080, USA.
Lionel Rouge
Christian Wiesmann
Justin M Scheer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

One key event in inflammatory signaling is the activation of the initiator caspase, procaspase-1. Presented here is the crystal structure of the procaspase-1 zymogen without its caspase recruitment domain solved to 2.05 A. Although the isolated domain is monomeric in solution, the protein appeared dimeric in crystals. The loop arrangements in the dimer provide insight into the first autoproteolytic events that occur during activation by oligomerization. Additionally, in contrast to other caspases, we demonstrate that autoproteolysis at the second cleavage site, Asp316, is necessary for conversion to a stable dimer in solution. Critical elements of secondary structure are revealed in the crystal structure that explain why a dimeric protein is favored after proteolysis at this aspartic acid. Dimer stabilization is concurrent with a 130-fold increase in kcat, the sole contributing kinetic factor to an activated and efficient mediator of inflammation.

Indexed as

Caspase 1Crystallography, X-RayDimerizationEnzyme ActivationEnzyme PrecursorsEnzyme StabilityHumansInflammationInflammation MediatorsKineticsProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryCaspase 1Enzyme PrecursorsInflammation Mediators

Identifiers

PMID19117953
PMCPMC2649088
OpenAlexW2012524417

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.