Evidence map›Paper›PMID 21381717›Full record

ArticleBiochemistry2011

Caspase-6 latent state stability relies on helical propensity.

Sravanti Vaidya, Jeanne A Hardy

Abstract read
In one paragraph

Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

14 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Zinc-mediated allosteric inhibition of caspase-6.The Journal of biological chemistry · 2012
    Article
  14. 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

2 authors at 1 institution in 1 country.

Sravanti VaidyaDepartment of Chemistry, 710 North Pleasant Street, University of Massachusetts, Amherst, Massachusetts 01003, United States.
Jeanne A Hardy
University of Massachusetts Amherst · US

Funding

Control of Executioner Caspases with an allosteric switch - SupplementR01GM080532 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI HARDY, JEANNE ANN · 2008 to 2022
$3.8M
NIGMS NIH HHS R01 GM080532
6 · The paper itself

Abstract

Caspase-6 is an apoptotic protease that also plays important roles in neurodegenerative disorders, including Huntington's and Alzheimer's diseases. Caspase-6 is the only caspase known to form a latent state in which two extended helices block access to the active site. These helices must convert to strands for binding substrate. We probed the interconverting region and found that the absence of helix-breaking residues is more critical than a helix-bridging, hydrogen-bond network for formation of the extended conformation. In addition, our results suggest that caspase-6 must undergo a transition through a low-stability intermediate to bind the active-site ligand. Mature caspase-6 is capable of adopting a latent state not observed in any other caspase. The absence of any helix-breaking residues allows caspase-6 to adopt the extended helical conformation. When we introduced helix-breaking residues similar to those seen in caspase-3 or -7, the structure and stability of the latent state were compromised.

Indexed as

Protein Structure, SecondaryApoenzymesCaspase 6Catalytic DomainEnzyme StabilityKineticsProtein ConformationApoenzymesCaspase 6

Identifiers

PMID21381717
PMCPMC3086340
OpenAlexW2068656477

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.