Evidence map›Paper›PMID 34019197›Full record

ArticleThe protein journal2021

"Computational and Functional Characterization of a Hemorrhagic Metalloproteinase Purified from Cerastes cerastes Venom".

Amel Bennacer, Hinda Boukhalfa-Abib, Fatima Laraba-Djebari

Abstract read
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In one paragraph

Article in The protein journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.2field-weighted citation impact, top 41% 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

0 citing papers in PubMed, 3 citations in OpenAlex.

No citing paper in PubMed yet.

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

3 authors at 1 institution in 1 country.

Amel BennacerUSTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, BP 32, El-Alia Bab Ezzouar, 16111, Algiers, Algeria.
Hinda Boukhalfa-AbibUSTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, BP 32, El-Alia Bab Ezzouar, 16111, Algiers, Algeria.
Fatima Laraba-DjebariUSTHB, Faculty of Biological Sciences, Laboratory of Cellular and Molecular Biology, BP 32, El-Alia Bab Ezzouar, 16111, Algiers, Algeria. flaraba@hotmail.com.
University of Sciences and Technology Houari Boumediene · DZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural and functional aspects of snake venoms metalloproteinases (SVMPs) have been extensively studied due to their role in envenomation. However, in the detection of certain coagulation disorders these biomolecules have been used and applied for the production of new thrombolytic drugs. CcMP-II, a SVMP-II metalloproteinase with a hemorrhagic activity, isolated from the venom of Cerastes cerastes, its sequence of 472 amino acids was identified. Predicted 3D structure showed an arrangement of CcMP-II into two distinct domains: i) a metalloproteinase domain where the zinc-binding motif is found (HXXGHNLGIDH) in addition to the sequence Cys-Ile-Met (CIM) at the Met-turn and ii) disintegrin-like domain containing RGD motif. CcMP-II inhibits platelet aggregation induced by collagen in a dose-dependent manner with an IC

Indexed as

HemorrhageMetalloendopeptidasesReptilian ProteinsViperidaeAnimalsMaleMicePlatelet AggregationProtein DomainsViper Venomshemorrhagic metalloproteinaseMetalloendopeptidasesReptilian ProteinsViper VenomsAnti-platelet aggregationHemorrhagic metalloproteinaseHomology modelingViperidae venom

Identifiers

PMID34019197
OpenAlexW3163847233

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.