Evidence map›Paper›PMID 29713337›Full record

ArticleThe journal of venomous animals and toxins including tropical diseases2018

Alternagin-C binding to α

Milene Nóbrega de Oliveira Moritz, Lívia Mara Santos Eustáquio, Kelli Cristina Micocci, Ana Carolina Caetano Nunes, Patty Karina Dos Santos, Tamires de Castro Vieira, Heloísa Sobreiro Selistre-de-Araujo

Open access · goldAbstract read
In one paragraph

Article in The journal of venomous animals and toxins including tropical diseases, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Review
  3. Measuring Matrix Metalloproteinases Activity by Gelatin Zymography.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  4. Article
  5. Snake venom disintegrins update: insights about new findings.The journal of venomous animals and toxins including tropical diseases · 2023
    Review
  6. Review
  7. Cell migration inhibition activity of a non-RGD disintegrin fromThe journal of venomous animals and toxins including tropical diseases · 2018
    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

7 authors at 1 institution in 1 country.

Milene Nóbrega de Oliveira MoritzDepartment of Physiological Sciences, Federal University of São Carlos (UFSCar), São Carlos, SP 13565-905 Brazil.
Lívia Mara Santos EustáquioDepartment of Physiological Sciences, Federal University of São Carlos (UFSCar), São Carlos, SP 13565-905 Brazil.
Kelli Cristina MicocciDepartment of Physiological Sciences, Federal University of São Carlos (UFSCar), São Carlos, SP 13565-905 Brazil.
Ana Carolina Caetano NunesDepartment of Physiological Sciences, Federal University of São Carlos (UFSCar), São Carlos, SP 13565-905 Brazil.
Patty Karina Dos SantosDepartment of Physiological Sciences, Federal University of São Carlos (UFSCar), São Carlos, SP 13565-905 Brazil.
Tamires de Castro VieiraDepartment of Physiological Sciences, Federal University of São Carlos (UFSCar), São Carlos, SP 13565-905 Brazil.
Heloísa Sobreiro Selistre-de-AraujoDepartment of Physiological Sciences, Federal University of São Carlos (UFSCar), São Carlos, SP 13565-905 Brazil.
Universidade Federal de São Carlos · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundMatrix metalloproteinases (MMPs) are key players in tumor progression, helping tumor cells to modify their microenvironment, which allows cell migration to secondary sites. The role of integrins, adhesion receptors that connect cells to the extracellular matrix, in MMP expression and activity has been previously suggested. However, the mechanisms by which integrins control MMP expression are not completely understood. Particularly, the role of α2β1 integrin, one of the major collagen I receptors, in MMP activity and expression has not been studied. Alternagin-C (ALT-C), a glutamate-cysteine-aspartate-disintegrin from

methodsALT-C was purified by two steps of gel filtration followed by anion exchange chromatography. The α

resultsOur data demonstrate that ALT-C, after binding to α

conclusionThese results demonstrate that α

Indexed as

ALT-CCancerC-MycMMPTumor microenvironmentα2β1 integrin

Identifiers

PMID29713337
PMCPMC5917863
OpenAlexW2804764407

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.