ReviewThe international journal of biochemistry & cell biology2013
Applications of snake venom components to modulate integrin activities in cell-matrix interactions.
Review in The international journal of biochemistry & cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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.
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.
Who cites it
27 citing papers in PubMed, 60 citations in OpenAlex.
- Snake Toxins Affecting Blood Vessel Walls: Mode of Action and Biological Significance.International journal of molecular sciences · 2025Review
- Snake venom toxins as potential therapeutic agents in the treatment of prostate cancer.Molecular biology reports · 2024Review
- Review
- Larval secretions of parasitoid wasps are new effectors that impair host immune defences.Crop health · 2023Article
- Effect of Dimeric Disintegrins Isolated fromCancers · 2023Article
- The First Snake Venom KTS/Disintegrins-Integrin Interactions Using Bioinformatics Approaches.Molecules (Basel, Switzerland) · 2022Article
- Specific Antiproliferative Properties of Proteinaceous Toxin Secretions from the Marine AnnelidMarine drugs · 2021Article
- Crotoxin Inhibits Endothelial Cell Functions in Two- and Three-dimensional Tumor Microenvironment.Frontiers in pharmacology · 2021Article
- Review
- Comprehensive Study of the Proteome and Transcriptome of the Venom of the Most Venomous European Viper: Discovery of a New Subclass of Ancestral Snake Venom Metalloproteinase Precursor-Derived Proteins.Journal of proteome research · 2019Article
- Structurally Robust and Functionally Highly Versatile-C-Type Lectin (-Related) Proteins in Snake Venoms.Toxins · 2019Review
- Review
- Beyond the Matrix: The Many Non-ECM Ligands for Integrins.International journal of molecular sciences · 2018Review
- Alternagin-C binding to αThe journal of venomous animals and toxins including tropical diseases · 2018Article
- Dramatic and concerted conformational changes enable rhodocetin to block α2β1 integrin selectively.PLoS biology · 2017Article
- The Molecular Basis of Toxins' Interactions with Intracellular Signaling via Discrete Portals.Toxins · 2017Review
- Bitistatin-functionalized fluorescent nanodiamond particles specifically bind to purified human platelet integrin receptor αInternational journal of nanomedicine · 2017Article
- Inhibition of αvβ3 integrin induces loss of cell directionality of oral squamous carcinoma cells (OSCC).PloS one · 2017Article
- Functional analysis of four single (RGDWL, RGDWM, RGDWP, RGDMN) and two double (RGDNM, RGDMP) mutants: The importance of methionine (M) in the functional potency of recombinant mojastin (r-Moj).Toxicon : official journal of the International Society on Toxinology · 2016Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Snake venom proteins are broadly investigated in the different areas of life science. Direct interaction of these compounds with cells may involve a variety of mechanisms that result in diverse cellular responses leading to the activation or blocking of physiological functions of the cell. In this review, the snake venom components interacting with integrins will be characterized in context of their effect on cellular response. Currently, two major families of snake venom proteins are considered as integrin-binding molecules. The most attention has been devoted to the disintegrin family, which binds certain types of integrins through specific motifs recognized as a tri-peptide structurally localized on an integrin-binding loop. Other snake venom integrin-binding proteins belong to the C-type lectin family. Snake venom molecules bind to the cellular integrins resulting in a modulation of cell signaling and in consequence, the regulation of cell proliferation, migration and apoptosis. Therefore, snake venom research on the integrin-binding molecules may have significance in biomedicine and basic cell biology.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.