Evidence map›Paper›PMID 40841907›Full record

ArticleJournal of translational medicine2025

Multivalent fusion protein targeting VEGFR2 and DR5 receptors: assessing the antiangiogenic and antitumor effects via multimodal microangiography.

Irina N Druzhkova, Anna G Orlova, Anastasiia S Fedulova, Arina V Avakiants, Alina A Isakova, Ekaterina V Kukovyakina, Yuan Zijian, Ekaterina A Plotnikova, Galina V Trunova, Andrey A Pankratov and 9 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of translational medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
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

19 authors.

Irina N DruzhkovaPrivolzhsky Research Medical University, Nizhny Novgorod, 603081, Russia.
Anna G OrlovaA.V. Gaponov-Grekhov Institute of Applied Physics of the Russian Academy of Sciences, Nizhny Novgorod, 603950, Russia.
Anastasiia S FedulovaFaculty of Biology, Lomonosov Moscow State University, Moscow, 119234, Russia.
Arina V AvakiantsFaculty of Biology, Lomonosov Moscow State University, Moscow, 119234, Russia.
Alina A IsakovaFaculty of Biology, Lomonosov Moscow State University, Moscow, 119234, Russia.
Ekaterina V KukovyakinaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997, Russia.
Yuan ZijianFaculty of Biology, Lomonosov Moscow State University, Moscow, 119234, Russia.
Ekaterina A PlotnikovaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997, Russia.
Galina V TrunovaP. A. Hertsen Moscow Oncology Research Institute - branch of the National Medical Research Radiological Centre of the Ministry of Health of the Russian Federation, Moscow, 125284, Russia.
Andrey A PankratovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997, Russia.
Anton A PlekhanovPrivolzhsky Research Medical University, Nizhny Novgorod, 603081, Russia.
Alexey A KurnikovA.V. Gaponov-Grekhov Institute of Applied Physics of the Russian Academy of Sciences, Nizhny Novgorod, 603950, Russia.
Pavel V SubochevA.V. Gaponov-Grekhov Institute of Applied Physics of the Russian Academy of Sciences, Nizhny Novgorod, 603950, Russia.
Alexey K ShaytanFaculty of Biology, Lomonosov Moscow State University, Moscow, 119234, Russia.
Marine E GasparianShemyakin-Ovchinnikov Institute of Bioorganic Chemistry of the Russian Academy of Sciences, Moscow, 117997, Russia.
Mikhail P KirpichnikovFaculty of Biology, Lomonosov Moscow State University, Moscow, 119234, Russia.
Dmitry A DolgikhFaculty of Biology, Lomonosov Moscow State University, Moscow, 119234, Russia.
Daniel RazanskyInstitute of Pharmacology and Toxicology, Institute for Biomedical Engineering, Faculty of Medicine, University of Zurich, Zurich, Switzerland. daniel.razansky@uzh.ch.ORCID 0000-0001-8676-0964
Anne V YagolovichFaculty of Biology, Lomonosov Moscow State University, Moscow, 119234, Russia. yagolovichav@my.msu.ru.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAnti-angiogenic therapy is a clinically validated method for cancer treatment. It was previously revealed that concurrent targeting of angiogenic and death receptor signaling pathways by a multivalent DR5-specific cytokine TRAIL variant DR5-B genetically fused with the effector peptides, SRH-DR5-B-iRGD, enhances solid tumor suppression and prolongs survival. The SRH peptide is aimed at blocking the tumor neoangiogenesis by preventing activation of the VEGFR2 receptor, while the iRGD peptide interferes with the activation of integrin α

methodsAn integrated approach has been applied involving molecular modeling of SRH-DR5-B-iRGD binding to DR5 receptor, optoacoustic (OA) and optical coherence tomography-based microangiography (OCT-MA) imaging of the vessel networks in xenografts of human glioblastoma and pancreatic adenocarcinoma in nude mice, supported by immunohistochemical (IHC) staining for vascularization marker CD31, and in vitro and in vivo bioactivity studies.

resultsMolecular modeling has demonstrated that genetic fusion of DR5-B with the SRH and iRGD peptides not only enables the engagement of additional tumor targets VEGFR2 and integrin α

conclusionAmeliorated interaction with the DR5 receptor and imparting antiangiogenic properties to the multivalent fusion protein SRH-DR5-B-iRGD resulted in improved antitumor activity compared to DR5-B. Thereby, SRH-DR5-B-iRGD can be considered as a promising candidate for the treatment of vascularized solid tumors.

Indexed as

Angiogenesis InhibitorsAngiographyAntineoplastic AgentsReceptors, TNF-Related Apoptosis-Inducing LigandRecombinant Fusion ProteinsVascular Endothelial Growth Factor Receptor-2AnimalsCell Line, TumorHumansMiceMice, NudeNeovascularization, PathologicXenograft Model Antitumor AssaysAngiogenesis InhibitorsAntineoplastic AgentsReceptors, TNF-Related Apoptosis-Inducing LigandRecombinant Fusion ProteinsVascular Endothelial Growth Factor Receptor-2Anti-angiogenicMolecular modelingOptical coherence tomographyOptoacoustic imagingTRAILVEGFR2

Identifiers

PMID40841907
PMCPMC12372350

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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.