Evidence map›Paper›PMID 29343861›Full record

ArticleScientific reports2018

Sensing Native Protein Solution Structures Using a Solid-state Nanopore: Unraveling the States of VEGF.

Nitinun Varongchayakul, Diana Huttner, Mark W Grinstaff, Amit Meller

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Pirfenidone Attenuates Fibrosis and Neovascularization in 3D Spheroid-Laden Hydrogel Culture.Journal of tissue engineering and regenerative medicine · 2026
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  13. Application of Solid-State Nanopore in Protein Detection.International journal of molecular sciences · 2020
    Review
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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

4 authors at 2 institutions in 2 countries.

Nitinun VarongchayakulDepartments of Biomedical Engineering, Boston University, Boston, 02215, Massachusetts, USA.
Diana HuttnerFaculty of Biomedical Engineering, Technion - Israel Institute of Technology, Haifa, 32000, Israel.
Mark W GrinstaffDepartments of Biomedical Engineering, Boston University, Boston, 02215, Massachusetts, USA. mgrin@bu.edu.ORCID http://orcid.org/0000-0002-5453-3668
Amit MellerDepartments of Biomedical Engineering, Boston University, Boston, 02215, Massachusetts, USA. ameller@technion.ac.il.ORCID http://orcid.org/0000-0001-7082-0985
Boston University · USTechnion – Israel Institute of Technology · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Monitoring individual proteins in solution while simultaneously obtaining tertiary and quaternary structural information is challenging. In this study, translocation of the vascular endothelial growth factor (VEGF) protein through a solid-state nanopore (ssNP) produces distinct ion-current blockade amplitude levels and durations likely corresponding to monomer, dimer, and higher oligomeric states. Upon changing from a non-reducing to a reducing condition, ion-current blockage events from the monomeric state dominate, consistent with the expected reduction of the two inter-chain VEGF disulfide bonds. Cleavage by plasmin and application of either a positive or a negative NP bias results in nanopore signals corresponding either to the VEGF receptor recognition domain or to the heparin binding domain, accordingly. Interestingly, multi-level analysis of VEGF events reveals how individual domains affect their translocation pattern. Our study shows that careful characterization of ssNP results elucidates real-time structural information about the protein, thereby complementing classical techniques for structural analysis of proteins in solution with the added advantage of quantitative single-molecule resolution of native proteins.

Indexed as

Binding SitesDNAElectrochemical TechniquesFibrinolysinHumansModels, MolecularNanoporesOxidation-ReductionPhosphinesProtein BindingProtein Interaction Domains and MotifsProtein Structure, SecondaryProtein TransportRecombinant ProteinsVascular Endothelial Growth Factor ADNAFibrinolysinPhosphinesRecombinant Proteinstris(2-carboxyethyl)phosphineVascular Endothelial Growth Factor AVEGFA protein, human

Identifiers

PMID29343861
PMCPMC5772516
OpenAlexW2783960527

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.