Evidence map›Paper›PMID 32051682›Full record

ArticleIEEE transactions on nanotechnology2019

Optimization of Protein-Protein Interaction Measurements for Drug Discovery Using AFM Force Spectroscopy.

Yongliang Yang, Bixi Zeng, Zhiyong Sun, Amir Monemian Esfahani, Jing Hou, Nian-Dong Jiao, Lianqing Liu, Liangliang Chen, Marc D Basson, Lixin Dong and 2 more

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in IEEE transactions on nanotechnology, 2019. 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
0.6field-weighted citation impact, top 31% 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

1 citing paper in PubMed, 9 citations in OpenAlex.

  1. 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

12 authors at 6 institutions in 3 countries.

Yongliang YangDepartment of Electrical and Computer Engineering, Michigan State University, East Lansing, MI, 48823, USA.
Bixi ZengDepartments of Surgery and Biomedical Sciences, University of North Dakota, Grand Forks, ND, 58202, USA.
Zhiyong SunDepartment of Electrical and Computer Engineering, Michigan State University, East Lansing, MI, 48823, USA.
Amir Monemian EsfahaniDepartment of Mechanical and Materials Engineering, University of Nebraska Lincoln, NE 68588 USA.
Jing HouSchool of Information and Control Engineering, Shenyang Jianzhu University, Shenyang 110168, China.
Nian-Dong JiaoState Key Laboratory of Robotics, Shenyang Institute of Automation, Chinese Academy of Sciences, Shenyang, 110006, China.
Lianqing LiuState Key Laboratory of Robotics, Shenyang Institute of Automation, Chinese Academy of Sciences, Shenyang, 110006, China.
Liangliang ChenDepartment of Electrical and Computer Engineering, Michigan State University, East Lansing, MI, 48823, USA.
Marc D BassonDepartments of Surgery and Biomedical Sciences, University of North Dakota, Grand Forks, ND, 58202, USA.
Lixin DongDepartment of Electrical and Computer Engineering, Michigan State University, East Lansing, MI, 48823, USA.
Ruiguo YangDepartment of Mechanical and Materials Engineering, University of Nebraska Lincoln, NE 68588 USA.
Ning XiDepartment of Electrical and Computer Engineering, Michigan State University, East Lansing, MI, 48823, USA.
Michigan State University · USCity University of Hong Kong · HKShenyang Institute of Automation · CNUniversity of Nebraska–Lincoln · USUniversity of North Dakota · USShenyang Jianzhu University · CN

Funding

Targeted mass spectrometry approaches to understand CART processing and recepter interactionsP20GM113126 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI RAZAVI RIZI, MOHAMMAD · 2016 to 2025
$20.8M
Nebraska Center for Nanomedicine- Pilot ProjectsP30GM127200 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI OUPICKY, DAVID · 2018 to 2022
$5.7M
NIGMS NIH HHS P20 GM113126NIGMS NIH HHS P30 GM127200
6 · The paper itself

Abstract

Increasingly targeted in drug discovery, protein-protein interactions challenge current high throughput screening technologies in the pharmaceutical industry. Developing an effective and efficient method for screening small molecules or compounds is critical to accelerate the discovery of ligands for enzymes, receptors and other pharmaceutical targets. Here, we report developments of methods to increase the signal-to-noise ratio (SNR) for screening protein-protein interactions using atomic force microscopy (AFM) force spectroscopy. We have demonstrated the effectiveness of these developments on detecting the binding process between focal adhesion kinases (FAK) with protein kinase B (Akt1), which is a target for potential cancer drugs. These developments include optimized probe and substrate functionalization processes and redesigned probe-substrate contact regimes. Furthermore, a statistical-based data processing method was developed to enhance the contrast of the experimental data. Collectively, these results demonstrate the potential of the AFM force spectroscopy in automating drug screening with high throughput.

Indexed as

Atomic force microscopyBionanotechnologyForce spectroscopyIndex TermsNanosensorsProtein-protein interactions

Identifiers

PMID32051682
PMCPMC7015265
OpenAlexW2945288534

What OpenQuestion holds

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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.