Evidence map›Paper›PMID 33676410›Full record

ArticleBMC molecular and cell biology2021

SPRD: a surface plasmon resonance database of common factors for better experimental planning.

Purushottam B Tiwari, Camelia Bencheqroun, Mario Lemus, Taryn Shaw, Marilyn Kouassi-Brou, Adil Alaoui, Aykut Üren

Open access · goldAbstract read
In one paragraph

Article in BMC molecular and cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 12 citations in OpenAlex.

  1. 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

7 authors at 2 institutions in 1 country.

Purushottam B TiwariDepartment of Oncology, Georgetown University, Washington, DC, 20057, USA. pbt7@georgetown.edu.ORCID http://orcid.org/0000-0002-3140-0723
Camelia BencheqrounInnovation Center for Biomedical Informatics (ICBI), Georgetown University, Washington, DC, 20057, USA.
Mario LemusDepartment of Oncology, Georgetown University, Washington, DC, 20057, USA.
Taryn ShawDepartment of Oncology, Georgetown University, Washington, DC, 20057, USA.
Marilyn Kouassi-BrouDepartment of Oncology, Georgetown University, Washington, DC, 20057, USA.
Adil AlaouiInnovation Center for Biomedical Informatics (ICBI), Georgetown University, Washington, DC, 20057, USA.
Aykut ÜrenDepartment of Oncology, Georgetown University, Washington, DC, 20057, USA. au26@georgetown.edu.
Georgetown University · USDartmouth College · US

Funding

Tissue Culture Shared ResourceP30CA051008 · NCI · GEORGETOWN UNIVERSITY · PI Louis M Weiner · 1990 to 2026
$71.5M
Maternal Morbidity and Mortality: Risk Factors, Early Detection and Personalized InterventionUL1TR001409 · NCATS · GEORGETOWN UNIVERSITY · PI GONDRE-LEWIS, MARJORIE C, MELLMAN, THOMAS A · 2015 to 2024
$37.8M
National Institutes of Health (US) P30CA51008NCATS NIH HHS UL1 TR001409NCI NIH HHS P30 CA051008
6 · The paper itself

Abstract

backgroundSurface plasmon resonance is a label-free biophysical technique that is widely used in investigating biomolecular interactions, including protein-protein, protein-DNA, and protein-small molecule binding. Surface plasmon resonance is a very powerful tool in different stages of small molecule drug development and antibody characterization. Both academic institutions and pharmaceutical industry extensively utilize this method for screening and validation studies involving direct molecular interactions. In most applications of the surface plasmon resonance technology, one of the studied molecules is immobilized on a microchip, while the second molecule is delivered through a microfluidic system over the immobilized molecules. Changes in total mass on the chip surface is recorded in real time as an indicator of the molecular interactions. MAIN BODY: Quality and accuracy of the surface plasmon resonance data depend on experimental variables, including buffer composition, type of sensor chip, coupling chemistry of molecules on the sensor surface, and surface regeneration conditions. These technical details are generally included in materials and methods sections of published manuscripts and are not easily accessible using the common internet browser search engines or PubMed. Herein, we introduce a surface plasmon resonance database, www.sprdatabase.info that contains technical details extracted from 5140 publications with surface plasmon resonance data. We also provide an analysis of experimental conditions preferred by different laboratories. These experimental variables can be searched within the database and help future users of this technology to design better experiments.

conclusionAmine coupling and CM5 chips were the most common methods used for immobilizing proteins in surface plasmon resonance experiments. However, number of different chips, capture methods and buffer conditions were used by multiple investigators. We predict that the database will significantly help the scientific community using this technology and hope that users will provide feedback to improve and expand the database indefinitely. Publicly available information in the database can save a great amount of time and resources by assisting initial optimization and troubleshooting of surface plasmon resonance experiments.

Indexed as

KineticsLigandsProtein BindingProtein Interaction MappingProteinsStatistics as TopicSurface Plasmon ResonanceLigandsProteinsAnalyte-ligand interactionsAnd equilibrium dissociation constantSensor chipSurface plasmon resonance (SPR)

Identifiers

PMID33676410
PMCPMC7937274
OpenAlexW3135396255

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.