Evidence map›Paper›PMID 28282970›Full record

ArticleScientific reports2017

New platform for simple and rapid protein-based affinity reactions.

Kei Kubota, Takuya Kubo, Tetsuya Tanigawa, Toyohiro Naito, Koji Otsuka

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

6 citing papers in PubMed, 25 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

5 authors at 1 institution in 1 country.

Kei KubotaGraduate School of Engineering, Kyoto University, Kyoto, Japan.
Takuya KuboGraduate School of Engineering, Kyoto University, Kyoto, Japan. kubo@anchem.mc.kyoto-u.ac.jp.ORCID 0000-0002-9274-3295
Tetsuya TanigawaGraduate School of Engineering, Kyoto University, Kyoto, Japan.
Toyohiro NaitoGraduate School of Engineering, Kyoto University, Kyoto, Japan.
Koji OtsukaGraduate School of Engineering, Kyoto University, Kyoto, Japan.ORCID 0000-0003-1088-0569
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We developed a spongy-like porous polymer (spongy monolith) consisting of poly(ethylene-co-glycidyl methacrylate) with continuous macropores that allowed efficient in situ reaction between the epoxy groups and proteins of interest. Immobilization of protein A on the spongy monolith enabled high-yield collection of immunoglobulin G (IgG) from cell culture supernatant even at a high flow rate. In addition, immobilization of pepsin on the spongy monolith enabled efficient online digestion at a high flow rate.

Indexed as

Chromatography, Reverse-PhaseImmobilized ProteinsImmunoglobulin GMethacrylatesPepsin APolyethylenesPolymersStaphylococcal Protein AImmobilized ProteinsImmunoglobulin GMethacrylatesPepsin Apoly(ethylene-co-glycidyl methacrylate)PolyethylenesPolymersStaphylococcal Protein A

Identifiers

PMID28282970
PMCPMC5428043
OpenAlexW2593786335

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.