Evidence map›Paper›PMID 30785944›Full record

ArticlePloS one2019

Molecular features of steroid-binding antidins and their use for assaying serum progesterone.

Nitin Agrawal, Soili I Lehtonen, Meri Uusi-Mäkelä, Purvi Jain, Sari Viitala, Juha A E Määttä, Niklas Kähkönen, Latifeh Azizi, Tiina A Riihimäki, Markku S Kulomaa and 3 more

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

Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

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

13 authors at 3 institutions in 1 country.

Nitin AgrawalStructural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland.
Soili I LehtonenBioMediTech Institute and Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.
Meri Uusi-MäkeläBioMediTech Institute and Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.ORCID 0000-0002-6518-1397
Purvi JainBioMediTech Institute and Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.
Sari ViitalaUniversity of Eastern Finland, School of Pharmacy, Kuopio, Finland.
Juha A E MäättäBioMediTech Institute and Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.
Niklas KähkönenBioMediTech Institute and Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.
Latifeh AziziBioMediTech Institute and Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.
Tiina A RiihimäkiBioMediTech Institute and Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.
Markku S KulomaaBioMediTech Institute and Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.
Mark S JohnsonStructural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland.
Vesa P HytönenBioMediTech Institute and Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland.ORCID 0000-0002-9357-1480
Tomi T AirenneStructural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland.ORCID 0000-0001-9645-8670
Tampere University · FIÅbo Akademi University · FIUniversity of Eastern Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chicken avidin (Avd) and streptavidin from Streptomyces avidinii are extensively used in bionanotechnology due to their extremely tight binding to biotin (Kd ~ 10-15 M for chicken Avd). We previously reported engineered Avds known as antidins, which have micro- to nanomolar affinities for steroids, non-natural ligands of Avd. Here, we report the 2.8 Å X-ray structure of the sbAvd-2 (I117Y) antidin co-crystallized with progesterone. We describe the creation of new synthetic phage display libraries and report the experimental as well as computational binding analysis of progesterone-binding antidins. We introduce a next-generation antidin with 5 nM binding affinity for progesterone, and demonstrate the use of antidins for measuring progesterone in serum samples. Our data give insights on how to engineer and alter the binding preferences of Avds and to develop better molecular tools for modern bionanotechnological applications.

Indexed as

AnimalsAvidinBinding SitesBiological AssayBiotinDogsLigandsModels, MolecularProgesteroneProtein BindingAvidinBiotinLigandsProgesterone

Identifiers

PMID30785944
PMCPMC6382169
OpenAlexW2917754477

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.