Evidence map›Paper›PMID 41288508›Full record

ArticleBiomacromolecules2025

Induced Proximity Approach Enables the Recombinant Production of Polyphosphorylated Silk Proteins with Improved Adhesiveness.

Nea B Möttönen, Ruxia Fan, Stefania Aspholm-Tsironi, Salla Keskitalo, Antti Tuhkala, Markku Varjosalo, A Sesilja Aranko

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biomacromolecules, 2025. 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
–field-weighted citation impact
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.

  1. Review
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.

Nea B MöttönenDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, 02150 Espoo, Finland.ORCID 0009-0005-3299-0058
Ruxia FanDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, 02150 Espoo, Finland.ORCID 0000-0001-7551-7432
Stefania Aspholm-TsironiDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, 02150 Espoo, Finland.
Salla KeskitaloInstitute of Biotechnology and Helsinki Institute of Life Science, University of Helsinki, 00014 Helsinki, Finland.ORCID 0000-0001-5555-1975
Antti TuhkalaInstitute of Biotechnology and Helsinki Institute of Life Science, University of Helsinki, 00014 Helsinki, Finland.ORCID 0009-0008-7956-9043
Markku VarjosaloInstitute of Biotechnology and Helsinki Institute of Life Science, University of Helsinki, 00014 Helsinki, Finland.ORCID 0000-0002-1340-9732
A Sesilja ArankoDepartment of Bioproducts and Biosystems, School of Chemical Engineering, Aalto University, 02150 Espoo, Finland.ORCID 0000-0001-9425-3524

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation is considered to play a role in many of the functional properties of silk proteins, affecting their solubility, environmental adaptability, adhesion, and biocompatibility. However, investigating these effects has been hampered by the difficulty of isolating phosphorylated proteins from natural sources and the limitations of the current

Indexed as

FibroinsRecombinant ProteinsSilkAdhesivenessAnimalsEscherichia coliPhosphorylationProtein EngineeringSpidersFibroinsRecombinant ProteinsSilk

Identifiers

PMID41288508
PMCPMC12690576

What Socratic 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 Socratic graph.