Evidence map›Paper›PMID 39989757›Full record

ArticleACS omega2025

Site-Specific Functionalization of Recombinant Spider Silk Using Enzymatic Sortase Coupling.

Rajeev Pasupuleti, Ronnie Jansson, Ida Isacsson, Felicia Hogan, Mona Widhe, My Hedhammar

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS omega, 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. Nanostructured Protein Surfaces Inspired by Spider Silk.Advanced materials (Deerfield Beach, Fla.) · 2025
    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

6 authors.

Rajeev PasupuletiKTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Protein Science, AlbaNova University Center, Roslagstullsbacken 21, SE-106 91 Stockholm, Sweden.ORCID https://orcid.org/0000-0002-9399-2699
Ronnie JanssonKTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Protein Science, AlbaNova University Center, Roslagstullsbacken 21, SE-106 91 Stockholm, Sweden.
Ida IsacssonKTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Protein Science, AlbaNova University Center, Roslagstullsbacken 21, SE-106 91 Stockholm, Sweden.
Felicia HoganKTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Protein Science, AlbaNova University Center, Roslagstullsbacken 21, SE-106 91 Stockholm, Sweden.
Mona WidheKTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Protein Science, AlbaNova University Center, Roslagstullsbacken 21, SE-106 91 Stockholm, Sweden.
My HedhammarKTH Royal Institute of Technology, School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Protein Science, AlbaNova University Center, Roslagstullsbacken 21, SE-106 91 Stockholm, Sweden.ORCID https://orcid.org/0000-0003-0140-419X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Functionalization of biomaterials with extra protein domains will expand their functional roles in biomedical research. The recombinant spider silk protein FN-4RepCT has been shown able to adapt various formats like coatings, nanowires, and macroscopic fibers. Functionalizing these various formats of FN-4RepCT in a site-specific manner will provide the next generation of biomaterials. The current study reports an enzymatic (sortase A) coupling method to site-specifically functionalize various formats of FN-4RepCT with target proteins. The approach is demonstrated with three different functional proteins: the IgG-binding Z-domain, a single-chain variable fragment with specificity for CD38 (scFv

Identifiers

PMID39989757
PMCPMC11840766

What OpenQuestion holds

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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.