Evidence map›Paper›PMID 41556522›Full record

ArticleProtein science : a publication of the Protein Society2026

Structural and dynamic similarities of nanofibrils and microparticles of engineered spider silk proteins probed by solid-state NMR spectroscopy.

Nina Wehr, Ettore Bartalucci, Sabrina Smid, Georg Künze, Martin Humenik, Thomas Scheibel, Thomas Wiegand

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Phosphate- and pH-dependent self-assembly of recombinant spider silk proteins.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Article
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.

Nina WehrInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, Aachen, Germany.
Ettore BartalucciInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, Aachen, Germany.
Sabrina SmidInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, Aachen, Germany.ORCID https://orcid.org/0000-0001-6654-3866
Georg KünzeInstitute for Drug Discovery, Leipzig University, Leipzig, Germany.
Martin HumenikDepartment of Biomaterials, University Bayreuth, Bayreuth, Germany.ORCID https://orcid.org/0000-0002-2097-8941
Thomas ScheibelDepartment of Biomaterials, University Bayreuth, Bayreuth, Germany.ORCID https://orcid.org/0000-0002-0457-2423
Thomas WiegandInstitute of Technical and Macromolecular Chemistry, RWTH Aachen University, Aachen, Germany.ORCID https://orcid.org/0000-0003-3655-6150

Funding

Deutsche Forschungsgemeinschaft 448298270Deutsche Forschungsgemeinschaft 455238107Deutsche Forschungsgemeinschaft 455240421Max-Planck-Gesellschaft
6 · The paper itself

Abstract

Spider silks are proteinaceous fiber materials inspiring material design in various technical and biomedical fields due to their exceptional toughness, which exceeds that of most natural and artificial fibers. Solid-state nuclear magnetic resonance (NMR) spectroscopy has been used herein to obtain insights into the structure and dynamics of

Indexed as

FibroinsNanofibersSilkSpidersAnimalsNuclear Magnetic Resonance, BiomolecularProtein Conformation, beta-StrandProtein EngineeringRecombinant ProteinsFibroinsRecombinant ProteinsSilkpolarization transferspoly‐alaninerecombinant spider silksecondary structuresself‐assembly

Identifiers

PMID41556522
PMCPMC12817280

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.