Evidence map›Paper›PMID 42038005›Full record

ArticleBiodesign research2026

Heptad insertion extends the

Ioannis Karageorgos, D Travis Gallagher

Abstract read
In one paragraph

Article in Biodesign research, 2026. 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
–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

0 citing papers in PubMed.

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

2 authors.

Ioannis KarageorgosMaterial Measurement Laboratory of the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD, USA.
D Travis GallagherMaterial Measurement Laboratory of the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibody function involves conformational variability, yet their extreme flexibility complicates measurement of their structure and properties. They also have numerous ligands, suggesting that a rigid bivalent ligand construct of appropriate length could interact with an antibody to reduce its flexibility for imaging, measurement or functional effect. Such a construct would ideally have an inter-ligand spacer that is fairly rigid and with length between 6 and 10 nm. Coiled-coil bundles of alpha helices represent a common motif in protein structure whose relatively simple parallel geometry makes them suitable for rational modification including applications in metrology. In this study, we describe a heptad-insertion heuristic for extending bundles and apply it to the

Indexed as

Coiled coilCrystal structureHelical bundleHeptad repeatProtein engineering

Identifiers

PMID42038005
PMCPMC13109292

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.