ArticleNature chemical biology2026
Covalently constrained 'Di-Gembodies' enable parallel structure solutions by cryo-EM.
Article in Nature chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed.
- Four IgG Antibodies and Protein G Are Shapeshifters.International journal of molecular sciences · 2026Article
- Thousandfold Expansion Microscopy.bioRxiv : the preprint server for biology · 2026Article
- Mapping the Structure and Conformational Landscape of the 10-23 DNAzyme.ACS chemical biology · 2026Article
- Exploiting plant immune "switches" for resistance engineering.Stress biology · 2026Review
- Tiny tools closing the gap: nanobodies in research and therapy.Function (Oxford, England) · 2026Review
- Hidden gems bring proteins into view.Nature chemical biology · 2026Article
- Gluebodies Offer a Route To Improve Crystal Reliability and Diversity through Transferable Nanobody Mutations That Introduce Constitutive Close Contacts.ACS central science · 2025Article
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
Whilst cryo-electron microscopy(cryo-EM) has become a routine methodology in structural biology, obtaining high-resolution cryo-EM structures of small proteins (<100 kDa) and increasing overall throughput remain challenging. One approach to augment protein size and improve particle alignment involves the use of binding proteins or protein-based scaffolds. However, a given imaging scaffold or linking module may prove inadequate for structure solution and availability of such scaffolds remains limited. Here, we describe a strategy that exploits covalent dimerization of nanobodies to trap an engineered, predisposed nanobody-to-nanobody interface, giving Di-Gembodies as modular constructs created in homomeric and heteromeric forms. By exploiting side-chain-to-side-chain assembly, they can simultaneously display two copies of the same or two distinct proteins through a subunit interface that provides sufficient constraint required for cryo-EM structure determination. We validate this method with multiple soluble and membrane structural targets, down to 14 kDa, demonstrating a flexible and scalable platform for expanded protein structure determination.
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Registered trials
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