ArticleBioconjugate chemistry2012
Assembly of protein building blocks using a short synthetic peptide.
Article in Bioconjugate chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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
10 citing papers in PubMed.
- Tuning the Dimensionality of Protein-Peptide Coassemblies to Build 2D Conductive Nanomaterials.ACS nano · 2025Article
- Transcytosis-Driven Treatment of Neurodegenerative Disorders by mRNA-Expressed Antibody-Transferrin Conjugates.Biomedicines · 2024Review
- SNARE Modulators and SNARE Mimetic Peptides.Biomolecules · 2022Review
- Engineering Botulinum Toxins to Improve and Expand Targeting and SNARE Cleavage Activity.Toxins · 2018Review
- Article
- Unexpected transcellular protein crossover occurs during canonical DNA transfection.Journal of cellular biochemistry · 2014Article
- Solid-phase bioconjugation of heterobifunctional adaptors for versatile assembly of bispecific targeting ligands.Bioconjugate chemistry · 2014Article
- Botulinum protease-cleaved SNARE fragments induce cytotoxicity in neuroblastoma cells.Journal of neurochemistry · 2014Article
- Synthetic self-assembling clostridial chimera for modulation of sensory functions.Bioconjugate chemistry · 2013Article
- Stapling of the botulinum type A protease to growth factors and neuropeptides allows selective targeting of neuroendocrine cells.Journal of neurochemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
Combining proteins or their defined domains offers new enhanced functions. Conventionally, two proteins are either fused into a single polypeptide chain by recombinant means or chemically cross-linked. However, these strategies can have drawbacks such as poor expression (recombinant fusions) or aggregation and inactivation (chemical cross-linking), especially in the case of large multifunctional proteins. We developed a new linking method which allows site-oriented, noncovalent, yet irreversible stapling of modified proteins at neutral pH and ambient temperature. This method is based on two distinct polypeptide linkers which self-assemble in the presence of a specific peptide staple allowing on-demand and irreversible combination of protein domains. Here we show that linkers can either be expressed or be chemically conjugated to proteins of interest, depending on the source of the proteins. We also show that the peptide staple can be shortened to 24 amino acids still permitting an irreversible combination of functional proteins. The versatility of this modular technique is demonstrated by stapling a variety of proteins either in solution or to surfaces.
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What OpenQuestion holds
Registered trials
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.