ArticleScientific reports2017
ACCORD: an assessment tool to determine the orientation of homodimeric coiled-coils.
Article in Scientific reports, 2017. 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.
- Recombinant dimeric PICK1 peptide inhibitors for long-term relief of chronic pain by AAV therapeutics.Cell reports. Medicine · 2026Article
- Mechanisms driving open-closed transitions and dimer stability of the large GTPases hGBP1 and hGBP5.Frontiers in molecular biosciences · 2026Article
- Peptide and Protein Cyclization by a Promiscuous Graspetide Synthetase.ACS central science · 2025Article
- The art of designed coiled-coils for the regulation of mammalian cells.Cell chemical biology · 2024Review
- Functions of Gle1 are governed by two distinct modes of self-association.The Journal of biological chemistry · 2020Article
- Pro-Tumoral Functions of Autophagy Receptors in the Modulation of Cancer Progression.Frontiers in oncology · 2020Review
- A Structural View of Xenophagy, a Battle between Host and Microbes.Molecules and cells · 2018Review
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The coiled-coil (CC) domain is a very important structural unit of proteins that plays critical roles in various biological functions. The major oligomeric state of CCs is a dimer, which can be either parallel or antiparallel. The orientation of each α-helix in a CC domain is critical for the molecular function of CC-containing proteins, but cannot be determined easily by sequence-based prediction. We developed a biochemical method for assessing differences between parallel and antiparallel CC homodimers and named it ACCORD (Assessment tool for homodimeric Coiled-Coil ORientation Decision). To validate this technique, we applied it to 15 different CC proteins with known structures, and the ACCORD results identified these proteins well, especially with long CCs. Furthermore, ACCORD was able to accurately determine the orientation of a CC domain of unknown directionality that was subsequently confirmed by X-ray crystallography and small angle X-ray scattering. Thus, ACCORD can be used as a tool to determine CC directionality to supplement the results of in silico prediction.
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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.