ArticleScience advances2026
The CENP-A chaperone complex spatially organizes centromeres.
Article in Science advances, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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
2 citing papers in PubMed.
- Dual Roads of CENP-A for Centromere Identification.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- M18BP1 valency and a distributed interaction footprint determine epigenetic centromere specification in humans.The EMBO journal · 2026Article
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Authors and funding
10 authors.
Funding
Abstract
Centromeres, defined by CENP-A-containing nucleosomes, direct kinetochore assembly for spindle attachment. In mitosis, CENP-A and the constitutive centromere-associated network (CCAN) of the inner kinetochore are arranged into bipartite subdomains within clearings of chromatin. However, less is known about their architecture during interphase. We report here an unrecognized structural role for the CENP-A chaperone machinery in establishing interphase centromere architecture. In interphase, CENP-A and the CCAN assemble conserved shell-like structures that enclose a chromatin-poor central cavity. This cavity is occupied by the interphase-specific CENP-A chaperone complex, which promotes CENP-A assembly once per cell cycle. The presence of the chaperone complex, but not its CENP-A-incorporating activity, is required to generate both the shell architecture and chromatin clearing. The CCAN scaffold CENP-C exhibits radial organization throughout the structure and is essential for its formation, primarily by recruiting the HJURP chaperone. Our findings broaden the role of the CENP-A chaperone machinery to include the structural organization of interphase vertebrate centromeres, independent of CENP-A deposition.
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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.