ArticleBiomolecular NMR assignments2019
Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains.
Article in Biomolecular NMR assignments, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Olduvai Domains Downregulate Mitochondrial Pathways to Promote Human Brain Evolution and Neoteny.Research square · 2026Article
- Article
- Olduvai domain expression downregulates mitochondrial pathways: implications for human brain evolution and neoteny.bioRxiv : the preprint server for biology · 2024Article
- The Structural Dynamics, Complexity of Interactions, and Functions in Cancer of Multi-SAM Containing Proteins.Cancers · 2023Review
- Proteolytic activation of human-specific Olduvai domains by the furin protease.International journal of biological macromolecules · 2023Article
- Solution NMR backbone assignments of disordered Olduvai protein domain CON1 employing Hα-detected experiments.Biomolecular NMR assignments · 2022Article
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Authors and funding
8 authors.
Funding
Abstract
Olduvai protein domains, encoded primarily by NBPF genes, have been linked to both human brain evolution and cognitive diseases such as autism and schizophrenia. There are six primary domains that comprise the Olduvai family: three conserved domains (CON1-3) and three human lineage-specific domains (HLS1-3), which typically occur as a triplet (HLS1, HLS2 and HLS3). Herein, we present the solution NMR assignment of the backbone chemical shifts of the separate HLS1, 2 and 3 domains of NBPF15. Our data suggest that there is no change in the structure of the separate domains when compared to the full-length triplet (HLS1-HLS2-HLS3). We also demonstrate that there is no direct interaction between the three domains.
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