ArticleNucleic acids research2017
Crystal structure of the N-terminal domain of human Timeless and its interaction with Tipin.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 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.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Article
- A new model for coordinating the functions of TIMELESS at the replication fork.bioRxiv : the preprint server for biology · 2025Article
- Article
- The TIMELESS effort for timely DNA replication and protection.Cellular and molecular life sciences : CMLS · 2023Review
- The Fork Protection Complex: A Regulatory Hub at the Head of the Replisome.Sub-cellular biochemistry · 2022Article
- Structure of a human replisome shows the organisation and interactions of a DNA replication machine.The EMBO journal · 2021Article
- SDE2 integrates into the TIMELESS-TIPIN complex to protect stalled replication forks.Nature communications · 2020Article
- Timeless couples G-quadruplex detection with processing by DDX11 helicase during DNA replication.The EMBO journal · 2020Article
- Crystal structure and interactions of the Tof1-Csm3 (Timeless-Tipin) fork protection complex.Nucleic acids research · 2020Article
- Cryo-EM Structure of the Fork Protection Complex Bound to CMG at a Replication Fork.Molecular cell · 2020Article
- Efficient and robust proteome-wide approaches for cross-linking mass spectrometry.Nature protocols · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Human Timeless is involved in replication fork stabilization, S-phase checkpoint activation and establishment of sister chromatid cohesion. In the cell, Timeless forms a constitutive heterodimeric complex with Tipin. Here we present the 1.85 Å crystal structure of a large N-terminal segment of human Timeless, spanning amino acids 1-463, and we show that this region of human Timeless harbours a partial binding site for Tipin. Furthermore, we identify minimal regions of the two proteins that are required for the formation of a stable Timeless-Tipin complex and provide evidence that the Timeless-Tipin interaction is based on a composite binding interface comprising different domains of Timeless.
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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.