ArticleThe Journal of biological chemistry2019
Solution structure and flexibility of the condensin HEAT-repeat subunit Ycg1.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 12 citations in OpenAlex.
- Condensin complexes: from chromatin organization to disease.Nucleus (Austin, Tex.) · 2026Review
- Conformational Stability of the N-Terminal Region of MDM2.Molecules (Basel, Switzerland) · 2023Article
- Structural insights into DNA loop extrusion by SMC protein complexes.Current opinion in structural biology · 2020Review
- Condensin complexes: understanding loop extrusion one conformational change at a time.Biochemical Society transactions · 2020Review
- A Role forCells · 2020Article
- Methods, development and applications of small-angle X-ray scattering to characterize biological macromolecules in solution.Current research in structural biology · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High-resolution structural analysis of flexible proteins is frequently challenging and requires the synergistic application of different experimental techniques. For these proteins, small-angle X-ray scattering (SAXS) allows for a quantitative assessment and modeling of potentially flexible and heterogeneous structural states. Here, we report SAXS characterization of the condensin HEAT-repeat subunit Ycg1
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Registered trials
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