Evidence map›Paper›PMID 12805565›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

The coiled-coil of the human Rad50 DNA repair protein contains specific segments of increased flexibility.

John van Noort, Thijn van Der Heijden, Martijn de Jager, Claire Wyman, Roland Kanaar, Cees Dekker

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
6.1field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. DNA Damage and Replication Stress Checkpoints.Annual review of biochemistry · 2025
    Review
  3. Dynamic Properties of the DNA Damage Response Mre11/Rad50 Complex.International journal of molecular sciences · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. The dynamic nature of the Mre11-Rad50 DNA break repair complex.Progress in biophysics and molecular biology · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Eukaryotic resectosomes: A single-molecule perspective.Progress in biophysics and molecular biology · 2017
    Review
  15. Article
  16. DNA End Resection: Facts and Mechanisms.Genomics, proteomics & bioinformatics · 2016
    Review
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

John van NoortDepartment of Nanoscience and Delft Institute of Microelectronics and Submicrontechnology, Delft University of Technology, Lorentzweg 1, 2628 CJ Delft, The Netherlands. noort@mb.tn.tudelft.nl
Thijn van Der Heijden
Martijn de Jager
Claire Wyman
Roland Kanaar
Cees Dekker
Delft University of Technology · NLJapan External Trade Organization · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein structural features are usually determined by defining regularities in a large population of homogeneous molecules. However, irregular features such as structural variation and flexibility are likely to be missed, despite their vital role for their biological function. In this paper, we report the observation of striking irregularities in the flexibility of the coiled-coil region of the human Rad50 DNA repair protein. Existing methods to quantitatively analyze flexibility are applicable to homogeneous polymers only. Because protein coiled-coils cannot be assumed to be homogeneous, we develop a method to quantify the local flexibility from high-resolution atomic force microscopy images. Indeed, in Rad50 coiled-coils, two positions of increased flexibility are observed. We discuss how this dynamic structural feature is integral to Rad50 function.

Indexed as

DNA RepairBiophysical PhenomenaBiophysicsDNADNA-Binding ProteinsHumansMicroscopy, Atomic ForceModels, MolecularModels, StatisticalProtein BindingProtein Structure, TertiarySaccharomyces cerevisiae ProteinsDNADNA-Binding ProteinsRAD50 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID12805565
PMCPMC164629
OpenAlexW2137212603

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.