Evidence map›Paper›PMID 15128941›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

Reduction in DNA-binding affinity of Cys2His2 zinc finger proteins by linker phosphorylation.

Derek Jantz, Jeremy M Berg

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

29 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Reassessing BenignGenes · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Transcription factors and transporters in zinc homeostasis: lessons learned from fungi.Critical reviews in biochemistry and molecular biology · 2020
    Review
  10. Article
  11. Article
  12. Protein phosphatases in chromatin structure and function.Biochimica et biophysica acta. Molecular cell research · 2019
    Review
  13. CTCF and cellular heterogeneity.Cell & bioscience · 2019
    Review
  14. Article
  15. Zinc finger proteins in cancer progression.Journal of biomedical science · 2016
    Review
  16. Article
  17. Article
  18. Article
  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

2 authors at 1 institution in 1 country.

Derek JantzDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. bergj@mail.nih.gov
Jeremy M Berg
Johns Hopkins Medicine · US

Funding

MULTIDOMAIN METALLOPROTEINSR01GM046257 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI AMANN, BARBARA T · 1991 to 2004
$720k
NIGMS NIH HHS GM04627NIGMS NIH HHS R01 GM046257
6 · The paper itself

Abstract

Cys(2)His(2) zinc finger proteins make up the largest class of transcription factors encoded in the genomes of higher eukaryotes. Recent studies of the Ikaros transcription factor demonstrated that this zinc finger protein undergoes cell cycle-dependent changes in association with DNA that seem to be due to phosphorylation of Thr or Ser residues in the linker regions connecting adjacent zinc finger domains. The high degree of conservation of this linker sequence within the Cys(2)His(2) superfamily suggested a common mechanism for the cell cycle-dependent modulation of DNA-binding affinity throughout this large class of transcription factors. The effects of linker phosphorylation on DNA-binding affinity were investigated through a direct comparison of the DNA-binding properties of four synthetic zinc finger proteins produced by native chemical ligation. The four proteins, comprising three zinc finger domains joined by two consensus Thr-Gly-Glu-Lys-Pro linkers, correspond to all four possible combinations of linker Thr phosphorylation states. Fluorescence-based DNA-binding studies of a specific DNA-binding site revealed that phosphorylation of a single linker reduced binding affinity approximately 40-fold, whereas phosphorylation of both linkers reduced binding affinity 130-fold. These results with purified components demonstrate that linker phosphorylation does, indeed, produce a significant reduction in DNA-binding affinity and support a model wherein a single cell cycle-dependent Ser/Thr kinase could simultaneously inactivate a large number of zinc finger transcription factors.

Indexed as

Amino Acid SequenceCarbon DioxideDNAMolecular Sequence DataPhosphoproteinsPhosphorylationProtein BindingCarbon DioxideDNAPhosphoproteins

Identifiers

PMID15128941
PMCPMC419650
OpenAlexW2012222076

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.