ArticleMolecular biology reports2002
Potential protein partners for the N-terminal domain of human topoisomerase I revealed by phage display.
Article in Molecular biology reports, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 7 citations in OpenAlex.
- Deletions initiated by the vaccinia virus TopIB protein in yeast.DNA repair · 2024Article
- Phage display: selecting straws instead of a needle from a haystack.Molecules (Basel, Switzerland) · 2011Review
- Cockayne syndrome group B cellular and biochemical functions.American journal of human genetics · 2003Review
- PP2A as a master regulator of the cell cycle.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phage display procedure was applied to the N-terminal domain of human topoisomerase I. The consensus sequence identified for clones binding to the N-terminal domain was found in 35 human proteins that are either permanently or temporarily located in the nucleus. They are in majority involved in the DNA repair, transcription, RNA metabolism or cell cycle control. Four of identified proteins: Bub3 protein, Cockayne syndrome protein A, damaged DNA binding protein 2 and GRWD protein belong to WD-repeat proteins and their sequences recognized by the N-terminal domain are identically localized.
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