ArticleNucleic acids research2003
Functional dissection of the C-terminal domain of type II DNA topoisomerase from the kinetoplastid hemoflagellate Leishmania donovani.
Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 13 papers.
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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
13 citing papers in PubMed, 31 citations in OpenAlex.
- A STDFT-CEEMD approach with wavelet packet thresholding for exon prediction in eukaryotic cells.Scientific reports · 2026Article
- Retraction of 'Functional dissection of the C-terminal domain of type II DNA topoisomerase from the kinetoplastid hemoflagellate Leishmania donovani'.Nucleic acids research · 2021Article
- Structural basis for allosteric regulation of Human Topoisomerase IIα.Nature communications · 2021Article
- Editorial Expression of Concern on article 'Functional dissection of the C-terminal domain of type II DNA topoisomerase from the kinetoplastid hemoflagellate Leishmania donovani'.Nucleic acids research · 2021Article
- Isobenzofuranone derivatives exhibit antileishmanial effect by inhibiting type II DNA topoisomerase and inducing host response.Pharmacology research & perspectives · 2014Article
- Trypanosomatids topoisomerase re-visited. New structural findings and role in drug discovery.International journal for parasitology. Drugs and drug resistance · 2014Review
- Article
- Centromere-associated topoisomerase activity in bloodstream form Trypanosoma brucei.Nucleic acids research · 2011Article
- In front of and behind the replication fork: bacterial type IIA topoisomerases.Cellular and molecular life sciences : CMLS · 2010Review
- mAMSA resistant human topoisomerase IIbeta mutation G465D has reduced ATP hydrolysis activity.Nucleic acids research · 2006Article
- Characterization of the ATPase activity of topoisomerase II from Leishmania donovani and identification of residues conferring resistance to etoposide.The Biochemical journal · 2005Article
- Impact of the C-terminal domain of topoisomerase IIalpha on the DNA cleavage activity of the human enzyme.Biochemistry · 2005Article
- Characterization of the DNA-binding domain and identification of the active site residue in the 'Gyr A' half of Leishmania donovani topoisomerase II.Nucleic acids research · 2005Article
Corrections and comments
- Retraction · 2021-05-07Duplication of/in Image · Investigation by Company/Institution · Investigation by Third Party · Manipulation of Images · Original Data and/or Images not Provided and/or not Available · Upgrade/Update of Prior Notice(s) · · see also: https://pubpeer.com/publications/34E9446142CBE8FCD55311F1EB9C1C
- Expression of concern · 2021-03-08Concerns/Issues about Data · Concerns/Issues about Image · Investigation by Third Party · Objections by Third Party · Original Data and/or Images not Provided and/or not Available · Updated to Retraction · · see also: https://pubpeer.com/publications/34E9446142CBE8FCD55311F1EB9C1C
- Expression of concern
- Retracted
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amino acid sequences of the C-terminal domain (CTD) of the type II DNA topoisomerases are divergent and species specific as compared with the highly conserved N-terminal and central domains. A set of C-terminal deletion mutants of Leishmania donovani topoisomerase II was constructed. Removal of more than 178 amino acids out of 1236 amino acid residues from the C-terminus inactivates the enzyme, whereas removal of 118 amino acids or less has no apparent effect on the ability of the parasite enzyme to complement a temperature-sensitive mutation of the Saccharomyces cerevisiae topoisomerase II gene. Deletion analysis revealed a potent nuclear localization signal (NLS) within the amino acid residues 998-1058. Immunomicroscopy results suggest that the removal of an NLS in the CTD is likely to contribute to the physiological dysfunction of these proteins. Modeling of the LdTOP2 based on the crystal structure of the yeast type II DNA topoisomerase showed that the parasite protein assumes a structure similar to its yeast counterpart harboring all the conserved residues in a structurally similar position. However, a marked difference in electrostatic potential was found in a span of 60 amino acid residues (998-1058), which also do not have any homology with topoisomerase II sequences. Such significant differences can be exploited by the structure-based design of selective inhibitors using the structure of the Leishmania enzyme as a template.
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