ArticleThe Biochemical journal2001
Second generation antitumour human RNase: significance of its structural and functional features for the mechanism of antitumour action.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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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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.
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Who cites it
3 citing papers in PubMed, 14 citations in OpenAlex.
- Structural features for the mechanism of antitumor action of a dimeric human pancreatic ribonuclease variant.Protein science : a publication of the Protein Society · 2009Article
- Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity.Current pharmaceutical biotechnology · 2008Review
- Highly selective toxic and proapoptotic effects of two dimeric ribonucleases on thyroid cancer cells compared to the effects of doxorubicin.British journal of cancer · 2004Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A second generation mutant of dimeric human pancreas RNase (HHP2-RNase), was obtained by a single residue mutation (Glu(111)-->Gly) of the previously described dimeric human pancreas RNase variant (HHP-RNase). HHP2-RNase was found to be a highly specific antitumour agent, with an enhanced cytotoxic activity compared with HHP-RNase. The structural and functional requisites of the antitumour action of HHP2-RNase were investigated and compared with those of other dimeric antitumour RNases. The stability of the dimeric structure, i.e. the resistance of human dimeric RNase variants to reductive cleavage of the two intersubunit disulphide bonds that bridge the subunits, was determined to be an essential feature of antitumour dimeric RNases. The stability of the dimeric structure is in turn responsible for the resistance to inhibition by the cytosolic RNase inhibitor (cRI). Both the stability of the dimeric structure and the resistance to cRI inhibition appeared to be highly enhanced by an RNase substrate. This suggests a possible role for RNA in the amplification of the antitumour potential of dimeric RNases.
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Registered trials
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.