ArticleThe Biochemical journal1995
Catalytic activity of bovine seminal ribonuclease is essential for its immunosuppressive and other biological activities.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
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.
Who cites it
27 citing papers in PubMed, 72 citations in OpenAlex.
- Decoding bull fertility in vitro: a proteomics exploration from sperm to blastocyst.Reproduction (Cambridge, England) · 2025Article
- The EViruses · 2021Article
- Strengths and Challenges of Secretory Ribonucleases as AntiTumor Agents.Pharmaceutics · 2021Review
- Protein signatures of seminal plasma from bulls with contrasting frozen-thawed sperm viability.Scientific reports · 2020Article
- Esterification Delivers a Functional Enzyme into a Human Cell.ACS chemical biology · 2019Article
- Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs.Frontiers in immunology · 2019Review
- Surveillance of Tumour Development: The Relationship Between Tumour-Associated RNAs and Ribonucleases.Frontiers in pharmacology · 2019Review
- Immune Modulation by Human Secreted RNases at the Extracellular Space.Frontiers in immunology · 2018Review
- NMR studies on structure and dynamics of the monomeric derivative of BS-RNase: new insights for 3D domain swapping.PloS one · 2012Article
- Rational design and evaluation of mammalian ribonuclease cytotoxins.Methods in enzymology · 2012Article
- Arginine residues are more effective than lysine residues in eliciting the cellular uptake of onconase.Biochemistry · 2011Article
- Site-specific folate conjugation to a cytotoxic protein.Bioorganic & medicinal chemistry letters · 2011Article
- Site-specific PEGylation endows a mammalian ribonuclease with antitumor activity.Cancer biology & therapy · 2011Article
- Ribonucleases as potential modalities in anticancer therapy.European journal of pharmacology · 2009Review
- Influence of naturally-occurring 5'-pyrophosphate-linked substituents on the binding of adenylic inhibitors to ribonuclease a: an X-ray crystallographic study.Biopolymers · 2009Article
- Onconase cytotoxicity relies on the distribution of its positive charge.The FEBS journal · 2009Article
- Silencing an inhibitor unleashes a cytotoxic enzyme.Biochemistry · 2009Article
- Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity.Current pharmaceutical biotechnology · 2008Review
- Cytotoxic ribonucleases: the dichotomy of Coulombic forces.Biochemistry · 2007Article
- The RNase a superfamily: generation of diversity and innate host defense.Molecular diversity · 2006Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Bovine seminal ribonuclease (BS-RNase) is a homologue of RNase A with special biological properties, including potent immunosuppressive activity. A mutant BS-RNase was created in which His-119, the active-site residue that acts as a general acid during catalysis, was changed to an aspartic acid. H119D BS-RNase formed a dimer with quaternary structure similar to that of the wild-type enzyme but with values of kcat. and kcat./Km for the cleavage of UpA [uridylyl(3'-->5')adenosine] that were 4 x 10(3)-fold lower. The mutant protein also demonstrated dramatically decreased immunosuppressive, anti-tumour, aspermatogenic, and embryotoxic activities. The catalytic activity of BS-RNase is therefore necessary for its special biological properties.
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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.