Literature DB >> 20843477

Ribonucleases of different origins with a wide spectrum of medicinal applications.

Evandro Fei Fang1, Tzi Bun Ng.   

Abstract

Ribonucleases (RNases) are a type of nucleases that catalyze the degradation of RNA into smaller components. They exist in a wide range of life forms from prokaryotes to eukaryotes. RNase-controlled RNA degradation is a determining factor in the control of gene expression, maturation and turnover, which are further associated with the progression of cancers and infectious diseases. Over the years, RNases purified from multiple origins have drawn increasing attention from medical scientists due to their remarkable antitumor properties. In this review, we present a brief summary of the representative RNases of fungal, bacterial, plant, and animal origins and outline their potential medicinal value in the treatment of tumor and AIDS. Among them, the most clinically promising RNases are mushroom RNases, Binase and Barnase from bacteria, ginseng RNases, and Onconase from frog (Rana pipiens). Fast developing protein engineering of RNases, which display more potent cytotoxic activity on and greater selectivity for malignant cells, has also aroused the interest of researchers. The multiple anti-cancer mechanisms of RNases are also included. To sum up, these inspiring studies unveil a new perspective for RNases as potential therapeutic agents. Copyright Â
© 2010 Elsevier B.V. All rights reserved.

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Year:  2010        PMID: 20843477     DOI: 10.1016/j.bbcan.2010.09.001

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  35 in total

1.  Site-specific PEGylation endows a mammalian ribonuclease with antitumor activity.

Authors:  Thomas J Rutkoski; John A Kink; Laura E Strong; Ronald T Raines
Journal:  Cancer Biol Ther       Date:  2011-08-01       Impact factor: 4.742

Review 2.  Killing of cancer cells through the use of eukaryotic expression vectors harbouring genes encoding nucleases and ribonuclease inhibitor.

Authors:  Elena M Glinka
Journal:  Tumour Biol       Date:  2015-04-01

3.  A novel ribonuclease with potent HIV-1 reverse transcriptase inhibitory activity from cultured mushroom Schizophyllum commune.

Authors:  Yong-Chang Zhao; Guo-Qing Zhang; Tzi-Bun Ng; He-Xiang Wang
Journal:  J Microbiol       Date:  2011-11-09       Impact factor: 3.422

4.  Arginine residues are more effective than lysine residues in eliciting the cellular uptake of onconase.

Authors:  Nadia K Sundlass; Ronald T Raines
Journal:  Biochemistry       Date:  2011-11-04       Impact factor: 3.162

5.  Site-specific folate conjugation to a cytotoxic protein.

Authors:  Bryan D Smith; Joshua J Higgin; Ronald T Raines
Journal:  Bioorg Med Chem Lett       Date:  2011-04-24       Impact factor: 2.823

Review 6.  Microbial ribonucleases (RNases): production and application potential.

Authors:  E Esin Hameş; Tuğçe Demir
Journal:  World J Microbiol Biotechnol       Date:  2015-10-03       Impact factor: 3.312

7.  Increased ribonuclease expression reduces inflammation and prolongs survival in TLR7 transgenic mice.

Authors:  Xizhang Sun; Alice Wiedeman; Nalini Agrawal; Thomas H Teal; Lena Tanaka; Kelly L Hudkins; Charles E Alpers; Silvia Bolland; Matthew B Buechler; Jessica A Hamerman; Jeffrey A Ledbetter; Denny Liggitt; Keith B Elkon
Journal:  J Immunol       Date:  2013-02-04       Impact factor: 5.422

8.  A Human Ribonuclease Variant and ERK-Pathway Inhibitors Exhibit Highly Synergistic Toxicity for Cancer Cells.

Authors:  Trish T Hoang; I Caglar Tanrikulu; Quinn A Vatland; Trieu M Hoang; Ronald T Raines
Journal:  Mol Cancer Ther       Date:  2018-10-03       Impact factor: 6.261

9.  Increased alkalotolerant and thermostable ribonuclease (RNase) production from alkaliphilic Streptomyces sp. M49-1 by optimizing the growth conditions using response surface methodology.

Authors:  Tuğçe Demir; Özkan Gübe; Mesut Yücel; E Esin Hameş-Kocabaş
Journal:  World J Microbiol Biotechnol       Date:  2013-03-27       Impact factor: 3.312

10.  A calcium ion-dependent dimeric bean lectin with antiproliferative activity toward human breast cancer MCF-7 cells.

Authors:  Randy Chi Fai Cheung; Ho Him Leung; Wen Liang Pan; Tzi Bun Ng
Journal:  Protein J       Date:  2013-03       Impact factor: 2.371

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