Full Antitumor Action of Recombinant Seminal Ribonuclease Depends on the Removal of Its N-Terminal Methionine
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Cited by 39 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. A novel ribonuclease with HIV-1 reverse transcriptase inhibitory activity purified from the fungusRamaria formosa;Journal of Basic Microbiology;2014-02-12
2. Improved detection of variants in recombinant human interferon alpha-2a products by reverse-phase high-performance liquid chromatography on a core–shell stationary phase;Journal of Pharmaceutical and Biomedical Analysis;2014-01
3. Double Domain Swapping in Bovine Seminal RNase: Formation of Distinct N- and C-swapped Tetramers and Multimers with Increasing Biological Activities;PLoS ONE;2012-10-11
4. Enforcing the positive charge of N-termini enhances membrane interaction and antitumor activity of bovine seminal ribonuclease;Biochimica et Biophysica Acta (BBA) - Biomembranes;2011-12
5. A novel ribonuclease with potent HIV-1 reverse transcriptase inhibitory activity from cultured mushroom Schizophyllum commune;The Journal of Microbiology;2011-10
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