相似文献
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Inhibition of protein degradation induced by dimeric ribonuclease A in hepatoma cells [proceedings].
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Comparison of antitumor activities of pancreatic ribonuclease and its cross-linked dimer.
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引用本文的文献
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RNase A Domain-Swapped Dimers Produced Through Different Methods: Structure-Catalytic Properties and Antitumor Activity.
Life (Basel). 2021 Feb 21;11(2):168. doi: 10.3390/life11020168.
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Ribonucleases endowed with specific toxicity for spermatogenic layers.
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Antitumor activity of ribonuclease multimers created by site-specific covalent tethering.
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A hinge region cis-proline in ribonuclease A acts as a conformational gatekeeper for C-terminal domain swapping.
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Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity.
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Oligomerization of bovine ribonuclease A: structural and functional features of its multimers.
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The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolution.
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The activity on double-stranded RNA of aggregates of ribonuclease A higher than dimers increases as a function of the size of the aggregates.
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Catalytic activity of bovine seminal ribonuclease is essential for its immunosuppressive and other biological activities.
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