Identification of lysine residues in the binding domain of ribonuclease A for the RNase inhibitor from human placenta.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference45 articles.
1. Ribonuclease inhibitor from human placenta. Purification and properties.
2. Ribonuclease inhibitor from human placenta: rapid purification and assay.
3. Ribonuclease inhibitor from human placenta: interaction with derivatives of ribonuclease A.
4. On the Alkylation of Amino Acid Residues at the Active Site of Ribonuclease
5. The role of lysine-41 of ribonuclease A in the interaction with RNase inhibitor from human placenta.
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1. The Different Types and Varieties of Nucleic Acid Target Molecules;Principles and Technical Aspects of PCR Amplification;2008
2. Ribonuclease Inhibitor;Ribonucleases;1997
3. Mechanism of Ribonuclease Inhibition by Ribonuclease Inhibitor Protein Based on the Crystal Structure of its Complex with Ribonuclease A;Journal of Molecular Biology;1996-12
4. Thiol-Disulfide Exchange of Ribonuclease Inhibitor Bound to Ribonuclease A EVIDENCE OF ACTIVE INHIBITOR-BOUND RIBONUCLEASE;Journal of Biological Chemistry;1995-12
5. Interaction of semisynthetic variants of RNase A with ribonuclease inhibitor;Protein Science;1994-02
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