Major Structural Differences between Pokeweed Antiviral Protein and Ricin A-Chain do not Account for their Differing Ribosome Specificity
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1996.00159.x/fullpdf
Reference30 articles.
1. X-ray Structure of a Pokeweed Antiviral Protein, Coded by a New Genomic Clone, at 0.23 nm Resolution. A Model Structure Provides a Suitable Electrostatic Field for Substrate Binding
2. A maize ribosome-inactivating protein is controlled by the transcriptional activator Opaque-2.
3. Mutagenesis and kinetic analysis of the active site Glu177 of ricin A-chain
4. Pokeweed antiviral protein (PAP) mutations which permitE.coligrowth do not eliminate catalytic activity towards prokaryotic ribosomes
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1. Double-Coated Nanoparticle of Ribosome Inactivating Protein (RIP) from Mirabilis jalapa L. prepared from Chitosan-Sodium Tripolyphosphate and Alginate-Calcium Chloride: The New Strategy for Protein Drug in Oral Delivery;BIO Web of Conferences;2023
2. Expression of novel fusion antiviral proteins ricin a chain-pokeweed antiviral proteins (RTA-PAPs) in Escherichia coli and their inhibition of protein synthesis and of hepatitis B virus in vitro;BMC Biotechnology;2018-08-06
3. Maize Ribosome-Inactivating Protein Uses Lys158–Lys161 to Interact with Ribosomal Protein P2 and the Strength of Interaction Is Correlated to the Biological Activities;PLoS ONE;2012-12-12
4. Immunity to Ricin: Fundamental Insights into Toxin–Antibody Interactions;Current Topics in Microbiology and Immunology;2011
5. X-ray crystallographic analysis of the structural basis for the interaction of pokeweed antiviral protein with guanine residues of ribosomal RNA;Protein Science;2008-12-31
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