By Fiorenzo Stirpe, Douglas Lappi
This crucial reference presents updated info on all features of ribosome-inactivating proteins (RIPs). together with a listing of all identified RIPs, their distribution in nature, constitution, genetics and chemical and immunological homes, this reference covers mechanisms of motion, together with the enzymatic job on numerous polynucleotide substrates; the interplay with, and access into cells; the toxicity to animals, together with the pathology of poisoning; and the immunomodulatory and allergenic job. The booklet additional emphasizes using immunotoxins and different conjugates in medical trials for the treatment of melanoma and intractable soreness.
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Additional resources for Ribosome-inactivating Proteins: Ricin and Related Proteins
2000;128:883–889. Chen ZC, White RF, Antoniw JF, Lin Q. Effect of pokeweed antiviral protein (PAP) on the infection of plant viruses. Plant Pathology. 1991;40:612–620. Irvin JD. Pokeweed antiviral protein. Pharmacology and Therapeutics. 1983;21:371–387. Tomlinson JA, Walker VM, Flewett TH, Barclay GR. The inhibition of infection by cucumber mosaic virus and influenza virus by extracts from phytolacca americana. J Gen Virol. 1974;22:225–232. Ussery MA, Irvin JD, Hardesty B. Inhibition of poliovirus replication by a plant antiviral peptide.
5). This novel chimeric protein will further be referred to as a type [AM] RIP (A fused to unknown C-terminal domain). 9–11 However, until now no evidence has been presented that any of these presumed RIPs comprises a domain that is structurally and evolutionarily related to the A chains of either bacterial Stx or plant RIPs. OCCURRENCE AND TAXONOMICAL DISTRIBUTION OF RIBOSOME-INACTIVATING PROTEINS 25 One group of fungal proteins/genes that is often referred to as RIPs belongs to the family of fungal ribotoxins.
Kurinov IV, Uckun FM. High resolution X-ray structure of potent anti-HIV pokeweed antiviral protein-III. Biochem Pharmacol. 2003;65:1709–1717. Ruggiero A, Chambery A, Di Maro A, et al. Crystallization and preliminary X-ray diffraction analysis of PD-L1, a highly glycosylated ribosome inactivating protein with DNase activity. Protein Pept Lett. 2007;14:407–409. Ruggiero A, Chambery A, Di Maro A, et al. 1 A) structure of the ribosome-inactivating protein PD-L4 from Phytolacca dioica L. leaves. Proteins.
Ribosome-inactivating Proteins: Ricin and Related Proteins by Fiorenzo Stirpe, Douglas Lappi