Transition State Structure of RNA Depurination by Saporin L3
Author:
Affiliation:
1. Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, New York 10461, United States
Funder
National Cancer Institute
Albert Einstein College of Medicine, Yeshiva University
National Institute of General Medical Sciences
Publisher
American Chemical Society (ACS)
Subject
Molecular Medicine,General Medicine,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acschembio.5b01069
Reference59 articles.
1. RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes.
2. Unexpected activity of saporins
3. Isolation and enzymatic characterization of lamjapin, the first ribosome-inactivating protein from cryptogamic algal plant (Laminaria japonicaA)
4. Polynucleotide:adenosine glycosidase activity of ribosome-inactivating proteins: effect on DNA, RNA and poly(A)
5. Ribosome-inactivating proteins depurinate poly(ADP-ribosyl)ated poly(ADP-ribose) polymerase and have transforming activity for 3T3 fibroblasts
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