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Ribosome-inactivating proteins

Toxicon, 2004
The known toxic and non-toxic ribosome-inactivating proteins are listed and classified and their nature, distribution mechanism of action and other properties are described.
Fiorenzo Stirpe
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Microenvironment of Cysteine 242 in Type-1 Ribosome-Inactivating Protein from Iris

Biochemical and Biophysical Research Communications, 2000
IRIP is a type-1 ribosome-inactivating protein isolated from the bulbs of Iris hollandica. It is one of the few type-1 RIPs that contain Cys residue(s) in their primary sequence. IRIP contains a single Cys residue at position 242. Although IRIP is thought to be a monomeric protein, SDS-PAGE indicates that part of the IRIP molecules can exist as ...
Q, Hao, E J, Van Damme, A, Barre, A, Sillen, P, Rougé, Y, Engelborghs, W J, Peumans   +6 more
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Structure/function studies on two type 1 ribosome inactivating proteins: Bouganin and lychnin

Journal of Structural Biology, 2009
The three-dimensional structures of two type 1 RIPs, bouganin and lychnin, has been solved. Their adenine polynucleotide glycosylase activity was also determined together with other known RIPs: dianthin 30, PAP-R, momordin I, ricin A chain and saporin-S6. Saporin-S6 releases the highest number of adenine molecules from rat ribosomes, and poly(A), while
FERMANI, SIMONA, TOSI, GIOVANNA, FARINI, VALENTINA, POLITO, LETIZIA, FALINI, GIUSEPPE, RIPAMONTI, ALBERTO, BARBIERI, LUIGI, Chambery A., BOLOGNESI, ANDREA   +8 more
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Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins

Molecules, 2016
Ribosome-inactivating proteins (RIPs) including ricin, Shiga toxin, and trichosanthin, are RNA N-glycosidases that depurinate a specific adenine residue (A-4324 in rat 28S ribosomal RNA, rRNA) in the conserved α-sarcin/ricin loop (α-SRL) of rRNA.
Pang-Chui Shaw, Kam-Bo Wong, Amanda Nga-Sze Mak   +2 more
exaly   +2 more sources

The type-1 ribosome-inactivating protein OsRIP1 triggers caspase-independent apoptotic-like death in HeLa cells

Food and Chemical Toxicology, 2021
Ribosome-inactivating proteins (RIPs) are capable of removing a specific adenine from 28S ribosomal RNA, thus inhibiting protein biosynthesis in an irreversible manner. In this study, recombinant OsRIP1, a type 1 RIP from rice (Oryza sativa L.), was investigated for its anti-proliferative properties.
Simin Chen, Cláudia Figueiredo Lóssio, Isabel Verbeke, Joost Verduijn, Bogdan Parakhonskiy, Louis Van der Meeren, Pengyu Chen, Jeroen De Zaeytijd, André G. Skirtach, Els J.M. Van Damme   +9 more
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Targeting of Type 1 Ribosome-Inactivating Proteins to CD30+ or CD25+ Hematologic Neoplasias by Bispecific Antibodies

Journal of Hematotherapy, 1995
In this study, we compared the ability of different bispecific monoclonal antibodies (BsmAb) and immunotoxins to deliver the type 1 ribosome-inactivating proteins (RIP) saporin and gelonin through the CD25 or CD30 target molecules to Hodgkin's lymphoma cells.
S, Sforzini, A, Bolognesi, R, Meazza, S, Marciano, P L, Tazzari, H, Stein, F, Stirpe, S, Ferrini   +7 more
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Use of blue‐sepharose for purification of immunotoxin containing type 1 ribosome‐inactivating protein, gelonin

Biomedical Chromatography, 1994
AbstractThis paper describes a method suitable for purifying immunotoxin containing type 1 ribosome‐inactivating protein, gelonin. The separation of free (unreacted) 80G, a monoclonal antibody against α‐fetoprotein (AFP), from semipurified 80G–gelonin conjugate was unsuccessful by conventional CM‐Sepharose ion‐exchange chromatography because the ...
K, Masuda, K, Hirano, Y, Takagishi
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Sequence determination of lychnin, a type 1 ribosome-inactivating protein from Lychnis chalcedonica seeds

Biological Chemistry, 2006
The complete amino acid sequence of lychnin, a type 1 ribosome-inactivating protein (RIP) isolated from Lychnis chalcedonica seeds, has been determined by automated Edman degradation and ESI-QTOF mass spectrometry. Lychnin consists of 234 amino acid residues with a molecular mass of 26 131.14 Da. All amino acid residues involved in the formation of the
Chambery A., de Donato A., BOLOGNESI, ANDREA, POLITO, LETIZIA, STIRPE, FIORENZO, Parente A.   +5 more
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Isolation and characterization of heterotepalins, type 1 ribosome-inactivating proteins from Phytolacca heterotepala leaves

Phytochemistry, 2007
Leaves from Phytolacca heterotepala H. Walter (Mexican pokeweed) contain at least 10 type 1 RIP isoforms, named heterotepalins. Their Mr values are included in the range 28,000-36,000, as shown by SDS-PAGE performed under reduced conditions and the pI values in the pH range 8.50-9.50. Some heterotepalins are glycosylated.
DI MARO, Antimo, CHAMBERY, Angela, DANIELE A., CASORIA P., PARENTE A.   +4 more
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A new type 1 ribosome-inactivating protein from the seeds of Gypsophila elegans M.Bieb.

Phytochemistry, 2019
Ribosome-inactivating proteins (RIPs) are enzymes with N-glycosylase activity that remove adenine bases from the ribosomal RNA. In theory, one single RIP molecule internalized into a cell is sufficient to induce cell death. For this reason, RIPs are of high potential as toxic payload for anti-tumor therapy. A considerable number of RIPs are synthesized
Kokorin, Arsenij, Weise, Christoph, Sama, Simko, Weng, Alexander   +3 more
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