Results 181 to 190 of about 21,394 (229)

Type 1 Ribosome-Inactivating Proteins from the Ombú Tree (Phytolacca dioica L.)

Planta, 2010
The toxicity of plant proteins, later identified as ribosome-inactivating proteins (RIPs), was described more than a century ago and their enzymatic activity was established more than 30 years ago. However, their physiological role and related biological activities are still uncertain.
PARENTE A, BERISIO R, CHAMBERY, Angela, DI MARO, Antimo   +3 more
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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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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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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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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
openaire   +2 more sources

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
openaire   +3 more sources

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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Clavin, a Type‐1 Ribosome‐Inactivating Protein from Aspergillus clavatus IF0 8605

European Journal of Biochemistry, 1996
We describe the cloning and expression of a new cDNA from the filamentous fungus Aspergillus clavatus IFO 8605. This cDNA contains an open reading frame (ORF) that predicts a putative ribonuclease precursor with high similarity to the α‐sarcin family of ribosome‐inactivating proteins (RIPS).
Dino Parente, Giuseppe Raucci, Bruna Celano, Aurelio Pacilli, Lorenzo Zanoni, Silvana Canevari, Elena Adobati, Maria I. Colnaghi, Franco Dosio, Silvia Arpicco, Luigi Cattel, Antonio Mele, Rita De Santis   +12 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
Arsenij, Kokorin, Christoph, Weise, Simko, Sama, Alexander, Weng   +3 more
openaire   +2 more sources

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
openaire   +2 more sources