Results 191 to 200 of about 30,415 (253)

A bioinspired pseudopeptide-based intracellular delivery platform enhances the cytotoxicity of a ribosome-inactivating protein through multiple death pathways.

Biomater Sci
Morrison G, Henry N, Kopytynski M, Chen R.   +3 more
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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
semanticscholar   +9 more sources

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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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   +4 more sources

In vitro anti‐tumour activity of anti‐CD80 and anti‐CD86 immunotoxins containing type 1 ribosome‐inactivating proteins

British Journal of Haematology, 2000
Immunotoxins specific for the CD80 and CD86 antigens were prepared by linking three type 1 ribosome‐inactivating proteins (RIPs), namely bouganin, gelonin and saporin‐S6, to the monoclonal antibodies M24 (anti‐CD80) and 1G10 (anti‐CD86). These immunotoxins showed a specific cytotoxicity for the CD80/CD86‐expressing cell lines Raji and L428.
Bolognesi A., Polito L., Tazzari P. L., Lemoli R. M., Lubelli C., Fogli M., Boon L., De Boer M., Stirpe F.   +8 more
openaire   +4 more sources

Cellular and subcellular distribution of saporins, type-1 ribosome-inactivating proteins, in soapwort (Saponaria officinalis L.)

Planta, 1994
Many plants contain ribosome-inactivating proteins (RIPs) which are either single enzymatically active polypeptides (type-1 RIPs) or heterodimers (type-2 RIPs) composed of an A-chain, functionally equivalent to a type-1 RIP, which is disulphide bonded to a sugar-binding B-chain.
Raffaella Carzaniga, Lesley Sinclair, Anthony P. Fordham-Skelton, Nick Harris, Ronald R. D. Croy   +4 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
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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
openaire   +2 more sources

Purification and Conjugation of Type 1 Ribosome-Inactivating Proteins

Methods in molecular biology, 2003
L, Barbieri, A, Bolognesi, F, 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
openaire   +2 more sources