Results 191 to 200 of about 21,394 (229)

Endocytosis and intracellular localisation of type 1 ribosome-inactivating protein saporin-s6.

Journal of biological regulators and homeostatic agents, 2012
Saporin-S6 is a single-chain ribosome-inactivating protein (RIP) that has low toxicity in cells and animals. When the protein is bound to a carrier that facilitates cellular uptake, the protein becomes highly and selectively toxic to the cellular target of the carrier.
BOLOGNESI, ANDREA, POLITO, LETIZIA, SCICCHITANO, VITTORIA, ORRICO, CATIA, PASQUINELLI, GIANANDREA, MUSIANI, SILVIA, Santi S., RICCIO, MASSIMO, BORTOLOTTI, MASSIMO, BATTELLI, MARIA GIULIA   +9 more
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Type-1 ribosome-inactivating protein from iris (Iris hollandica var. Professor Blaauw) binds specific genomic DNA fragments

Biochemical Journal, 2001
The capacity of IRIP, a type-1 ribosome-inactivating protein (RIP) isolated from the bulbs of Iris hollandica, to bind specific DNA sequences from a mixture of approx. 200bp (average length) fragments of total genomic DNA from Iris genome was studied. Fragments that were preferentially bound by IRIP were enriched by several cycles of affinity binding ...
Q, Hao, W J, Peumans, E J, Van Damme
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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   +1 more source

Type-1 ribosome-inactivating protein from iris bulbs: a useful agronomic tool to engineer virus resistance?

Plant Molecular Biology, 2003
To study the in planta antiviral activity of a type-1 ribosome-inactivating protein from iris bulbs, called IRIP, Nicotiana tabacum cv. Samsun NN was transformed with the IRIP sequence expressed under the control of the 35S cauliflower mosaic virus promoter.
Stijn, Desmyter, Frank, Vandenbussche, Qiang, Hao, Paul, Proost, Willy J, Peumans, Els J M, Van Damme   +5 more
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A novel type-1 ribosome-inactivating protein isolated from the supernatant of transformed suspension cultures of Trichosanthes kirilowii

Plant Cell Reports, 1998
A type-1 ribosome-inactivating protein (RIP) designated TK-35 has been purified from the supernatant of suspension cultures of Agrobacterium rhizogenes-transformed stem sections of Trichosanthes kirilowii. The protein was purified from the supernatant by PerSeptive SH/M cation exchange and Sephadex G-75 S gel permeation chromatography.
N-J, Remi Shih, K A, McDonald, A M, Dandekar, T, Girbés, R, Iglesias, A P, Jackman   +5 more
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The mechanism of action of barley toxin: a type 1 ribosome-inactivating protein with RNA N-glycosidase activity

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
In a previous report (Endo, Y. and Tsurugi, K. (1987) J. Biol. Chem. 262, 8128-8130) it was shown that the RNA N-glycosidase activity of ricin A-chain was responsible for the ability of this protein to inactivate eukaryotic ribosomes. The objective of the present study was to determine whether a similar mechanism was used by a ribosome-inactivating ...
Y, Endo, K, Tsurugi, R F, Ebert
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GENOTOXIC EVALUATION IN ZEBRAFISH OF QUINOIN, TYPE 1 RIBOSOME-INACTIVATING PROTEIN FROM QUINOA SEEDS

2023
Nowadays, functional foods have greatly increased attention thanks to the numerous benefits for human health. Among them, quinoa contains all essential amino acids and minerals, for which is particularly suitable for consumption. However, quinoin (~30- kDa), a toxic enzyme classified as ribosome inactivating protein (RIP, EC: 3.2.2.22)1, recently found
F. Mottola, M. Carannante, N. Landi, S. Ragucci, R. Scudiero, M. Della Corte, D. Paciolla, A. Di Maro, L. Rocco   +8 more
openaire   +1 more source

Gypsophilin, a New Type 1 Ribosome-inactivating Protein fromGypsophila elegans: Purification, Enzymatic Characterization, and Subcellular Localization

Bioscience, Biotechnology, and Biochemistry, 1997
Gypsophila elegans contains a new type 1 ribosome-inactivating protein, which we named gypsophilin. The protein was purified to apparent homogeneity by (NH4)2SO4 fractionation, ion-exchange chromatography, and adsorption chromatography. The protein was found to have a molecular mass of 28.0 kDa and a pI of about 10.1.
S, Yoshinari, S, Koresawa, S, Yokota, H, Sawamoto, M, Tamura, Y, Endo   +5 more
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Structure/funcion studies on type 1 ribosome inactivating proteins.

2008
Ribosome inactivating proteins (RIPs) are toxins, which depurinate major RNA inhibiting protein synthesis1. The cleaved N-glycosidic bond corresponds to a specific adenine located in the sarcin/ricin loop, highly conserved in rRNAs from different species and essential for interaction with elongation factors.
FERMANI, SIMONA, TOSI, GIOVANNA, FARINI, VALENTINA, POLITO, LETIZIA, FALINI, GIUSEPPE, RIPAMONTI, ALBERTO, BARBIERI, LUIGI, A. Chambery, BOLOGNESI, ANDREA   +8 more
openaire   +1 more source

Atomic resolution structure of cucurmosin, a novel type 1 ribosome-inactivating protein from the sarcocarp of Cucurbita moschata

Journal of Structural Biology, 2008
A novel type 1 ribosome-inactivating protein (RIP) designated cucurmosin was isolated from the sarcocarp of Cucurbita moschata (pumpkin). Besides rRNA N-glycosidase activity, cucurmosin exhibits strong cytotoxicities to three cancer cell lines of both human and murine origins, but low toxicity to normal cells.
Xiaomin, Hou, Edward J, Meehan, Jieming, Xie, Mingdong, Huang, Minghuang, Chen, Liqing, Chen   +5 more
openaire   +2 more sources