Results 211 to 220 of about 35,431,844 (244)

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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A Simplified Procedure for the Purification of Trichosanthin (A Type 1 Ribosome Inactivating Protein) fromTrichosanthes kirilowiiRoot Tubers

Protein Expression and Purification, 1996
A one step rapid and simple purification procedure for trichosanthin, a type 1 ribosome inactivating protein, from root tubers of Trichosanthes kirilowii has been developed using cation-exchange perfusion chromatography. The identity of the protein has been confirmed by its size, immunoreactivity, and sequence information.
N, Bhatia, K A, McDonald, A P, Jackman, A M, Dandekar   +3 more
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Crystal structures of a type-1 ribosome inactivating protein from Momordica balsamina in the bound and unbound states

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2012
The ribosome inactivating proteins (RIPs) of type 1 are plant toxins that eliminate adenine base selectively from the single stranded loop of rRNA. We report six crystal structures, type 1 RIP from Momordica balsamina (A), three in complexed states with ribose (B), guanine (C) and adenine (D) and two structures of MbRIP-1 when crystallized with ...
Gajraj Singh, Kushwaha, Nisha, Pandey, Mau, Sinha, S Baskar, Singh, Punit, Kaur, Sujata, Sharma, Tej P, Singh   +6 more
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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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Enhanced cytotoxic activity of a bifunctional chimeric protein containing a type 1 ribosome-inactivating protein and a serine protease inhibitor

Biochimie, 2012
Both ribosome-inactivating proteins (RIPs) and plant proteinase inhibitors, belong to protein families known to regulate cellular homeostasis and likely involved in plant defense. Nevertheless the interest in these protein classes is due to their potential use for the treatment of several important human diseases such as cancer.
Rachele Tamburino, PIZZO, ELIODORO, SARCINELLI, CARMEN, Elia Poerio, Francesca Tedeschi, Anna G. Ficca, Augusto Parente, Antimo Di Maro   +7 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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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
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Purification, Characterization and Subcellular Localization of a Type‐1 Ribosome‐Inactivating Protein from the Sarcocarp of Cucurbita pepo

European Journal of Biochemistry, 1996
The flesh of the fruit of Cucurbita pepo contains a type‐1 ribosome‐inactivating protein (RIP), which we named pepocin. Pepocin was purified to apparent homogeneity by acid fractionation, ion‐exchange chromatography and adsorption chromatography. The protein was found to have a molecular mass of 26 kDa and a PI of about 9.9.
S, Yoshinari, S, Yokota, H, Sawamoto, S, Koresawa, M, Tamura, Y, Endo   +5 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
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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
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