Results 201 to 210 of about 30,415 (253)
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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 +9 more
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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 +9 more
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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. +5 more
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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. +5 more
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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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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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A new type 1 ribosome-inactivating protein from the seeds of Gypsophila elegans M.Bieb.
Phytochemistry, 2019Ribosome-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 +3 more
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Endocytosis and intracellular localisation of type 1 ribosome-inactivating protein saporin-s6.
Journal of biological regulators and homeostatic agents, 2012Saporin-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 +9 more
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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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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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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 +5 more
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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 +5 more
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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 +5 more
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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 +5 more
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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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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
2023Nowadays, 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 +8 more
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