Results 211 to 220 of about 25,832 (246)

Recent Progress in Research on Ribosome Inactivating Proteins

Current Protein and Peptide Science, 2009
The intent of this article is to review recent literature on ribosome inactivating proteins (RIPs) including isolation and characterization of new RIPs, studies on the crystal structures and mechanisms of actions of RIPs, the use of saporin-based neurotoxins to selectively lesion cholinergic neurons in neuroscience research, and the use of RIP-based ...
T B, Ng, Jack Ho, Wong, Hexiang, Wang
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Antiviral Activity Of Ribosome Inactivating Proteins In Medicine

Mini-Reviews in Medicinal Chemistry, 2004
Pokeweed antiviral protein and several other ribosome inactivating proteins are effective against a broad range of viruses. Recent results have shown that their enzymatic activity is not limited to depurination of the large rRNA, they can depurinate other nucleic acids, including viral RNAs.
Bijal A, Parikh, Nilgun E, Tumer
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Ribosome Inactivating Proteins and Apoptosis

2010
Ribosome inactivating proteins (RIPs) are RNA N-glycosidases which potently inhibit translation by inactivating ribosomes. RIPs have also been shown to possess the ability to induce apoptosis. A number of RIPs from different sources have been used to study the mechanism of apoptosis induction.
Deepa Sikriwal, Janendra K. Batra
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Ribosome-Inactivating Proteins in Cereals

2010
Plants constitutively accumulate proteins that are either toxic or inhibitory against pathogens, including ribosome-inactivating proteins (RIPs) and N-glycosidases that depurinate the universally conserved α-sarcin loop of large rRNAs. Cereal RIPs share a high similarity with all the other RIPs; however, they retain characteristic features forming a ...
Carlotta Balconi, Chiara Lanzanova, Mario Motto   +2 more
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The structure and function of ribosome-inactivating proteins

Trends in Plant Science, 1996
Many plants produce ribosome-inactivating proteins (RIPs) — enzymes that act on ribosomes in a highly specific way, thereby inhibiting protein synthesis. Some RIPs can bind to and enter cells, making them among the most toxic substances known. More commonly, however, RIPs are unable to enter healthy cells, and are therefore poorly cytotoxic. Their role
Martin R. Hartley, John A. Chaddock, Maureen S. Bonness   +2 more
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Virus resistance mediated by ribosome inactivating proteins

2000
Publisher Summary This chapter describes recent advances in understanding the structure and function of ribosome inactivating proteins (RIPs) and the mechanism of their antiviral activity. RIPs are widely distributed among plants, fungi, and bacteria.
P, Wang, N E, Tumer
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Ribosome inactivating proteins of plants.

Seminars in cell biology, 1992
Many plant tissues produce single chain proteins which can enzymatically remove a specific adenine residue from ribosomal RNA. Although these proteins are potently toxic to isolated ribosomes, they are non-toxic to intact cells, being unable to gain access to their ribosomal substrate.
J M, Lord, M R, Hartley, L M, Roberts
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Ribosome-inactivating proteins: From toxins to useful proteins

Toxicon, 2013
Ribosome-inactivating proteins (RIPs) either single-chain (type 1) or two-chain (type 2) are frequent in plants, often in multiple forms. They are RNA N-glycosidases, have antiviral, antifungal and insecticidal activity. Their expression in plants is increased under stressful conditions.
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Biotechnology of ribosome-inactivating proteins

1993
See the proper ...
SANITA' di TOPPI, LUIGI, SPANO' L.
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Sambucus Ribosome-Inactivating Proteins and Lectins

2010
Plant ribosome-inactivating proteins (RIPs) are inhibitors with RNA-N-glycosidase activity that irreversibly inactivate eukaryotic ribosomes, thereby impairing protein synthesis. In recent years, more than 40 RIPs and lectins belonging to the Sambucus genus have been isolated and characterized to varying degrees.
José Miguel Ferreras, Lucía Citores, Rosario Iglesias, Pilar Jiménez, Tomás Girbés   +4 more
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