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Novel role for pectin methylesterase in Arabidopsis: A new function showing ribosome-inactivating protein (RIP) activity

Biochimica Et Biophysica Acta - General Subjects, 2008
Ribosome-inactivating proteins (RIPs, EC 3.2.2.22) are plant enzymes that can inhibit the translation process by removing single adenine residues of the large rRNA. These enzymes are known to function in defense against pathogens, but their biological role is unknown, partly due to the absence of work on RIPs in a model plant.
Jorge Vivanco   +2 more
exaly   +3 more sources

Enzymatic properties of ribosome-inactivating proteins (RIPs) and related toxins

Life Sciences, 1991
Ribosome-inactivating proteins (RIPs) are a group of proteins that inhibit protein synthesis in eucaryotic cells. While the biological effects have been well characterized, the underlying enzymatic mechanisms have not been elucidated until recently. Two different mechanisms have been identified. Plant and bacterial RIPs act as N-glycosidases.
W.P. Fong   +3 more
openaire   +2 more sources

Ribosome-Inactivating Proteins with an Emphasis on Bacterial RIPs and their Potential Medical Applications

Future Microbiology, 2012
Ribosome-inactivating proteins (RIPs) are toxic due to their N-glycosidase activity catalyzing depurination at the universally conserved α-sarcin loop of the 60S ribosomal subunit. In addition, RIPs have been shown to also have other enzymatic activities, including polynucleotide:adenosine glycosidase activity.
Ana G, Reyes   +2 more
openaire   +2 more sources

Ribosome-Inactivating and Related Proteins [PDF]

open access: yesToxins, 2015
Ribosome-inactivating proteins (RIPs) are toxins that act as N-glycosidases (EC 3.2.2.22). They are mainly produced by plants and classified as type 1 RIPs and type 2 RIPs.
Alexander Weng, Matthias F Melzig
exaly   +2 more sources

Ribosome Inactivating Proteins (RIPs) from Momordica charantia for Anti Viral Therapy

Current Molecular Medicine, 2009
This review describes the nature and applications of ribosome inactivating proteins (RIPs) from Momordica charantia (bitter melon). RIPs from the plant kingdom have received much attention in biomedical research because they target conserved host protein synthesis machinery and show specificity towards human and animal cell targets.
M, Puri   +5 more
openaire   +2 more sources

Molecular action of the type 1 ribosome-inactivating protein saporin 5 onVicia sativaribosomes [PDF]

open access: yesFEBS Letters, 1993
The type 1 ribosome-inactivating protein (RIP) saporin 5 isolated from seeds of Saponaria officinalis L. strongly inhibited translation carried out by Vicia sativa L. purified ribosomes. The toxin multidepurinated V.
Francisco Javier Arias   +2 more
exaly   +2 more sources

Different in vitro toxicities of structurally similar type I ribosome-inactivating proteins (RIPs)

Toxicology in Vitro, 2010
This study was aimed at investigating and comparing the cytotoxicities of two structurally similar type I RIPs, namely trichosanthin (TCS) and free ricin A chain (RTA). A type II RIP, namely Ricinus communis agglutinin (RCA), was also included for comparison. The three RIPs were added separately to cultures of NIH 3T3 cells.
Ou, Sha   +4 more
openaire   +2 more sources

Different in vitro toxicity of ribosome-inactivating proteins (RIPs) on sensory neurons and Schwann cells

Neuroscience Letters, 2012
To study the neurotoxicity induced by Ricinus communis agglutinin (RCA), ricin A chain (RTA), and trichosanthin (TCS) in vitro.Rat neurons and Schwann cells were cultured and real-time up-take of RIPs was traced. TUNEL, Annexin V and DAPI were employed to study the mechanism.The purity of both primary neuronal and Schwann cell cultures attained 80-90%.
Wai-Man, Tong   +4 more
openaire   +2 more sources

Structural insights into the toxicity of type II ribosome inactivating proteins (RIPs): a molecular dynamics study

Journal of Biomolecular Structure and Dynamics
Ribosome Inactivating Proteins (RIPs) act by irreversibly depurinating the 28S rRNA ricin-sarcin loop (SRL) of the eukaryotic ribosome resulting in protein synthesis inhibition. In general, they consist of two variants: Type I which is single chained (∼30 kDa), and Type II, a more toxic variant which is a Type I N-glycosidase chain covalently linked to
Pavan K, Madasu, Thyageshwar, Chandran
openaire   +2 more sources

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