Results 1 to 10 of about 11,798 (95)

Ribosome-Inactivating Proteins from Salsola soda L. and Saponaria officinalis L. Are Promising Candidates for Targeted Therapy of Colon Cancer [PDF]

open access: yesBiomedicines
Background/Objectives: Ribosome-inactivating proteins (RIPs) are plant-derived enzymes with potent cytotoxic activity, widely studied as anticancer agents, particularly as toxic payloads in immunoconjugates. Despite numerous encouraging results reported,
Francesco Biscotti   +8 more
doaj   +2 more sources

Ribosome-Inactivating and Related Proteins

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   +3 more sources

Ribosome Inactivating Proteins from Rosaceae

open access: yesMolecules, 2016
Ribosome-inactivating proteins (RIPs) are widespread among higher plants of different taxonomic orders. In this study, we report on the RIP sequences found in the genome/transcriptome of several important Rosaceae species, including many economically ...
Els van Damme   +2 more
exaly   +3 more sources

Recombinant tritin protein exhibits antiviral activity against zucchini yellow mosaic virus [PDF]

open access: yesBMC Plant Biology
Background Ribosome-inactivating proteins (RIPs) are a group of proteins known to inhibit protein synthesis and contribute to plant defense responses. Although the antiviral properties of various RIPs have been demonstrated, the antiviral potential of ...
Serap Demi̇rel   +3 more
doaj   +2 more sources

Isolation, Characterization and Biological Action of Type-1 Ribosome-Inactivating Proteins from Tissues of Salsola soda L.

open access: yesToxins, 2022
Ribosome-inactivating proteins (RIPs) are known as RNA N-glycosylases. They depurinate the major rRNA, damaging ribosomes and inhibiting protein synthesis.
Nicola Landi   +7 more
doaj   +1 more source

Charged and hydrophobic surfaces on the a chain of shiga-like toxin 1 recognize the C-terminal domain of ribosomal stalk proteins. [PDF]

open access: yesPLoS ONE, 2012
Shiga-like toxins are ribosome-inactivating proteins (RIP) produced by pathogenic E. coli strains that are responsible for hemorrhagic colitis and hemolytic uremic syndrome.
Andrew J McCluskey   +5 more
doaj   +1 more source

Structure and Biological Properties of Ribosome-Inactivating Proteins and Lectins from Elder (Sambucus nigra L.) Leaves

open access: yesToxins, 2022
Ribosome-inactivating proteins (RIPs) are a group of proteins with rRNA N-glycosylase activity that catalyze the removal of a specific adenine located in the sarcin–ricin loop of the large ribosomal RNA, which leads to the irreversible inhibition of ...
Rosario Iglesias   +8 more
doaj   +1 more source

Kirkiin: A New Toxic Type 2 Ribosome-Inactivating Protein from the Caudex of Adenia kirkii

open access: yesToxins, 2021
Ribosome-inactivating proteins (RIPs) are plant toxins that irreversibly damage ribosomes and other substrates, thus causing cell death. RIPs are classified in type 1 RIPs, single-chain enzymatic proteins, and type 2 RIPs, consisting of active A chains ...
Massimo Bortolotti   +5 more
doaj   +1 more source

Inhibition of HIV-1 replication by balsamin, a ribosome inactivating protein of Momordica balsamina. [PDF]

open access: yesPLoS ONE, 2013
Ribosome-inactivating proteins (RIPs) are endowed with several medicinal properties, including antiviral activity. We demonstrate here that the recently identified type I RIP from Momordica balsamina also possesses antiviral activity, as determined by ...
Inderdeep Kaur   +5 more
doaj   +1 more source

Anti-Human Endoglin (hCD105) Immunotoxin—Containing Recombinant Single Chain Ribosome-Inactivating Protein Musarmin 1

open access: yesToxins, 2016
Endoglin (CD105) is an accessory component of the TGF-β receptor complex, which is expressed in a number of tissues and over-expressed in the endothelial cells of tumor neovasculature.
Begoña Barriuso   +7 more
doaj   +1 more source

Home - About - Disclaimer - Privacy