Results 21 to 30 of about 30,415 (253)

Elderberries: A Source of Ribosome-Inactivating Proteins with Lectin Activity

open access: yesMolecules, 2015
Sambucus (Adoxaceae) species have been used for both food and medicine purposes. Among these, Sambucus nigra L. (black elder), Sambucus ebulus L. (dwarf elder), and Sambucus sieboldiana L. are the most relevant species studied.
Jesús Tejero   +7 more
doaj   +2 more sources

Nucleotide sequence of cDNA coding for saporin‐6, a type‐1 ribosome‐inactivating protein from Saponaria officinalis [PDF]

open access: yesEuropean Journal of Biochemistry, 1989
We have isolated and sequenced partial cDNA clones that encode SO‐6, a ribosome‐inactivating protein from Saponaria officinalis. A cDNA library was constructed from the leaves of this plant and screened with synthetic oligonucleotide probes representing various portions of the protein.
L, Benatti   +7 more
openaire   +3 more sources

Genotoxicity Assessment of Quinoin, a Ribosome Inactivating Protein from Quinoa Seeds, in the Teleost Danio rerio

open access: yesFrontiers in Bioscience-Landmark
Background: Ribosome inactivating proteins (RIPs) are N-glycosylases found in various plants that are able to specifically and irreversibly inhibit protein translation, thereby leading to cell death. Their cytotoxic properties have attracted attention in
Filomena Mottola   +6 more
doaj   +2 more sources

Molecular action of the type 1 ribosome‐inactivating protein saporin 5 on Vicia sativa ribosomes [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. sativa rRNA, which upon treatment with acid aniline releases several RNA fragments including an RNA fragment of approximately 370 ...
Iglesias, Rosario   +5 more
openaire   +3 more sources

Ribosome inactivating proteins: Enzymes in search of biological function

open access: yesAnales de la Real Academia Nacional de Farmacia, 2022
Ribosome-inactivating proteins (RIPs) are enzymes (N-glycosidases classified as rRNA N-glycohydrolases, EC 3.2.2.22), mostly of plant origin, but also of bacterial, fungal and algal origin, which cause irreversible inhibition of protein biosynthesis ...
Tomás Girbés Juan, D. Cordoba Díaz
semanticscholar   +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

Extensive evolution of cereal ribosome-inactivating proteins translates into unique structural features, activation mechanisms, and physiological roles [PDF]

open access: yes, 2017
Ribosome-inactivating proteins (RIPs) are a class of cytotoxic enzymes that can depurinate rRNAs thereby inhibiting protein translation. Although these proteins have also been detected in bacteria, fungi, and even some insects, they are especially ...
De Zaeytijd, Jeroen, Van Damme, Els
core   +2 more sources

Novel small molecule retrograde transport blocker confers post-exposure protection against ricin intoxication

open access: yesActa Pharmaceutica Sinica B, 2020
Ricin is a highly toxic type 2 ribosome-inactivating protein (RIP) which is extracted from the seeds of castor beans. Ricin is considered a potential bioterror agent and no effective antidote for ricin exists so far.
Xu Zhao   +7 more
doaj   +1 more source

Identification of the catalytic motif of the microbial ribosome inactivating cytotoxin colicin E3 [PDF]

open access: yes, 2004
Colicin E3 is a cytotoxic ribonuclease that specifically cleaves 16S rRNA at the ribosomal A-site to abolish protein synthesis in sensitive Escherichia coli cells.
Bohm   +30 more
core   +2 more sources

Evolution of plant ribosome-inactivating proteins [PDF]

open access: yes, 2010
This contribution presents an updated analysis of the evolution of ribosome-inactivating proteins (RIPs) in plants. All evidence suggests that an ancestor of modern seed plants developed the RIP domain at least 300 million years ago.
Peumans, Willy J, Van Damme, Els
core   +1 more source

Home - About - Disclaimer - Privacy