Results 21 to 30 of about 26,838 (281)

Biocontrol Potential of Sodin 5, Type 1 Ribosome-Inactivating Protein from Salsola soda L. Seeds [PDF]

open access: yesBiomolecules
Sodin 5 is a type 1 ribosome-inactivating protein isolated from the seeds of Salsola soda L., an edible halophytic plant that is widespread in southern Europe, close to the coast.
Monika Novak Babič   +8 more
doaj   +2 more sources

Ribosome Inactivating Proteins from Rosaceae [PDF]

open access: goldMolecules, 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 important edible fruits such as apple, pear, peach, apricot, and strawberry.
Chenjing Shang   +2 more
openalex   +7 more sources

Crystallization and preliminary X-ray studies of snake gourd lectin: homology with type II ribosome-inactivating proteins [PDF]

open access: bronze, 2001
Arulanandam, Jeyaprakash   +6 more
core   +2 more sources

An unusual type I ribosome-inactivating protein from Agrostemma githago L. [PDF]

open access: goldSci Rep, 2020
Weise C   +7 more
europepmc   +3 more sources

Antiviral Activity of Ribosome-Inactivating Proteins [PDF]

open access: yesToxins, 2021
Ribosome-inactivating proteins (RIPs) are rRNA N-glycosylases from plants (EC 3.2.2.22) that inactivate ribosomes thus inhibiting protein synthesis. The antiviral properties of RIPs have been investigated for more than four decades. However, interest in these proteins is rising due to the emergence of infectious diseases caused by new viruses and the ...
Citores González, Lucía   +2 more
openaire   +4 more sources

Ribosome-inactivating proteins [PDF]

open access: yesVirulence, 2013
Ribosome-inactivating proteins (RIPs) were first isolated over a century ago and have been shown to be catalytic toxins that irreversibly inactivate protein synthesis. Elucidation of atomic structures and molecular mechanism has revealed these proteins to be a diverse group subdivided into two classes.
Walsh, M.J.   +2 more
openaire   +4 more sources

Maize ribosome-inactivating protein uses Lys158-lys161 to interact with ribosomal protein P2 and the strength of interaction is correlated to the biological activities. [PDF]

open access: yesPLoS ONE, 2012
Ribosome-inactivating proteins (RIPs) inactivate prokaryotic or eukaryotic ribosomes by removing a single adenine in the large ribosomal RNA. Here we show maize RIP (MOD), an atypical RIP with an internal inactivation loop, interacts with the ribosomal ...
Yuen-Ting Wong   +5 more
doaj   +1 more source

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. There are also RIPs and RIP related proteins that cannot be grouped into the classical type 1 and type 2 RIPs because of their different sizes, structures or functions. In addition,
Schrot, Joachim   +2 more
openaire   +4 more sources

Biological Activities of Ribosome-Inactivating Proteins

open access: yesToxins, 2023
After more than 50 years of research, studies on the structure and biological activities of ribosome-inactivating proteins (RIPs) continue to provide a field of great interest within the scientific community, both for the health risks they pose and their applications in medicine and biotechnology [...]
Citores González, Lucía   +1 more
openaire   +4 more sources

Suicide nanoplasmids coding for ribosome-inactivating proteins [PDF]

open access: yesEuropean Journal of Pharmaceutical Sciences, 2022
Conventional eukaryotic expression plasmids contain a DNA backbone that is dispensable for the cellular expression of the transgene. In order to reduce the vector size, minicircle DNA technology was introduced. A drawback of the minicircle technology are considerable production costs.
Mitdank, Hardy   +8 more
openaire   +2 more sources

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