Results 11 to 20 of about 23,875 (181)
Biological Activities of Ribosome-Inactivating Proteins. [PDF]
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 L, Ferreras JM.
europepmc +5 more sources
Antiviral Activity of Ribosome-Inactivating Proteins. [PDF]
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 L, Iglesias R, Ferreras JM.
europepmc +6 more sources
Ribosome Inactivating Proteins from Rosaceae. [PDF]
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.
Shang C, Rougé P, Van Damme EJ.
europepmc +7 more sources
Antifungal Activity of Ribosome-Inactivating Proteins. [PDF]
The control of crop diseases caused by fungi remains a major problem and there is a need to find effective fungicides that are environmentally friendly. Plants are an excellent source for this purpose because they have developed defense mechanisms to cope with fungal infections.
Iglesias R +3 more
europepmc +4 more sources
Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins. [PDF]
Ribosome-inactivating proteins (RIPs) including ricin, Shiga toxin, and trichosanthin, are RNA N-glycosidases that depurinate a specific adenine residue (A-4324 in rat 28S ribosomal RNA, rRNA) in the conserved α-sarcin/ricin loop (α-SRL) of rRNA.
Shi WW, Mak AN, Wong KB, Shaw PC.
europepmc +5 more sources
Ribosome-inactivating proteins: potent poisons and molecular tools. [PDF]
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 MJ, Dodd JE, Hautbergue GM.
europepmc +4 more sources
Ribosome-Inactivating and Related Proteins [PDF]
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
Suicide nanoplasmids coding for ribosome-inactivating proteins [PDF]
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
Ribosome-Inactivating Proteins from Plants: A Historical Overview. [PDF]
This review provides a historical overview of the research on plant ribosome-inactivating proteins (RIPs), starting from the first studies at the end of eighteenth century involving the purification of abrin and ricin, as well as the immunological experiments of Paul Erlich. Interest in these plant toxins was revived in 1970 by the observation of their
Bolognesi A +4 more
europepmc +5 more sources
Ribosomal RNA N-glycosylase Activity Assay of Ribosome-inactivating Proteins. [PDF]
Ribosome-inactivating proteins (RIPs) are enzymes that irreversibly inactivate ribosomes as a consequence of their N-glycosylase (EC 3.2.2.22) activity. The enzyme cleaves the N-glycosidic bond between the adenine No. 4324 from the 28S rRNA and its ribose in rat ribosomes (or the equivalent adenine in sensitive ribosomes from other organisms).
Iglesias R, Citores L, Ferreras JM.
europepmc +5 more sources

