Special Issue: Ribosome-Inactivating Proteins-Commemorative Issue in Honor of Professor Fiorenzo Stirpe. [PDF]
Molecules, 2017 The family of ribosome-inactivating proteins (RIPs) groups all enzymes (EC.3.2.2.22) with a so-called RIP domain which comprises N-glycosidase activity and enables these proteins to catalytically inactivate ribosomes.[...
Van Damme EJ.
europepmc +6 more sources
Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins [PDF]
Molecules, 2016 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.
Amanda Nga-Sze Mak +2 more
exaly +4 more sources
Ribosome-Inactivating Proteins from Plants: A Historical Overview [PDF]
Molecules, 2016 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 ...
Andrea Bolognesi +2 more
exaly +4 more sources
Extensive Evolution of Cereal Ribosome-Inactivating Proteins Translates into Unique Structural Features, Activation Mechanisms, and Physiological Roles. [PDF]
Toxins (Basel), 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 J, Van Damme EJ.
europepmc +6 more sources
Structures of Eukaryotic Ribosomal Stalk Proteins and Its Complex with Trichosanthin, and Their Implications in Recruiting Ribosome-Inactivating Proteins to the Ribosomes [PDF]
Toxins, 2015 Ribosome-inactivating proteins (RIP) are RNA N-glycosidases that inactivate ribosomes by specifically depurinating a conserved adenine residue at the α-sarcin/ricin loop of 28S rRNA. Recent studies have pointed to the involvement of the C-terminal domain
Ka-Ming Lee, Kam-Bo Wong
exaly +4 more sources
Use of Ribosome-Inactivating Proteins from Sambucus for the Construction of Immunotoxins and Conjugates for Cancer Therapy [PDF]
Toxins, 2011 The type 2 ribosome-inactivating proteins (RIPs) isolated from some species belonging to the Sambucus genus, have the characteristic that although being even more active than ricin inhibiting protein synthesis in cell-free extracts, they lack the high ...
José M Ferreras +2 more
exaly +4 more sources
Biological Activities of Ribosome-Inactivating Proteins. [PDF]
Toxins (Basel), 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
Citores L, Ferreras JM.
europepmc +2 more sources
Antiviral Activity of Ribosome-Inactivating Proteins. [PDF]
Toxins (Basel), 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.
Citores L, Iglesias R, Ferreras JM.
europepmc +2 more sources
The ribosome-inactivating proteins MAP30 and Momordin inhibit SARS-CoV-2. [PDF]
PLoS One, 2023 The continuing emergence of SARS-CoV-2 variants has highlighted the need to identify additional points for viral inhibition. Ribosome inactivating proteins (RIPs), such as MAP30 and Momordin which are derived from bitter melon (Momordica charantia), have
Watts NR +7 more
europepmc +3 more sources
Ribosome Inactivating Proteins from Rosaceae. [PDF]
Molecules, 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 ...
Shang C, Rougé P, Van Damme EJ.
europepmc +2 more sources