Maize ribosome-inactivating proteins (RIPs) with distinct expression patterns have similar requirements for proenzyme activation [PDF]
Journal of Experimental Botany, 2004 Ribosome-inactivating proteins (RIPs, EC 3.2.2.22) are potent naturally occurring toxins found in numerous and diverse plant species. The maize RIP is unusual among the plant RIPs because it is synthesized as an inactive precursor (also known as maize proRIP1 or b-32). The proenzyme undergoes proteolytic activation that results in the removal of the NH(
Hank W, Bass +5 more
openaire +2 more sources
Ribosome Inactivating Proteins from Rosaceae
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 ...
Chenjing Shang +2 more
doaj +1 more source
Insights into the mechanism of cell death induced by saporin delivered into cancer cells by an antibody fusion protein targeting the transferrin receptor 1 [PDF]
, 2012 We previously developed an antibody-avidin fusion protein (ch128.1Av) that targets the human transferrin receptor 1 (TfR1) and exhibits direct cytotoxicity against malignant B cells in an iron-dependent manner. ch128.1Av is also a delivery system and its
Casero, David +9 more
core +2 more sources
Ribosome Inactivating Proteins: From Plant Defense to Treatments against Human Misuse or Diseases
Toxins, 2018 Ribosome inactivating proteins (RIPs) form a vast family of hundreds of toxins from plants, fungi, algae, and bacteria. RIP activities have also been detected in animal tissues.
Julien Barbier, Daniel Gillet
doaj +1 more source
Double-Coated Nanoparticle of Ribosome Inactivating Protein (RIP) from Mirabilis jalapa L. prepared from Chitosan-Sodium Tripolyphosphate and Alginate-Calcium Chloride: The New Strategy for Protein Drug in Oral Delivery [PDF]
BIO Web of Conferences, 2023 Oral delivery of protein drugs is challenging due to the instability of the compound and structural barrier exists in the gastrointestinal (GI) tract. Nanoparticle technology is known as a promising drug delivery strategy to ensure drug bioavailability ...
Miranda Amalia +7 more
doaj +1 more source
Comparative study of lectin domains in model species : new insights into evolutionary dynamics [PDF]
, 2017 Lectins are present throughout the plant kingdom and are reported to be involved in diverse biological processes. In this study, we provide a comparative analysis of the lectin families from model species in a phylogenetic framework. The analysis focuses
Dang, Liuyi +5 more
core +3 more sources
Structure and Activity of a Cytosolic Ribosome-Inactivating Protein from Rice
Toxins, 2019 Ribosome-inactivating proteins (RIPs) are cytotoxic enzymes that inhibit protein translation by depurinating ribosomal RNA. Although most plant RIPs are synthesized with leader sequences that sequester them away from the host ribosomes, several RIPs from
Jeroen De Zaeytijd +3 more
doaj +1 more source
Identification of small molecules that suppress ricin-induced stress-activated signaling pathways. [PDF]
PLoS ONE, 2012 Ricin is a member of the ribosome-inactivating protein (RIP) family of plant and bacterial toxins. In this study we used a high-throughput, cell-based assay to screen more than 118,000 compounds from diverse chemical libraries for molecules that reduced ...
Paul G Wahome +2 more
doaj +1 more source
Immunotoxins and Anticancer Drug Conjugate Assemblies: The Role of the Linkage between Components [PDF]
, 2011 Immunotoxins and antibody-drug conjugates are protein-based drugs combining a target-specific binding domain with a cytotoxic domain. Such compounds are potentially therapeutic against diseases including cancer, and several clinical trials have shown ...
Franco Dosio, Luigi Cattel, Paola Brusa
core +3 more sources
, 2008 We studied the in vitro and in planta antiviral activity of the PhRIP I, a type 1 Ribosome-Inactivating Protein originally purified from leaves of the Phytolacca heterotepala.
ANTIMO DI MARO +6 more
core +1 more source