Results 11 to 20 of about 25,784 (242)

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   +2 more sources

Overexpression of the ribosome-inactivating protein OsRIP1 modulates the jasmonate signaling pathway in rice [PDF]

open access: yesFrontiers in Plant Science
Ribosome-inactivating proteins (RIPs) are plant enzymes that target the rRNA. The cytoplasmic RIP, called OsRIP1, plays a crucial role in regulating jasmonate, a key plant hormone.
Simin Chen   +10 more
doaj   +2 more sources

Primary Sequence and Three-Dimensional Structural Comparison between Malanin and Ricin, a Type II Ribosome-Inactivating Protein [PDF]

open access: yesToxins
Malanin is a new type II ribosome-inactivating protein (RIP) purified from Malania oleifera, a rare, endangered tree is only found in the southwest of Guangxi Province and the southeast of Yunnan Province, China.
Yan Yuan, Shuxiao Wu, Philip J. R. Day
doaj   +2 more sources

Revising the taxonomic distribution, origin and evolution of ribosome inactivating protein genes. [PDF]

open access: yesPLoS ONE, 2013
Ribosome inactivating proteins are enzymes that depurinate a specific adenine residue in the alpha-sarcin-ricin loop of the large ribosomal RNA, being ricin and Shiga toxins the most renowned examples.
Walter J Lapadula   +2 more
doaj   +2 more sources

Structure of Ribosome-Inactivating Protein from Mirabilis jalapa and Its L12-Stalk-Dependent Inhibition of Escherichia coli Ribosome [PDF]

open access: yesToxins
Mirabilis antiviral protein (MAP) is the type I ribosome-inactivating protein (RIP), which consists of an RNA N-glycosylase domain with no carbohydrate-binding domain.
Nanami Nishida   +7 more
doaj   +2 more sources

Comparative Efficacy of Ribosome-Inactivating Protein-Containing Immunotoxins in 2D and 3D Models of Sarcoma [PDF]

open access: yesToxins
Sarcomas are very complex and clinically challenging mesenchymal tumors. Although the standard therapeutic approach has improved the 5-year survival rate, many patients experience local relapses and/or distant metastases.
Giulia Calafato   +3 more
doaj   +2 more sources

Structural and Functional Investigation and Pharmacological Mechanism of Trichosanthin, a Type 1 Ribosome-Inactivating Protein [PDF]

open access: yesToxins, 2018
Trichosanthin (TCS) is an RNA N-glycosidase that depurinates adenine-4324 in the conserved α-sarcin/ricin loop (α-SRL) of rat 28 S ribosomal RNA (rRNA).
Wei-Wei Shi, Kam-Bo Wong, Pang-Chui Shaw
doaj   +2 more sources

Anti-Human Endoglin (hCD105) Immunotoxin—Containing Recombinant Single Chain Ribosome-Inactivating Protein Musarmin 1 [PDF]

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   +2 more sources

Recombinant tritin protein exhibits antiviral activity against zucchini yellow mosaic virus [PDF]

open access: yesBMC Plant Biology
Background Ribosome-inactivating proteins (RIPs) are a group of proteins known to inhibit protein synthesis and contribute to plant defense responses. Although the antiviral properties of various RIPs have been demonstrated, the antiviral potential of ...
Serap Demi̇rel   +3 more
doaj   +2 more sources

A Novel Cysteine Protease from Phytolacca americana Cleaves Pokeweed Antiviral Protein Generating Bioactive Fragments [PDF]

open access: yesPlants
The apoplast is often the first point of contact between plant cells and invading pathogens, serving as an important site for defense signaling. Pokeweed antiviral protein (PAP), a ribosome-inactivating protein from Phytolacca americana (pokeweed), is ...
Annabelle Audet   +2 more
doaj   +2 more sources

Home - About - Disclaimer - Privacy