Results 71 to 80 of about 26,838 (281)

N4‐acetylcytidine in LncRNA Gm26917 Promotes Translation in Female Germline Stem Cells by Recruiting Ribosomal Protein mRNA via EEF1A1

open access: yesAdvanced Science, EarlyView.
This work establishes that ac4C modification on lncRNA Gm26917 governs its spatial interactions with Rpl10 mRNA, and RBP EEF1A1 mediates the interaction between Gm26917 and Rpl10. It elucidates a novel ac4C‐Gm26917‐EEF1A1‐Rpl10 axis in FGSC maintenance both in vitro and in vivo, and provides a potential molecular target for modulating germ cell ...
Xinyue Li, Xiaopeng Hu, Ji Wu
wiley   +1 more source

Modification of ribosomal RNA by ribosome-inactivating proteins from plants [PDF]

open access: greenNucleic Acids Research, 1988
We have surveyed 14 different toxic and nontoxic ribosome-inactivating proteins from plants for the ability to act on the RNA of the eucaryotic 60 S ribosomal subunit. All of these proteins act to introduce a specific modification into 26-28 S RNA which renders the RNA sensitive to cleavage by aniline.
Fiorenzo Stirpe   +3 more
openalex   +5 more sources

Antifungal Activity of Ribosome-Inactivating Proteins

open access: yesToxins
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 Álvarez, María del Rosario   +3 more
openaire   +3 more sources

Development and Structural Characterization of UTE‐156, a Covalent Inhibitor of the VCP/p97 AAA+ ATPase

open access: yesAdvanced Science, EarlyView.
The AAA+ ATPase Valosin‐containing protein (VCP/p97) regulates protein homeostasis by unfolding ubiquitinated substrates. Here, we describe UTE‐156, a novel irreversible covalent inhibitor that modifies Cys522 in the D2 ATPase motor domain. Although its pharmacochemical limitations preclude immediate therapeutic use, UTE‐156 serves as a valuable ...
Daniela Tamayo‐Jaramillo   +8 more
wiley   +1 more source

Isolation and Molecular Characterization of Two Lectins from Dwarf Elder (Sambucus ebulus L.) Blossoms Related to the Sam n1 Allergen

open access: yesToxins, 2013
Sambucus species contain a number of lectins with and without antiribosomal activity. Here, we show that dwarf elder (Sambucus ebulus L.) blossoms express two D-galactose-binding lectins that were isolated and purified by affinity chromatography and gel ...
Tomas Girbes   +5 more
doaj   +1 more source

Engineering of Ribosome-inactivating Proteins for Improving Pharmacological Properties

open access: yesToxins, 2020
Ribosome-inactivating proteins (RIPs) are N-glycosidases, which depurinate a specific adenine residue in the conserved α-sarcin/ricin loop (α-SRL) of rRNA.
Jia-Qi Lu   +3 more
doaj   +1 more source

Glycotope structures and intramolecular affinity factors of plant lectins for Tn/T antigens [PDF]

open access: yes, 2011
B
A Babino   +42 more
core   +3 more sources

“More” Artificial mRNAs: Beyond the Art of Nature

open access: yesAdvanced Science, EarlyView.
Inspired by nature yet transcending it, synthetic mRNA is being redesigned beyond the canonical architecture. This review highlights emerging forms—circular, branched, and self‐amplifying mRNAs—that expand stability, persistence, and functional control, illustrating how artificial mRNA is evolving into a new medium for programmable biological ...
Yuanzhe Cui   +3 more
wiley   +1 more source

Burkholderia Lethal Factor 1, a Novel Anti-Cancer Toxin, Demonstrates Selective Cytotoxicity in MYCN-Amplified Neuroblastoma Cells

open access: yesToxins, 2018
Immunotoxins are being investigated as anti-cancer therapies and consist of a cytotoxic enzyme fused to a cancer targeting antibody. All currently used toxins function via the inhibition of protein synthesis, making them highly potent in both healthy and
Aleksander Rust   +3 more
doaj   +1 more source

Ribosome-Inactivating Proteins from Plants: A Historical Overview [PDF]

open access: yesMolecules, 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 experiments of Paul Erlich. Interest in these plant toxins was revived in 1970 by the observation of their
BOLOGNESI, ANDREA   +4 more
openaire   +3 more sources

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