Results 41 to 50 of about 1,593,838 (216)

Protein folding on the ribosome studied using NMR spectroscopy [PDF]

open access: yes, 2013
NMR spectroscopy is a powerful tool for the investigation of protein folding and misfolding, providing a characterization of molecular structure, dynamics and exchange processes, across a very wide range of timescales and with near atomic resolution.
Christodoulou, J   +9 more
core   +1 more source

The Recombinant Maize Ribosome-Inactivating Protein Transiently Reduces Viral Load in SHIV89.6 Infected Chinese Rhesus Macaques

open access: yesToxins, 2015
Ribosome inactivating proteins (RIPs) inhibit protein synthesis by depurinating the large ribosomal RNA and some are found to possess anti-human immunodeficiency virus (HIV) activity. Maize ribosome inactivating protein (RIP) has an internal inactivation
Rui-Rui Wang   +13 more
doaj   +1 more source

Ribosome inactivation by Escherichia coli GTPase RsgA inhibits T4 phage

open access: yesFrontiers in Microbiology, 2023
IntroductionBacteria must combat phages, and myriad bacterial anti-phage systems have been discovered that reduce host metabolism, for example, by depleting energetic compounds like ATP and NAD+. Hence, these systems indirectly inhibit protein production.
Laura Fernández-García   +3 more
doaj   +1 more source

Antifungal Activity of Ageritin, a Ribotoxin-like Protein from Cyclocybe aegerita Edible Mushroom, against Phytopathogenic Fungi

open access: yesToxins, 2023
Ageritin from poplar mushrooms is a specific endonuclease that hydrolyzes a single phosphodiester bond located in the sarcin-ricin loop (SRL) of the large rRNA, thereby blocking protein synthesis.
Sara Ragucci   +4 more
doaj   +1 more source

2A-induced ribosome stalling [PDF]

open access: yes, 2014
Originally 2A was characterised in foot-and-mouth disease virus. Site directed mutagenesis identified a C-terminus consensus motif [D(V/I)ExNPGP] and it is proposed that 2A interacts with the exit tunnel of the ribosome in a way that a specific peptide ...
Odon, Valèrie
core   +1 more source

Saporins - Type 1 Ribosome-inactivating proteins from soapwort (saponaria officinalis L.) [PDF]

open access: yes, 1995
Ribosome-inactivating proteins (RlPs) are found distributed throughout the plant kingdom. These proteins possess a RNA N-glycosidase activity whereby the depurination of a specific adenine residue from the large ribosomal subunit renders eukaryotic and ...
Sinclair, Lesley Jean
core  

The small-subunit processome is a ribosome assembly intermediate [PDF]

open access: yes, 2004
The small-subunit (SSU) processome is a large ribonucleoprotein required for the biogenesis of the 18S rRNA and likely corresponds to the terminal knobs visualized by electron microscopy on the 5' end of nascent rRNAs.
Granneman, Sander; id_orcid   +4 more
core   +1 more source

Plant proteins that inactivate foreign ribosomes

open access: yesBioscience Reports, 1986
Ribosome-inactivating proteins are a group of closely related proteins that are widely distributed throughout the plant kingdom and which share the unusual property of being able to inactivate mammalian ribosomes by an enzymic (non-stoichiometric) mechanism (1). Two major classes of these proteins are found in plants.
W K, Roberts, C P, Selitrennikoff
openaire   +2 more sources

Translophagy—A potential link between autophagy impairment and translational errors

open access: yesFEBS Letters, EarlyView.
Neurodegenerative diseases are characterised by the accumulation of abnormal proteins and protein aggregates, but their origin often remains unknown. We propose that selective autophagy removes damaged protein‐making machinery, preventing errors during protein synthesis.
Mykola V. Korolchuk   +11 more
wiley   +1 more source

Gene sequences encoding ribosome-inactivating proteins from soapwort (Saponaria officinalis L.) [PDF]

open access: yes, 1991
Ribosome-inactivating proteins (RIPs) are found in a wide variety of plant species. They possess an RNA N-glycosidase activity whereby the removal of a specific adenine residue from 28 S RNA renders a eukaryotic ribosome inactive.
Fordham-Skelton, Anthony P.
core  

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