Results 71 to 80 of about 19,244,439 (340)

Identification of novel components of Trypanosoma brucei editosomes [PDF]

open access: yes, 2003
The editosome is a multiprotein complex that catalyzes the insertion and deletion of uridylates that occurs during RNA editing in trypanosomatids. We report the identification of nine novel editosome proteins in Trypanosoma brucei.
Carmean, Nicole   +6 more
core   +2 more sources

Cationic poly(amidoamine) promotes cytosolic delivery of bovine RNase A in melanoma cells, while maintaining its cellular toxicity [PDF]

open access: yes, 2015
Ribonucleases are known to cleave ribonucleic acids, inducing cell death. RNase A, a member of the ribonuclease family, generally displayed poor in vitro activity. This has been attributed to factors such as low intracellular delivery.
Akinc   +60 more
core   +1 more source

On the Stabilizing Action of Protein Denaturants: Acetonitrile Effect on Stability of Lysozyme in Aqueous Solutions [PDF]

open access: yes, 2000
Stability of hen lysozyme in the presence of acetonitrile (MeCN) at different pH values of the medium was studied by scanning microcalorimetry with a special emphasis on determination of reliable values of the denaturational heat capacity change.
Kovriguine, Evgueni, Potekhin, Sergey A.
core   +2 more sources

A conformational RNA zipper promotes intron ejection during non-conventional XBP1 mRNA splicing. [PDF]

open access: yes, 2015
The kinase/endonuclease IRE1 is the most conserved signal transducer of the unfolded protein response (UPR), an intracellular signaling network that monitors and regulates the protein folding capacity of the endoplasmic reticulum (ER).
Acosta-Alvear, Diego   +3 more
core   +1 more source

Evaluation of the allergenicity potential of TcPR-10 protein from Theobroma cacao. [PDF]

open access: yesPLoS ONE, 2012
BACKGROUND: The pathogenesis related protein PR10 (TcPR-10), obtained from the Theobroma cacao-Moniliophthora perniciosa interaction library, presents antifungal activity against M. perniciosa and acts in vitro as a ribonuclease.
Sara Pereira Menezes   +8 more
doaj   +1 more source

RNase footprinting demonstrates antigenomic hepatitis delta virus ribozyme structural rearrangement as a result of self-cleavage reaction

open access: yesBMC Research Notes, 2008
Background Hepatitis delta virus (HDV) is a satellite virus of hepatitis B. During viral replication the 1700-nucleotide-long genomic RNA and its complement, the antigenomic RNA, undergo self-cleavage catalyzed by internal ribozyme motifs that are ...
Dobrynina Nadezhda   +4 more
doaj   +1 more source

Vertical transmission of Mycoplasma wenyonii in cattle, supported by analysis of the ribonuclease P RNA gene - Short communication.

open access: yesActa Veterinaria Hungarica, 2015
The vertical transmission of Mycoplasma (M.) wenyonii was investigated in beef cattle raised on a farm in Japan by analysing the ribonuclease P RNA (rnpB) gene sequence using PCR. Peripheral blood samples from 17 dams infected with M.
Fumina Sasaoka   +6 more
semanticscholar   +1 more source

Ribonucleolytic resection is required for repair of strand displaced nonhomologous end-joining intermediates [PDF]

open access: yes, 2013
Nonhomologous end-joining (NHEJ) pathways repair DNA double-strand breaks (DSBs) in eukaryotes and many prokaryotes, although it is not reported to operate in the third domain of life, archaea. Here, we describe a complete NHEJ complex, consisting of DNA
Bartlett, Edward   +2 more
core   +1 more source

Novel Aspects of Polynucleotide Phosphorylase Function in Streptomyces

open access: yesAntibiotics, 2018
Polynucleotide phosphorylase (PNPase) is a 3′–5′-exoribnuclease that is found in most bacteria and in some eukaryotic organelles. The enzyme plays a key role in RNA decay in these systems.
George H. Jones
doaj   +1 more source

Reducing conditions are the key for efficient production of active ribonuclease inhibitor in Escherichia coli

open access: yesMicrobial Cell Factories, 2011
Background The eukaryotic RNase ribonuclease/angiogenin inhibitors (RI) are a protein group distinguished by a unique structure - they are composed of hydrophobic leucine-rich repeat motifs (LRR) and contain a high amount of reduced cysteine residues ...
Neubauer Peter, Šiurkus Juozas
doaj   +1 more source

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