Results 21 to 30 of about 33,782 (294)

Assembly of the 68- and 72-kD Proteins of Signal Recognition Particle with 7S RNA [PDF]

open access: yes, 1993
Signal recognition particle (SRP), the cytoplasmic ribonucleoprotein particle that mediates the targeting of proteins to the ER, consists of a 7S RNA and six different proteins. The 68- (SRP68) and 72-(SRP72) kD proteins of SRP are bound to the 7S RNA of
Ashford, Anthony J.   +5 more
core   +1 more source

Packaging and Uncoating of CRISPR/Cas Ribonucleoproteins for Efficient Gene Editing with Viral and Non-Viral Extracellular Nanoparticles

open access: yesViruses, 2023
Rapid progress in gene editing based on clustered regularly interspaced short palindromic repeats/CRISPR-associated protein (CRISPR/Cas) has revolutionized functional genomic studies and genetic disease correction.
Dmitriy Mazurov   +2 more
doaj   +1 more source

The TROVE module: A common element in Telomerase, Ro and Vault ribonucleoproteins

open access: yesBMC Bioinformatics, 2003
Background Ribonucleoproteins carry out a variety of important tasks in the cell. In this study we show that a number of these contain a novel module, that we speculate mediates RNA-binding. Results The TROVE module – Telomerase, Ro and Vault module – is
Bateman Alex, Kickhoefer Valerie
doaj   +1 more source

R2TP/PAQosome as a promising chemotherapeutic target in cancer

open access: yesJapanese Dental Science Review, 2020
R2TP/PAQosome (particle for arrangement of quaternary structure) is a novel multisubunit chaperone specialized in the assembly/maturation of protein complexes that are involved in essential cellular processes such as PIKKs (phosphatidylinositol 3-kinase ...
Yoshito Kakihara   +3 more
doaj   +1 more source

Signal Recognition Particle in Human Diseases

open access: yesFrontiers in Genetics, 2022
The signal recognition particle (SRP) is a ribonucleoprotein complex with dual functions. It co-translationally targets proteins with a signal sequence to the endoplasmic reticulum (ER) and protects their mRNA from degradation.
Morgana K. Kellogg   +2 more
doaj   +1 more source

Functionality of in vitro reconstituted group II intron RmInt1-derived ribonucleoprotein particles

open access: yesFrontiers in Molecular Biosciences, 2016
The functional unit of mobile group II introns is a ribonucleoprotein particle (RNP) consisting of the intron-encoded protein (IEP) and the excised intron RNA. The IEP has reverse transcriptase activity but also promotes RNA splicing, and the RNA-protein
María Dolores Molina-Sánchez   +2 more
doaj   +1 more source

The synthesis of hemoglobin in a cell-free system [PDF]

open access: yes, 1958
The microsomal particles (1) have been implicated as the major sites of protein synthesis within the cells of a variety of tissues. The studies of Borsook, Zamecnik, Hultin, and others, with intact animals and various types of whole cell systems (see ...
Allen, Esther   +2 more
core   +2 more sources

Measles Virus Ribonucleoprotein Complexes Rapidly Spread across Well-Differentiated Primary Human Airway Epithelial Cells along F-Actin Rings

open access: yesmBio, 2019
Measles virus (MeV) is a highly contagious human pathogen that continues to be a worldwide health burden. One of the challenges for the study of MeV spread is the identification of model systems that accurately reflect how MeV behaves in humans.
Brajesh K. Singh   +3 more
doaj   +1 more source

RNase P Branches Out from RNP to Protein: Organelle-Triggered Diversification? [PDF]

open access: yes, 2012
RNase P is the enzyme that removes 5′ leader sequences from precursor tRNAs. Remarkably, in most organisms, RNase P is a ribonucleoprotein particle where the RNA component is responsible for catalysis. In this issue of Genes \u26 Development, Gutmann and
Borah, Sumit   +2 more
core   +3 more sources

PRP4: a protein of the yeast U4/U6 small nuclear ribonucleoprotein particle [PDF]

open access: yes, 1989
The Saccharomyces cerevisiae prp mutants (prp2 through prp11) are known to be defective in pre-mRNA splicing at nonpermissive temperatures. We have sequenced the PRP4 gene and shown that it encodes a 52-kilodalton protein.
Abelson, John N., Banroques, Josette
core   +1 more source

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