Results 41 to 50 of about 25,923,055 (288)

RNAse selection screen for RNAse V1.

, 2014
RNAse selection screen for RNAse V1.
Renata Ochocka (535928), Piotr Madanecki (560221), Susan Nozell (157202), James F. Collawn (551889), Rafal Bartoszewski (535921)   +4 more
core   +1 more source

The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological Functions

Biomolecules, 2016
Ribonuclease P (RNase P) is an essential endonuclease responsible for catalyzing 5’ end maturation in precursor transfer RNAs. Since its discovery in the 1970s, RNase P enzymes have been identified and studied throughout the three domains of life ...
Bradley P. Klemm, Nancy Wu, Yu Chen, Xin Liu, Kipchumba J. Kaitany, Michael J. Howard, Carol A. Fierke   +6 more
doaj   +1 more source

Activity of RNase P-G and RNase P-U holoenzyme complexes at different ammonium acetate concentrations.

, 2016
The pre-tRNA processing activity of RNase P-G and RNase P-U proteins and their holoenzymes was assayed in the presence of different concentrations of ammonium acetate.
Shah Ubaid-ullah (487293), Alla Singh (2614780), Anup K. Ramteke (2614777), Janendra K Batra (2614774)   +3 more
core   +1 more source

Playing RNase P evolution: swapping the RNA catalyst for a protein reveals functional uniformity of highly divergent enzyme forms.

PLoS Genetics, 2014
The RNase P family is a diverse group of endonucleases responsible for the removal of 5' extensions from tRNA precursors. The diversity of enzyme forms finds its extremes in the eukaryal nucleus where RNA-based catalysis by complex ribonucleoproteins in ...
Christoph Weber, Andreas Hartig, Roland K Hartmann, Walter Rossmanith   +3 more
doaj   +1 more source

Chance and necessity in the evolution of RNase P [PDF]

RNA, 2017
RNase P catalyzes 5′-maturation of tRNAs in all three domains of life. This primary function is accomplished by either a ribozyme-centered ribonucleoprotein (RNP) or a protein-only variant (with one to three polypeptides). The large, multicomponent archaeal and eukaryotic RNase P RNPs appear disproportionate to the simplicity of their role in tRNA 5 ...
Gopalan, Venkat, Jarrous, Nayef, Krasilnikov, Andrey S.   +2 more
openaire   +2 more sources

Composition of RNase P from plant nuclei and plastids

, 2003
Ribonuklease P (RNaseP) ist eine essentielle Endonuklease, welche die 5'-Flanke von pre-tRNAs entfernt. In nahezu allen bisher untersuchten Organismen und Organellen besteht das Holoenzym aus einer RNA-Untereinheit und einer Protein-Komponente ...
Heubeck, Christian
core   +2 more sources

A Novel Fully Human Antitumor ImmunoRNase Targeting ErbB2-Positive Tumors [PDF]

, 2010
A second generation anti-ErbB2 ImmunoRNase, called Erb-hcAb-RNase, was obtained by the fusion of Erb-hcAb, a human compact anti-ErbB2 antibody, with human pancreatic ribonuclease (HP-RNase or RNase 1).
Borriello, Marianna
core   +1 more source

Nuclear RNase P of Trypanosoma brucei: A Single Protein in Place of the Multicomponent RNA-Protein Complex

Cell Reports, 2012
RNase P is the endonuclease that removes 5′ extensions from tRNA precursors. In its best-known form, the enzyme is composed of a catalytic RNA and a protein moiety variable in number and mass. This ribonucleoprotein enzyme is widely considered ubiquitous
Andreas Taschner, Christoph Weber, Aurélie Buzet, Roland K. Hartmann, Andreas Hartig, Walter Rossmanith   +5 more
doaj   +1 more source

A Novel Method to Isolate RNase MRP Using RNA Streptavidin Aptamer Tags

Bio-Protocol, 2023
Interactions between RNA-binding proteins and RNA molecules are at the center of multiple biological processes. Therefore, accurate characterization of the composition of ribonucleoprotein complexes (RNPs) is crucial.
Violette Charteau, Merel Derksen, Ger Pruijn   +2 more
doaj   +1 more source

A context‐dependent modulatory role for eIF6 in acquired resistance to vemurafenib in melanoma

FEBS Letters, EarlyView.
Acquired resistance to vemurafenib upregulates the translation factor eIF6 in melanoma cells. Silencing eIF6 in resistant cells reduces proliferation and partially restores drug sensitivity, whereas its overexpression increases sensitivity across melanoma lines regardless of BRAF status, via modulation of mTOR, S6K, and MAPK signaling.
George Kyriakopoulos, Antonia Petropoulou, Alexandra Anastogianni, Angelina Bania, Vassilis Stamatakis, Argyris Alexiou, Chi‐Ping Day, Glenn Merlino, Katerina Grafanaki, Constantinos Stathopoulos   +9 more
wiley   +1 more source