Results 171 to 180 of about 4,940 (209)

The Impact of Chemical Modifications on the Interferon-Inducing and Antiproliferative Activity of Short Double-Stranded Immunostimulating RNA. [PDF]

Molecules
Bishani A, Meschaninova MI, Zenkova MA, Chernolovskaya EL.   +3 more
europepmc   +1 more source

14-3-3σ up-regulation in the temporal cortex associates with tau pathology and reactive astroglia in Lewy body disorders. [PDF]

Brain Pathol
Marsal-García L, Mena J, Lao CA, Adamuz D, Arnaldo L, Carrato C, Menendez A, Samaniego D, Vilas D, Ispierto L, Planas A, Alvarez R, Pastor P, Beyer K.   +13 more
europepmc   +1 more source

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Drosophila 5′ → 3′-Exoribonuclease Pacman

Methods in enzymology, 2001
Publisher Summary This chapter concentrates on the methods used to express a Drosophila recombinat 5′ → 3′-exoribonuclease, purify the protein, and analyze its activity in vitro . Analysis of early development in Drosophila has shown that RNA localization, control of translation, and mRNA stability are intimately linked.
I V, Chernukhin, J E, Seago, S F, Newbury   +2 more
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Exoribonucleases and Endoribonucleases

EcoSal Plus, 2004
This review provides a description of the known Escherichia coli ribonucleases (RNases), focusing on their structures, catalytic properties, genes, physiological roles, and possible regulation. Currently, eight E. coli exoribonucleases are known.
Zhongwei, Li, Murray P, Deutscher
openaire   +2 more sources

Promiscuous exoribonucleases of Escherichia coli [PDF]

Journal of Bacteriology, 1993
exaly   +3 more sources

Escherichiacoli mutants deficient in exoribonucleases

Biochemical and Biophysical Research Communications, 1976
Abstract Strain S296, isolated by screening 2000 colonies after nitrosoguanidine mutagenesis, yields extracts with less than 1% of wild-type RNase activity against ( 3 H) poly(U). Unlike other E. coli strains, S296 grows with a doubling time of about 2 hr., both in nutrient broth and in minimal medium, and at 30°, 37° and 42°. The strain retains
N, Nikolaev, V, Folsom, D, Schlessinger
openaire   +2 more sources

A microsomal exoribonuclease from rat liver

Biochimica et Biophysica Acta (BBA) - Enzymology, 1979
A exoribonuclease has been purified from the microsomes of rat liver. The enzyme had an apparent molecular weight of 80 000-83 000 and produced, via a processive mechanism, 5'-AMP as the only product from poly(A). The degradation was found to proceed in the 3' to 5' direction.
H, Kumagai, K, Igarashi, K, Tanaka, H, Nakao, S, Hirose   +4 more
openaire   +2 more sources

Structures of 5′–3′ Exoribonucleases

2012
5'-3' Exoribonucleases (XRNs) have important functions in RNA processing, RNA turnover and decay, RNA interference, RNA polymerase transcription, and other cellular processes. Their sequences share two highly conserved regions, CR1 and CR2. The cytoplasmic Xrn1 and the nuclear Xrn2/Rat1 are found in yeast and animals, and XRNs are found in most other ...
Jeong Ho, Chang, Song, Xiang, Liang, Tong   +2 more
openaire   +2 more sources

5′-3′ Exoribonucleases

2011
The 5′-3′ exoribonucleases have important functions in RNA processing, RNA degradation, RNA interference, transcription, and other cellular processes. The Xrn1 and Xrn2/Rat1 family of enzymes are the best characterized 5′-3′ exoribonucleases, and there has been significant recent progress in the understanding of their structure and function. Especially,
Jeong Ho Chang, Song Xiang, Liang Tong
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5′-Exoribonuclease 1: Xrn1

2001
Publisher Summary The detection, purification, and partial characterization of 5′-exoribonuclease 1 (Xrn1) from Saccharomyces cerevisiae as a 160-kDa RNase was reported in 1980 and 1985. The enzyme is a processive exonuclease hydrolyzing RNA from the 5′ end with the production of 5′-mononucleofides.
openaire   +2 more sources