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Regulation of RNA helicase activity: principles and examples

Biological chemistry, 2021
RNA helicases are a ubiquitous class of enzymes involved in virtually all processes of RNA metabolism, from transcription, mRNA splicing and export, mRNA translation and RNA transport to RNA degradation.
Pascal Donsbach, D. Klostermeier
semanticscholar   +1 more source

A DEAD-box RNA helicase in the Escherichia coli RNA degradosome

Nature, 1996
The Escherichia coli RNA degradosome is a multi-enzyme complex that contains the exoribonuclease polynucleotide phosphorylase (PNPase) and the endoribonuclease RNase E. Both enzymes are important in RNA processing and messenger RNA degradation. Here we report that enolase and RhlB are two other major components of the degradosome.
B, Py   +3 more
openaire   +2 more sources

CaRH57, a RNA helicase, contributes pepper tolerance to heat stress

Plant Physiology and Biochemistry, 2023
RNA helicases (RHs) are required for most aspects of RNA metabolism and play an important role in plant stress tolerance. Heat stress (HS) causes the deleterious effects on plant cells, such as membrane disruption and protein misfolding, which results in the inhibition of plant growth and development.
Min Zheng   +6 more
openaire   +2 more sources

The RNA helicase Mtr4p is a duplex-sensing translocase

Nature Chemical Biology, 2016
The conserved Saccharomyces cerevisiae Ski2-like RNA helicase Mtr4p plays essential roles in eukaryotic nuclear RNA processing. RNA helicase activity of Mtr4p is critical for biological functions of the enzyme, but the molecular basis for RNA unwinding is not understood.
Eric M, Patrick   +3 more
openaire   +2 more sources

Molecular determinants of nucleolar translocation of RNA helicase A

Experimental Cell Research, 2007
RNA helicase A (RHA) is a member of the DEAH-box family of DNA/RNA helicases involved in multiple cellular processes and the life cycles of many viruses. The subcellular localization of RHA is dynamic despite its steady-state concentration in the nucleoplasm.
Zhe, Liu   +3 more
openaire   +2 more sources

Pre-mRNA and mRNA binding of human nuclear DNA helicase II (RNA helicase A)

Journal of Cell Science, 1999
ABSTRACT Nuclear DNA helicase II (NDH II), alternatively named RNA helicase A, seems to function as a pre-mRNA and mRNA binding protein in human cells. Immunofluorescence studies of NDH II gave a highly diffused nucleoplasmic staining that was similar to that of hnRNP A1 but differed from the localization of the RNA splicing factor Sc-35.
S, Zhang, C, Herrmann, F, Grosse
openaire   +2 more sources

Solution structures of the double‐stranded RNA‐binding domains from rna helicase A

Proteins: Structure, Function, and Bioinformatics, 2012
AbstractRNA helicase A (RHA) is a highly conserved protein with multifaceted functions in the gene expression of cellular and viral mRNAs. RHA recognizes highly structured nucleotides and catalytically rearranges the various interactions between RNA, DNA, and protein molecules to provide a platform for the ribonucleoprotein complex.
Takashi, Nagata   +7 more
openaire   +2 more sources

Active Disruption of an RNA-Protein Interaction by a DExH/D RNA Helicase

Science, 2001
All aspects of cellular RNA metabolism and the replication of many viruses require DExH/D proteins that manipulate RNA in a manner that requires nucleoside triphosphates. Although DExH/D proteins have been shown to unwind purified RNA duplexes, most RNA molecules in the cellular environment are complexed with proteins.
E, Jankowsky   +3 more
openaire   +2 more sources

A Novel Human Homolog of a Dead-Box RNA Helicase Family

Biochemical and Biophysical Research Communications, 1994
Putative cDNA clones for a nuclear antigen that cross-reacts with anti-human aldolase A monoclonal antibody MAb1A2 were isolated from the HeLa lambda gt11 cDNA library and a candidate clone (clone 3) was analyzed. The cDNA has an open reading frame (ORF) of 1,317 bp encoding a novel RNA helicase belonging to the DEAD RNA helicase family.
Y, Kitajima   +4 more
openaire   +2 more sources

Escherichia coli DbpA Is a 3‘ → 5‘ RNA Helicase

Biochemistry, 2005
Previous work has demonstrated that Escherichia coli DbpA is a nonprocessive RNA helicase that can disrupt short RNA helices on either the 5' side or 3' side of hairpin 92 of 23S rRNA. Here the directionality of the helicase activity of DbpA was determined by using substrates containing a short reporter helix in the presence of a second adjacent helix ...
Camille M, Diges, Olke C, Uhlenbeck
openaire   +2 more sources

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