Results 61 to 70 of about 2,163,835 (311)

An improved method for surface immobilisation of RNA: application to small Non-Coding RNA - mRNA pairing [PDF]

open access: yes, 2013
Characterisation of RNA and its intermolecular interactions is increasing in importance as the inventory of known RNA functions continues to expand. RNA-RNA interactions are central to post-transcriptional gene regulation mechanisms in bacteria, and the ...
Darren M. Gowers (485354)   +29 more
core   +2 more sources

Impacts of Small RNAs and Their Chaperones on Bacterial Pathogenicity [PDF]

open access: yesFrontiers in Cellular and Infection Microbiology, 2021
Bacterial small RNAs (sRNAs) are critical post-transcriptional regulators that exert broad effects on cell physiology. One class of sRNAs, referred to as trans-acting sRNAs, base-pairs with mRNAs to cause changes in their stability or translation. Another class of sRNAs sequesters RNA-binding proteins that in turn modulate mRNA expression.
Louise Djapgne   +2 more
openaire   +3 more sources

Recognition of two distinct elements in the RNA substrate by the RNA-binding domain of the T. thermophilus DEAD box helicase Hera [PDF]

open access: yes, 2013
DEAD box helicases catalyze the ATP-dependent destabilization of RNA duplexes. Whereas duplex separation is mediated by the helicase core shared by all members of the family, flanking domains often contribute to binding of the RNA substrate.
Wöhnert, Jens   +5 more
core   +1 more source

RNA Chaperones and the RNA Folding Problem [PDF]

open access: yesJournal of Biological Chemistry, 1995
Functional and structural inter-relationships of RNA and proteins in the execution and control of biological processes such as RNA processing, RNA splicing, and translation are increasingly apparent. In this minireview, I present an RNA chaperone hypothesis, which fosters the view that constraints imposed by fundamental problems in the folding of RNA ...
openaire   +2 more sources

RNA Helicase Proteins as Chaperones and Remodelers [PDF]

open access: yesAnnual Review of Biochemistry, 2014
Superfamily 2 helicase proteins are ubiquitous in RNA biology and have an extraordinarily broad set of functional roles. Central among these roles are the promotion of rearrangements of structured RNAs and the remodeling of ribonucleoprotein complexes (RNPs), allowing formation of native RNA structure or progression through a functional cycle of ...
Inga, Jarmoskaite, Rick, Russell
openaire   +2 more sources

An RNA Chaperone–Like Protein Plays Critical Roles in Chloroplast mRNA Stability and Translation in Arabidopsis and Maize

open access: yesThe Plant Cell, 2019
An RNA-chaperone-like protein stabilizes 3ʹ processed transcripts of photosynthetic electron transfer B (petB) and stimulates the translation of petD and petA in the chloroplasts of vascular plants.
Jing-Jing Jiang   +12 more
semanticscholar   +1 more source

Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD [PDF]

open access: yes, 2012
Schreiner M, Niemann H. Crystal structure of the Yersinia enterocolitica type III secretion chaperone SycD in complex with a peptide of the minor translocator YopD. BMC Structural Biology. 2012;12(1): 13.Background Type III secretion systems are used by
Niemann, H.H.   +5 more
core   +1 more source

The Mitochondrial Chaperone Protein TRAP1 Mitigates α-Synuclein Toxicity [PDF]

open access: yes, 2012
Overexpression or mutation of alpha-Synuclein is associated with protein aggregation and interferes with a number of cellular processes, including mitochondrial integrity and function.
Butler, Erin K.   +41 more
core   +2 more sources

A cold shock protein promotes high-temperature microbial growth through binding to diverse RNA species

open access: yesCell Discovery, 2021
Endowing mesophilic microorganisms with high-temperature resistance is highly desirable for industrial microbial fermentation. Here, we report a cold-shock protein (CspL) that is an RNA chaperone protein from a lactate producing thermophile strain ...
Zikang Zhou   +10 more
doaj   +1 more source

Domain orientation in the RNA helicase YxiN and the role of conformational changes for RNA unwinding [PDF]

open access: yes, 2010
The RNA helicase YxiN from Bacillus subtilis is a member of the family of DEAD box proteins. YxiN is able to unwind RNA double strands in an ATP-dependent manner. The ability to catalyse RNA rearrangement is in vivo presumably necessary for the bacterial
Karow, Anne R.
core   +1 more source

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