Results 51 to 60 of about 20,358 (251)

Quantitative analysis of snoRNA association with pre-ribosomes and release of snR30 by Rok1 helicase [PDF]

open access: yes, 2008
In yeast, three small nucleolar RNAs (snoRNAs) are essential for the processing of pre-ribosomal RNA—U3, U14 and snR30—whereas 72 non-essential snoRNAs direct site-specific modification of pre-rRNA. We applied a quantitative screen for alterations in the
Martin Kos   +6 more
core   +1 more source

A conserved role of a DEAD box helicase in mRNA masking [PDF]

open access: yesRNA, 2001
Clam p82 is a member of the cytoplasmic polyadenylation element-binding protein (CPEB) family of RNA-binding proteins and serves dual functions in regulating gene expression in early development. In the oocyte, p82/CPEB is a translational repressor, whereas in the activated egg, it acts as a polyadenylation factor. Coimmunoprecipitations were performed
N, Minshall, G, Thom, N, Standart
openaire   +2 more sources

DEAD-box helicase 56 functions as an oncogene promote cell proliferation and invasion in gastric cancer via the FOXO1/p21 Cip1/c-Myc signaling pathway. [PDF]

open access: yesBioengineered, 2022
DEAD-box helicase (DDX) family exerts a critical effect on cancer initiation and progression through alternative splicing, transcription and ribosome biogenesis.
Wang J   +9 more
europepmc   +2 more sources

Expression of DDX3 is directly modulated by hypoxia inducible factor-1 alpha in breast epithelial cells [PDF]

open access: yes, 2011
DEAD box protein, DDX3, is aberrantly expressed in breast cancer cells ranging from weakly invasive to aggressive phenotypes and functions as an important regulator of cancer cell growth and survival.
Krishnamachary, B.   +16 more
core   +1 more source

Comparative structural analysis of human DEAD-box RNA helicases. [PDF]

open access: yesPLoS ONE, 2010
DEAD-box RNA helicases play various, often critical, roles in all processes where RNAs are involved. Members of this family of proteins are linked to human disease, including cancer and viral infections.
Patrick Schütz   +12 more
doaj   +1 more source

Snf2 family ATPases and DExx box helicases:differences and unifying concepts from high-resolution crystal structures [PDF]

open access: yes, 2006
Proteins with sequence similarity to the yeast Snf2 protein form a large family of ATPases that act to alter the structure of a diverse range of DNA-protein structures including chromatin. Snf2 family enzymes are related in sequence to DExx box helicases,
Owen-Hughes, Tom; id_orcid   +3 more
core   +1 more source

Splicing Factor DDX23, Transcriptionally Activated by E2F1, Promotes Ovarian Cancer Progression by Regulating FOXM1

open access: yesFrontiers in Oncology, 2021
Ovarian carcinoma remains the most lethal gynecological carcinoma. Abnormal expression of splicing factors is closely related to the occurrence and development of tumors.
Chen Zhao   +17 more
doaj   +1 more source

Molecular insights into RNA and DNA helicase evolution from the determinants of specificity for a DEAD-box RNA helicase

open access: yeseLife, 2014
How different helicase families with a conserved catalytic ‘helicase core’ evolved to function on varied RNA and DNA substrates by diverse mechanisms remains unclear.
Anna L Mallam   +2 more
doaj   +1 more source

Broad anti-pathogen potential of DEAD box RNA helicase eIF4A-targeting rocaglates

open access: yesScientific Reports, 2023
Inhibition of eukaryotic initiation factor 4A has been proposed as a strategy to fight pathogens. Rocaglates exhibit the highest specificities among eIF4A inhibitors, but their anti-pathogenic potential has not been comprehensively assessed across ...
Wiebke Obermann   +22 more
doaj   +1 more source

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

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

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