Results 91 to 100 of about 15,822 (213)

A conserved structural element in the RNA helicase UPF1 regulates its catalytic activity in an isoform-specific manner [PDF]

open access: yes, 2018
The RNA helicase UPF1 is a key component of the nonsense mediated mRNA decay (NMD) pathway. Previous X-ray crystal structures of UPF1 elucidated the molecular mechanisms of its catalytic activity and regulation.
Bonneau, Fabien   +8 more
core   +3 more sources

N6‐Methyladenosine (m6A) in Liver Disease: Pathogenic Mechanisms and Therapeutic Potential

open access: yesiNew Medicine, EarlyView.
ABSTRACT Accumulating evidence highlights the critical role of epigenetic modifications, particularly N6‐methyladenosine (m6A), in liver disease. As the most abundant RNA modification in eukaryotic cells, m6A is dynamically regulated by multicomponent m6A methyltransferases (e.g., METTL3 and METTL14), demethylases (FTO and ALKBH5), and m6A‐binding ...
Yingfen Chen   +6 more
wiley   +1 more source

Alterations in the expression of DEAD-box and other RNA binding proteins during HIV-1 replication

open access: yesRetrovirology, 2004
Recent results showed that certain DEAD box protein RNA helicases, DDX3 and DDX1, play an important role in the HIV infection cycle by facilitating the export of long, singly spliced or unspliced HIV RNAs from the nucleus via the CRM1-Rev pathway.
Zeichner Steven L, Krishnan Vyjayanthi
doaj   +1 more source

An in vivo control map for the eukaryotic mRNA translation machinery [PDF]

open access: yes, 2013
Rate control analysis defines the in vivo control map governing yeast protein synthesis and generates an extensively parameterized digital model of the translation pathway.
Amy Claydon   +12 more
core   +3 more sources

MDM2 Mediates Nonproteolytic Polyubiquitylation of the DEAD-Box RNA Helicase DDX24 [PDF]

open access: yesMolecular and Cellular Biology, 2014
MDM2 mediates the ubiquitylation and thereby triggers the proteasomal degradation of the tumor suppressor protein p53. However, genetic evidence suggests that MDM2 contributes to multiple regulatory networks independently of p53 degradation. We have now identified the DEAD-box RNA helicase DDX24 as a nucleolar protein that interacts with MDM2.
Takayoshi, Yamauchi   +4 more
openaire   +2 more sources

Oncogenic KRAS Rewires Stress Granule Dynamics: Mechanisms and Therapeutic Opportunities

open access: yesThe Kaohsiung Journal of Medical Sciences, EarlyView.
ABSTRACT Stress granules (SGs) are dynamic, membrane‐less structures that form in response to various cellular stresses, including metabolic, oxidative, and therapeutic challenges. They function as adaptive hubs and reorganize protein synthesis and signaling networks to help cells survive under stress. In cancer, these condensates are often hijacked to
Msimisi Ndzinisa   +2 more
wiley   +1 more source

The ATPase cycle of PcrA helicase and its coupling to translocation on DNA. [PDF]

open access: yes, 2009
The superfamily 1 bacterial helicase PcrA has a role in the replication of certain plasmids, acting with the initiator protein (RepD) that binds to and nicks the double-stranded origin of replication.
Martinez-Senac, Maria M   +3 more
core   +1 more source

LPCAT3 as a Potential Drug Target for Ultraviolet Radiation–Induced Cataract: Insights From Multiomics Analysis

open access: yesThe Kaohsiung Journal of Medical Sciences, EarlyView.
ABSTRACT Ultraviolet B (UVB) radiation is a major risk factor for cataract development, but the molecular mechanisms underlying this process, particularly the involvement of regulated cell death pathways such as ferroptosis, remain unclear. Transcriptomic, proteomic, and metabolomic analyses were performed on lens tissues from UVB‐induced cataract rat ...
Fei Xu   +4 more
wiley   +1 more source

DHX33 transcriptionally controls genes involved in the cell cycle [PDF]

open access: yes, 2016
The RNA helicase DHX33 has been shown to be a critical regulator of cell proliferation and growth. However, the underlying mechanisms behind DHX33 function remain incompletely understood.
Fan, Chunyan   +7 more
core   +2 more sources

Proteome Analysis of Corynebacterium diphtheriae–Macrophage Interaction

open access: yesPROTEOMICS, EarlyView.
ABSTRACT Contact of Corynebacterium diphtheriae with macrophages induces adaptations on both bacterial and cellular sides. The study presented here was aiming to shed light on the simultaneous intracellular adaptation of the bacteria and changes in the proteome of the phagocytes in response to the internalization of C. diphtheriae.
Luca Musella   +6 more
wiley   +1 more source

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