Results 121 to 130 of about 354,238 (282)

A dsRNA Viral Transcriptional Regulator Evades Innate Immunity by Hijacking Host CoTranscription Factor DHX9

open access: yesAdvanced Science, EarlyView.
This study identifies a new viral mechanism by a viral protein σ3 that functions as a vTR to suppress NF‐κB gene expression via its direct interaction with the host helicase DHX9. Through their interaction, σ3 not only impairs the initial recruitment of Pol II but also affects Pol II pause‐release and ultimately suppresses NF‐κB gene expression ...
Xueyang Pang   +12 more
wiley   +1 more source

Site-Directed Mutagenesis v1

open access: yes, 2018

Moriah Beck, Abby Jurgensmeier
openaire   +1 more source

Cleavage‐Resistant CYLD Protects Against Autoimmune Hepatitis

open access: yesAdvanced Science, EarlyView.
Proteolytic cleavage of the deubiquitinase CYLD emerges as a critical driver of autoimmune hepatitis. TNFα‐induced CYLD loss in macrophages amplifies S100A9‐triggered MAPK activation, leading to excessive chemokine production and hepatic inflammation. Pharmacological inhibition of MEK signaling effectively attenuates experimental disease, highlighting ...
Han Liu   +13 more
wiley   +1 more source

キイロショウジョウバエ由来のチオレドキシン還元酵素のC未端テトラペプチド配列は、ヒト肺由来のチオレドキシン還元酵素では酸化還元活性を示さない [PDF]

open access: yes, 2007
The isozymes of mammalian thioredoxin reductase (TrxR) contain the penultimate selenocysteineresidue (SeCys) in the redox-active C-terminal tetrapeptide, -Gly-Cys-SeCys-Gly (end). Amutant form of the mammalian enzyme TrxR-X498C in which SeCys is replaced
Inagaki, Kenji   +3 more
core  

ERM Inhibition Confers Ferroptosis Resistance through ROS‐Induced NRF2 Signaling

open access: yesAdvanced Science, EarlyView.
ERM inhibition disrupts ERM‐actin interactions, elevating ROS and triggering KEAP1 degradation, which stabilizes and activates NRF2. Nuclear NRF2 induces cytoprotective genes, notably HMOX1, enhancing redox buffering and suppressing lipid peroxidation to resist erastin‐induced ferroptosis.
Menghao Qiao   +19 more
wiley   +1 more source

Endocytic Control of Cell‐Autonomous and Non‐Cell‐Autonomous Functions of p53

open access: yesAdvanced Science, EarlyView.
NUMB Ex3‐containing isoforms localize to the plasma membrane, where they recruit p53 through SNX9 and direct it to multivesicular bodies and exosomes. Exported p53 is taken up by neighboring cells and activates nuclear programs, revealing an intercellular, exosome‐based pathway that might help establish a tumor‐suppressive microenvironment.
Roberta Cacciatore   +20 more
wiley   +1 more source

PDIA3 Inhibition Facilitates Sensitivity of IKE‐Induced Ferroptosis via STAT3/LCN2 Axis to Improve Glioblastoma Therapy

open access: yesAdvanced Science, EarlyView.
In this manuscript, protein disulfide isomerase A3 (PDIA3) is identified as a key factor mediating the susceptibility of ferroptosis in GBM. Inhibition of PDIA3 enhances IKE or cystine starvation‐induced ferroptosis in GBM cells by resulting in the accumulation of lipid peroxidation and a reduction in GSH level.
Jie Zhang   +19 more
wiley   +1 more source

A Natural Sweetener‐inducible Genetic Switch Controls Therapeutic Protein Expression in Mammals

open access: yesAdvanced Science, EarlyView.
This study develops a natural sweetener, the psicose‐inducible transgene expression (PURE) system based on an Agrobacterium tumefaciens–derived transcriptional repressor PsiR. The PURE system is highly specific to psicose, being insensitive to other sugars and structurally similar molecules.
Longliang Qiao   +16 more
wiley   +1 more source

Modification of a PCRBased Site-Directed Mutagenesis Method

open access: yesBioTechniques, 1997
Constance L. Fisher, Guo Kui Pei
doaj   +1 more source

Site directed mutagenesis and purification of the cDNA for human class I aldehyde dehydrogenase : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science at Massey University [PDF]

open access: yes, 1998
Aldehyde dehydrogenase (ALDH) is a key enzyme of alcohol metabolism, removing acetaldehyde which is formed as a product of the alcohol dehydrogenase reaction.
Wansbrough, Erin M
core  

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