Results 71 to 80 of about 1,851 (152)

The unfolded protein response links ER stress to cancer-associated thrombosis

open access: yesJCI Insight, 2023
Thrombosis is a common complication of advanced cancer, yet the cellular mechanisms linking malignancy to thrombosis are poorly understood. The unfolded protein response (UPR) is an ER stress response associated with advanced cancers.
Oluwatoyosi Muse   +10 more
doaj   +1 more source

Charcot‐Marie‐Tooth disease in children

open access: yesAnnals of the Child Neurology Society, Volume 2, Issue 4, Page 256-268, December 2024.
Abstract Charcot‐Marie‐Tooth (CMT) disease represents a diverse group of inherited neuropathies with a broad spectrum of symptoms. It is the most prevalent inherited neuropathy, with an estimated prevalence ranging from 9.7 to 82 cases per 100,000 individuals.
Ezgi Saylam   +4 more
wiley   +1 more source

Correction: Phosphorylation Affects DNA-Binding of the Senescence-Regulating bZIP Transcription Factor GBF1. Plants 2015, 4, 691–709

open access: yesPlants, 2016
The authors wish to make the following corrections to their paper [1].[...]
Anja Smykowski   +2 more
doaj   +1 more source

Workflow to Select Functional Promoter DNA Baits and Screen Arrayed Gene Libraries in Yeast

open access: yesCurrent Protocols, Volume 4, Issue 11, November 2024.
Abstract The yeast one‐hybrid system (Y1H) is used extensively to identify DNA–protein interactions. The generation of large collections of open reading frames (ORFs) to be used as prey in screenings is not a bottleneck nowadays and can be carried out in‐house or offered as a service by companies. However, the straightforward use of full gene promoters
Iris Fañanás‐Pueyo   +4 more
wiley   +1 more source

Quantitative proteomics of Uukuniemi virus - host cell interactions reveals GBF1 as proviral host factor for phleboviruses. [PDF]

open access: yes, 2019
Novel tick-borne phleboviruses in the Phenuiviridae family, which are highly pathogenic in humans and all closely related to Uukuniemi virus (UUKV), have recently emerged on different continents.
Voss, Yannik   +42 more
core   +1 more source

Novel Arf1 Inhibitors Drive Cancer Stem Cell Aging and Potentiate Anti‐Tumor Immunity

open access: yesAdvanced Science, Volume 11, Issue 39, October 23, 2024.
Potent small‐molecule inhibitors of Arf1, designated as DU101 and DU102, have been discovered to initiate a series of aging processes in CSCs and systemically remodeled immune microenvironment including increasing the population of tumor‐associated CD8+ CD4+ double‐positive T (DPT) cells in preclinical mouse cancer and PDX models.
Yuetong Wang   +10 more
wiley   +1 more source

Golgicide A Reveals Essential Roles for GBF1 in Golgi Assembly and Function [PDF]

open access: yes, 2013
ADP-ribosylation factor 1 (Arf1) plays a critical role in regulating secretory traffic and membrane transport within the Golgi of eukaryotic cells. Arf1 is activated by guanine nucleotide exchange factors (ArfGEFs) which confer spatial and temporal ...
Bursulaya, Badry   +6 more
core   +1 more source

MYC2 regulates ARR16, a component of cytokinin signaling pathways, in Arabidopsis seedling development

open access: yesPlant Direct, 2019
MYC2 is a basic helix‐loop‐helix transcription factor that acts as a repressor of blue light‐mediated photomorphogenic growth; however, it promotes lateral root formation.
Archana Kumari Srivastava   +2 more
doaj   +1 more source

Structure-Function Relationships In The Sec7 Guanine Nucleotide Exchange Factor Gbf1 [PDF]

open access: yes, 2016
All eukaryotic cells contain a secretory pathway composed of membrane-bound compartments connected by vesicles that transport cargo from the endoplasmic reticulum (ER) through the Golgi apparatus to various destination within and outside the cell.
Bhatt, Jay Manoj
core  

GBF1- and ACBD3-independent recruitment of PI4KIIIβ to replication sites by rhinovirus 3A proteins [PDF]

open access: yes, 2014
PI4KIIIβ recruitment to Golgi membranes relies on GBF1/Arf and ACBD3. Enteroviruses like poliovirus and coxsackievirus recruit PI4KIIIβ to their replication sites via their 3A proteins. Here, we show that human rhinovirus (HRV) 3A also recruited PI4KIIIβ
van der Schaar, Hilde M   +16 more
core   +3 more sources

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