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Stress-Independent Activation of XBP1s and/or ATF6 Reveals Three Functionally Distinct ER Proteostasis Environments

NIAID Data Ecosystem2026-03-07 收录

内质网蛋白质稳态

ATF6功能研究

数据链接：

https://www.ncbi.nlm.nih.gov/bioproject/PRJNA192597 数据链接链接失效反馈

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资源简介：

This SuperSeries is composed of the SubSeries listed below. Overall design: Refer to individual Series

应用场景：

创建时间：

2013-03-07

IRE1/XBP1s激活剂筛选

内质网蛋白质稳态

Activation of the IRE1/XBP1s signaling arm of the unfolded protein response (UPR) is a promising strategy to correct defects in endoplasmic reticulum (ER) proteostasis implicated in diverse diseases.

NIAID Data Ecosystem90

Stress-Independent Activation of XBP1s and/or ATF6 Reveals Three Functionally Distinct ER Proteostasis Environments [HEK293DYG]

内质网蛋白质稳态

未折叠蛋白反应研究

The unfolded protein response (UPR) maintains endoplasmic reticulum (ER) proteostasis through the activation of transcription factors such as XBP1s and ATF6. The functional consequences of these trans

NIAID Data Ecosystem60

Kawano et al., Cell Reports

睡眠调控机制

内质网蛋白质稳态

Raw data for Kawano et al., "ER proteostasis regulators cell-non-autonomously control sleep" (Cell Reports; 2023)

NIAID Data Ecosystem60

Divergent Proteome Reactivity Influences Arm-Selective Activation of Pharmacological Endoplasmic Reticulum Proteostasis Regulators. Divergent Proteome Reactivity Influences Arm-Selective Activation of Pharmacological Endoplasmic Reticulum Proteostasis Regulators

内质网蛋白质稳态

ATF6通路药理学激活

Pharmacological activation of the activating transcription factor 6 (ATF6) arm of the Unfolded Protein Response (UPR) has proven useful for ameliorating proteostasis deficiencies in a variety of etiol

NIAID Data Ecosystem60

Control of AGR2 dimerization links endoplasmic reticulum proteostasis to inflammation

内质网蛋白质稳态

炎症性肠病分子机制

Anterior Gradient 2 (AGR2) is a dimeric Protein Disulfide Isomerase family member involved in the regulation of protein quality control in the Endoplasmic Reticulum (ER). Mouse AGR2 deletion increases

NIAID Data Ecosystem60

Stress-Independent Activation of XBP1s and/or ATF6 Reveals Three Functionally Distinct ER Proteostasis Environments

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