Negative feedback by IRE1β optimizes mucin production in goblet cells. - Wikidata - awgldk - TriplyDB

Negative feedback by IRE1β optimizes mucin production in goblet cells.

Negative feedback by IRE1β optimizes mucin production in goblet cells.

http://www.wikidata.org/entity/Q36637632

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Innate immunity at mucosal surfaces: the IRE1-RIDD-RIG-I pathway Role of endoplasmic reticulum stress and autophagy as interlinking pathways in the pathogenesis of inflammatory bowel disease Emerging functions of the unfolded protein response in immunity The unfolded protein response in immunity and inflammation Expression of inositol-requiring enzyme 1β is downregulated in colorectal cancer Endoplasmic reticulum stress and oxidative stress in cell fate decision and human disease.The mucus and mucins of the goblet cells and enterocytes provide the first defense line of the gastrointestinal tract and interact with the immune system.Shuttling of information between the mucosal and luminal environment drives intestinal homeostasis.Tight regulation of the unfolded protein sensor Ire1 by its intramolecularly antagonizing subdomain.The Endoplasmic Reticulum Stress Sensor IRE1α in Intestinal Epithelial Cells Is Essential for Protecting against Colitis.Epithelial Sel1L is required for the maintenance of intestinal homeostasis New developments in goblet cell mucus secretion and function IRE1: ER stress sensor and cell fate executor.Regulation of the transcriptome by ER stress: non-canonical mechanisms and physiological consequences.Nuclear Receptors Resolve Endoplasmic Reticulum Stress to Improve Hepatic Insulin Resistance.Regulatory crosstalk within the mammalian unfolded protein response.The essential biology of the endoplasmic reticulum stress response for structural and computational biologists.Endoplasmic reticulum dysfunction in Alzheimer's disease.Physiological roles of regulated Ire1 dependent decay.Mucus layers in inflammatory bowel disease.Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 1. An overview.Organelle autoregulation-stress responses in the ER, Golgi, mitochondria and lysosome.Endoplasmic reticulum stress in intestinal epithelial cell function and inflammatory bowel disease Endoplasmic reticulum quality control in cancer: Friend or foe.Epithelial ER Stress in Crohn's Disease and Ulcerative Colitis.The Unfolded Protein Response in Homeostasis and Modulation of Mammalian Immune Cells.Endoplasmic reticulum stress in the regulation of liver diseases: Involvement of Regulated IRE1α and β-dependent decay and miRNA.Causes and consequences of endoplasmic reticulum stress in rheumatic disease.Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Nexus Implicated in Bowel Disease Pathophysiology The Unfolded Protein Response in the Immune Cell Development: Putting the Caretaker in the Driving Seat.Novel mechanism of enhancing IRE1α-XBP1 signalling via the PERK-ATF4 pathway.Defective ATG16L1-mediated removal of IRE1α drives Crohn's disease-like ileitis.Ultrastructure and immunohistochemical characterization of proteins concerned with the secretory machinery in goat ceruminous glands.An unfolded protein-induced conformational switch activates mammalian IRE1.Intestinal Epithelial Cell Endoplasmic Reticulum Stress and Inflammatory Bowel Disease Pathogenesis: An Update Review.Role of the unfolded protein response in determining the fate of tumor cells and the promise of multi-targeted therapies.Driving Cancer Tumorigenesis and Metastasis Through UPR Signaling.IRE1-XBP1 pathway regulates oxidative proinsulin folding in pancreatic β cells.Immune regulation of the unfolded protein response at the mucosal barrier in viral infection.Role of the unfolded protein response in organ physiology: lessons from mouse models.

P2860

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P2860

Negative feedback by IRE1β optimizes mucin production in goblet cells.

http://www.wikidata.org/entity/Q36637632

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年论文

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2013年论文

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2013年论文

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name

Negative feedback by IRE1β optimizes mucin production in goblet cells.

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Negative feedback by IRE1β optimizes mucin production in goblet cells.

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type

label

Negative feedback by IRE1β optimizes mucin production in goblet cells.

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Negative feedback by IRE1β optimizes mucin production in goblet cells.

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prefLabel

Negative feedback by IRE1β optimizes mucin production in goblet cells.

@ast

Negative feedback by IRE1β optimizes mucin production in goblet cells.

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PNAS.1212484110

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Negative feedback by IRE1β optimizes mucin production in goblet cells.

@en

P2093

Akio Tsuru

http://www.w3.org/2001/XMLSchema#string

Daisuke Nakamura

http://www.w3.org/2001/XMLSchema#string

Hiroshi Kadokura

http://www.w3.org/2001/XMLSchema#string

Kenji Kohno

http://www.w3.org/2001/XMLSchema#string

Megumi Iwano

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Michiko Saito

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Naoko Fujimoto

http://www.w3.org/2001/XMLSchema#string

Satsuki Takahashi

http://www.w3.org/2001/XMLSchema#string

Takao Iwawaki

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P2860

XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease

Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress

XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

Structure of the Dual Enzyme Ire1 Reveals the Basis for Catalysis and Regulation in Nonconventional RNA Splicing

The unfolded protein response signals through high-order assembly of Ire1

Signal integration in the endoplasmic reticulum unfolded protein response

Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins.

Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway.

The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response.

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2864-2869

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110

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3581977

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