Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM). - Wikidata - wikimedia - TriplyDB

Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM).

Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM).

http://www.wikidata.org/entity/Q39734860

about

Disulphide production by Ero1α-PDI relay is rapid and effectively regulated Killing Me Softly: Connotations to Unfolded Protein Response and Oxidative Stress in Alzheimer's Disease Antioxidant responses and cellular adjustments to oxidative stress Protein folding and quality control in the ER Cell death and survival through the endoplasmic reticulum-mitochondrial axis Endoplasmic reticulum chaperones and oxidoreductases: critical regulators of tumor cell survival and immunorecognition Stress responses from the endoplasmic reticulum in cancer Redox regulation of store-operated Ca2+ entry Proteomic analysis of mitochondrial-associated ER membranes (MAM) during RNA virus infection reveals dynamic changes in protein and organelle trafficking ERO1α-dependent endoplasmic reticulum-mitochondrial calcium flux contributes to ER stress and mitochondrial permeabilization by procaspase-activating compound-1 (PAC-1).Comparative Proteomic Analysis of the Mitochondria-associated ER Membrane (MAM) in a Long-term Type 2 Diabetic Rodent Model.Bax inhibitor-1-mediated inhibition of mitochondrial Ca2+ intake regulates mitochondrial permeability transition pore opening and cell death.Valosin-containing protein-interacting membrane protein (VIMP) links the endoplasmic reticulum with microtubules in concert with cytoskeleton-linking membrane protein (CLIMP)-63 Rab32 modulates apoptosis onset and mitochondria-associated membrane (MAM) properties.Interaction between endoplasmic/sarcoplasmic reticulum stress (ER/SR stress), mitochondrial signaling and Ca(2+) regulation in airway smooth muscle (ASM)Quantitative proteomic analyses of human cytomegalovirus-induced restructuring of endoplasmic reticulum-mitochondrial contacts at late times of infection.Recruitment of cellular prion protein to mitochondrial raft-like microdomains contributes to apoptosis execution.Palmitoylated TMX and calnexin target to the mitochondria-associated membrane.Mitochondrial- and endoplasmic reticulum-associated oxidative stress in Alzheimer's disease: from pathogenesis to biomarkers.Isolation of Endoplasmic Reticulum, Mitochondria, and Mitochondria-Associated Membrane and Detergent Resistant Membrane Fractions from Transfected Cells and from Human Cytomegalovirus-Infected Primary Fibroblasts PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress Interactions between sarco-endoplasmic reticulum and mitochondria in cardiac and skeletal muscle - pivotal roles in Ca²⁺ and reactive oxygen species signaling.Dynamic regulation of Ero1α and peroxiredoxin 4 localization in the secretory pathway.Of yeast, mice and men: MAMs come in two flavors.Mitochondrial Dysregulation Secondary to Endoplasmic Reticulum Stress in Autosomal Dominant Tubulointerstitial Kidney Disease - UMOD (ADTKD-UMOD)Oxidative protein folding in the endoplasmic reticulum: tight links to the mitochondria-associated membrane (MAM).Calcium signaling around Mitochondria Associated Membranes (MAMs).Mitochondria at the interface between danger signaling and metabolism: role of unfolded protein responses in chronic inflammation.Role of mitochondrial raft-like microdomains in the regulation of cell apoptosis.Role of Endoplasmic Reticulum-Mitochondria Communication in Type 2 Diabetes.Subcellular ROS imaging methods: Relevance for the study of calcium signaling.The coming of age of the mitochondria-ER contact: a matter of thickness.Mitochondria-Associated Membranes (MAMs): Overview and Its Role in Parkinson's Disease.Crosstalk between calcium and reactive oxygen species signaling in cancer.Sarcoplasmic reticulum-mitochondria communication in cardiovascular pathophysiology.Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum Mitochondria-Associated Membranes and ER Stress.The Unfolded Protein Response: At the Intersection between Endoplasmic Reticulum Function and Mitochondrial Bioenergetics Mechanisms of cytosolic targeting of matrix metalloproteinase-2.Subcellular Redox Signaling.

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P2860

Ero1alpha requires oxidizing and normoxic conditions to localize to the mitochondria-associated membrane (MAM).

http://www.wikidata.org/entity/Q39734860

description

2010 nî lūn-bûn

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2010年の論文

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年学术文章

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2010年學術文章

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2010年學術文章

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2010年學術文章

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name

Ero1alpha requires oxidizing a ...... ria-associated membrane (MAM).

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Ero1alpha requires oxidizing a ...... ria-associated membrane (MAM).

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S12192-010-0174-1

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Cell Stress & Chaperones

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Ero1alpha requires oxidizing a ...... ria-associated membrane (MAM).

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P2093

Emily M Lynes

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

Jean E Vance

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Matthew D Benson

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Michael Bui

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Russell Watts

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Susanna Y Gilady

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Thomas Simmen

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P2860

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response

Manipulation of oxidative protein folding and PDI redox state in mammalian cells

ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family

Structural organization of the endoplasmic reticulum.

The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha

Getting in and out from calnexin/calreticulin cycles

MAM: more than just a housekeeper

Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44

The gene product of the gp78/AMFR ubiquitin E3 ligase cDNA is selectively recognized by the 3F3A antibody within a subdomain of the endoplasmic reticulum

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s12192-010-0174-1

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619-629

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10.1007/S12192-010-0174-1

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5

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15

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2010-02-26T00:00:00Z

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20186508

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3006622

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