Novel roles for protein disulphide isomerase in disease states: a double edged sword?

Protein disulphide isomerase (PDI) is a multifunctional redox chaperone of the endoplasmic reticulum (ER). Since it was first discovered 40 years ago the functions ascribed to PDI have evolved significantly and recent studies have recognized its distinct functions, with adverse as well as protectiv...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Sonam eParakh [verfasserIn] Julie eAtkin [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2015

Schlagwörter:	Cancer post-translational modifications Protein chaperones protein disulfide isomerase family neurodegnerative diseases

Übergeordnetes Werk:	In: Frontiers in Cell and Developmental Biology - Frontiers Media S.A., 2014, 3(2015)
Übergeordnetes Werk:	volume:3 ; year:2015

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3389/fcell.2015.00030

Katalog-ID:	DOAJ073953067

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callnumber-first	Q - Science
author	Sonam eParakh
spellingShingle	Sonam eParakh misc QH301-705.5 misc Cancer misc post-translational modifications misc Protein chaperones misc protein disulfide isomerase family misc neurodegnerative diseases misc Biology (General) Novel roles for protein disulphide isomerase in disease states: a double edged sword?
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topic_title	QH301-705.5 Novel roles for protein disulphide isomerase in disease states: a double edged sword? Cancer post-translational modifications Protein chaperones protein disulfide isomerase family neurodegnerative diseases
topic	misc QH301-705.5 misc Cancer misc post-translational modifications misc Protein chaperones misc protein disulfide isomerase family misc neurodegnerative diseases misc Biology (General)
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title	Novel roles for protein disulphide isomerase in disease states: a double edged sword?
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title_full	Novel roles for protein disulphide isomerase in disease states: a double edged sword?
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title_sort	novel roles for protein disulphide isomerase in disease states: a double edged sword?
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title_auth	Novel roles for protein disulphide isomerase in disease states: a double edged sword?
abstract	Protein disulphide isomerase (PDI) is a multifunctional redox chaperone of the endoplasmic reticulum (ER). Since it was first discovered 40 years ago the functions ascribed to PDI have evolved significantly and recent studies have recognized its distinct functions, with adverse as well as protective effects in disease. Furthermore, post translational modifications of PDI abrogate its normal functional roles in specific disease states. This review focusses on recent studies that have identified novel functions for PDI relevant to specific diseases.
abstractGer	Protein disulphide isomerase (PDI) is a multifunctional redox chaperone of the endoplasmic reticulum (ER). Since it was first discovered 40 years ago the functions ascribed to PDI have evolved significantly and recent studies have recognized its distinct functions, with adverse as well as protective effects in disease. Furthermore, post translational modifications of PDI abrogate its normal functional roles in specific disease states. This review focusses on recent studies that have identified novel functions for PDI relevant to specific diseases.
abstract_unstemmed	Protein disulphide isomerase (PDI) is a multifunctional redox chaperone of the endoplasmic reticulum (ER). Since it was first discovered 40 years ago the functions ascribed to PDI have evolved significantly and recent studies have recognized its distinct functions, with adverse as well as protective effects in disease. Furthermore, post translational modifications of PDI abrogate its normal functional roles in specific disease states. This review focusses on recent studies that have identified novel functions for PDI relevant to specific diseases.
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title_short	Novel roles for protein disulphide isomerase in disease states: a double edged sword?
url	https://doi.org/10.3389/fcell.2015.00030 https://doaj.org/article/1c880c952a65432eaf5c29ee9f8c343c http://journal.frontiersin.org/Journal/10.3389/fcell.2015.00030/full https://doaj.org/toc/2296-634X
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up_date	2024-07-03T20:31:20.256Z
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