Endoplasmic reticulum stress and the development of diabetes: a review
HP Harding, D Ron - Diabetes, 2002 - Am Diabetes Assoc
The early steps of insulin biosynthesis occur in the endoplasmic reticulum (ER), and the β-
cell has a highly developed and active ER. All cells regulate the capacity of their ER to fold …
cell has a highly developed and active ER. All cells regulate the capacity of their ER to fold …
Uncoupling proteostasis and development in vitro with a small molecule inhibitor of the pancreatic endoplasmic reticulum kinase, PERK
HP Harding, AF Zyryanova, D Ron - Journal of Biological Chemistry, 2012 - ASBMB
Loss-of-function mutations in EIF2AK3, encoding the pancreatic endoplasmic reticulum (ER)
kinase, PERK, are associated with dysfunction of the endocrine pancreas and diabetes …
kinase, PERK, are associated with dysfunction of the endocrine pancreas and diabetes …
Proinsulin misfolding and endoplasmic reticulum stress during the development and progression of diabetes☆
J Sun, J Cui, Q He, Z Chen, P Arvan, M Liu - Molecular aspects of medicine, 2015 - Elsevier
To maintain copious insulin granule stores in the face of ongoing metabolic demand,
pancreatic beta cells must produce large quantities of proinsulin, the insulin precursor …
pancreatic beta cells must produce large quantities of proinsulin, the insulin precursor …
Endoplasmic reticulum stress in β-cells and development of diabetes
SG Fonseca, M Burcin, J Gromada, F Urano - Current opinion in …, 2009 - Elsevier
The endoplasmic reticulum (ER) is a cellular compartment responsible for multiple important
cellular functions including the biosynthesis and folding of newly synthesized proteins …
cellular functions including the biosynthesis and folding of newly synthesized proteins …
Endoplasmic reticulum stress, pancreatic β-cell degeneration, and diabetes
FR Papa - Cold Spring Harbor perspectives in …, 2012 - perspectivesinmedicine.cshlp.org
Overwhelming of protein folding in the endoplasmic reticulum (ER)—referred to as “ER
stress”—activates a set of intracellular signaling pathways termed the unfolded protein …
stress”—activates a set of intracellular signaling pathways termed the unfolded protein …
[HTML][HTML] Endoplasmic reticulum stress and eIF2α phosphorylation: The Achilles heel of pancreatic β cells
M Cnop, S Toivonen, M Igoillo-Esteve, P Salpea - Molecular metabolism, 2017 - Elsevier
Background Pancreatic β cell dysfunction and death are central in the pathogenesis of most
if not all forms of diabetes. Understanding the molecular mechanisms underlying β cell …
if not all forms of diabetes. Understanding the molecular mechanisms underlying β cell …
ER stress and development of type 1 diabetes
F Engin - Journal of Investigative Medicine, 2016 - journals.sagepub.com
Type 1 diabetes (T1D) results from an autoimmune-mediated destruction of pancreatic β
cells. The incidence of T1D is on the rise globally around 3% to 5% per year and rapidly …
cells. The incidence of T1D is on the rise globally around 3% to 5% per year and rapidly …
Endoplasmic reticulum stress and diabetes mellitus
E Araki, S Oyadomari, M Mori - Internal medicine, 2003 - jstage.jst.go.jp
Pancreatic p-cells are strongly engagedin protein secretion and have highly developed
endoplasmic reticulum (ER). Proper folding of polypeptide into a threedimensional structure …
endoplasmic reticulum (ER). Proper folding of polypeptide into a threedimensional structure …
Translational control is required for the unfolded protein response and in vivo glucose homeostasis
The accumulation of unfolded protein in the endoplasmic reticulum (ER) attenuates protein
synthesis initiation through phosphorylation of the α subunit of eukaryotic translation …
synthesis initiation through phosphorylation of the α subunit of eukaryotic translation …
The endoplasmic reticulum stress response in the pancreatic β‐cell
A Volchuk, D Ron - Diabetes, Obesity and Metabolism, 2010 - Wiley Online Library
Eukaryotic cells respond to stress in the endoplasmic reticulum (ER) resulting from
insufficient protein folding capacity or altered ER homeostasis by activating the unfolded …
insufficient protein folding capacity or altered ER homeostasis by activating the unfolded …
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