Results 111 to 120 of about 86,419 (320)
Extracellular pools of intracellular molecular chaperones are increasingly evident. The peri/epicellular(pec) pool of the endoplasmic reticulum redox chaperone protein disulfide isomerase-A1(PDI) is involved in thrombosis and vascular remodeling, while ...
Thaís L.S. Araujo +2 more
doaj +1 more source
Retarded PDI diffusion and a reductive shift in poise of the calcium depleted endoplasmic reticulum [PDF]
Background: Endoplasmic reticulum (ER) lumenal protein thiol redox balance resists dramatic variation in unfolded protein load imposed by diverse physiological challenges including compromise in the key upstream oxidases.
AE Palmer +43 more
core +2 more sources
Abstract The isoproterenol‐induced myocardial infarction model is a well‐established experimental approach for studying cardiac injury and testing potential protective treatments. By overstimulating beta‐adrenergic receptors, this model closely reproduces key features of human heart attacks, including oxidative damage, calcium imbalance, inflammatory ...
Bushra Imran +5 more
wiley +1 more source
Anterior gradient protein 2 promotes survival, migration and invasion of papillary thyroid carcinoma cells [PDF]
Through a transcriptome microarray analysis, we have isolated Anterior gradient protein 2 (AGR2) as a gene up-regulated in papillary thyroid carcinoma (PTC).
Chiappetta, G +11 more
core +1 more source
Thiol isomerases such as protein-disulfide isomerase (PDI) direct disulfide rearrangements required for proper folding of nascent proteins synthesized in the endoplasmic reticulum.
Jack D. Stopa +4 more
semanticscholar +1 more source
Proteome Analysis of Corynebacterium diphtheriae–Macrophage Interaction
ABSTRACT Contact of Corynebacterium diphtheriae with macrophages induces adaptations on both bacterial and cellular sides. The study presented here was aiming to shed light on the simultaneous intracellular adaptation of the bacteria and changes in the proteome of the phagocytes in response to the internalization of C. diphtheriae.
Luca Musella +6 more
wiley +1 more source
A substrate-driven allosteric switch that enhances PDI catalytic activity
Protein Disulfide Isomerase (PDI) is a prothrombotic, multidomain enzyme with separate substrate binding and catalytic domains. Here, the authors identify a new class of compounds that target the PDI substrate binding site, inducing a conformational ...
Roelof H. Bekendam +12 more
doaj +1 more source
Reticulon1-C modulates protein disulphide isomerase function [PDF]
Endoplasmic reticulum (ER) is the primary site for the synthesis and folding of secreted and membrane-bound proteins. Accumulation of unfolded and misfolded proteins in ER underlies a wide range of human neurodegenerative disorders.
Bernardoni, P +8 more
core +1 more source
The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in Neurodegeneration
The maintenance and regulation of proteostasis is a critical function for post-mitotic neurons and its dysregulation is increasingly implicated in neurodegenerative diseases. Despite having different clinical manifestations, these disorders share similar
E. Perri +4 more
semanticscholar +1 more source
Protein processing in the endoplasmic reticulum is highlighted in response to heat stress in Platysternon megacephalum. Under heat stress, the up‐regulation of genes such as CHOP in protein processing in the endoplasmic reticulum pathway, along with the suppression of energy and lipid metabolism and the up‐regulation of JARID2 expression, leads to ...
Jian Hong +7 more
wiley +1 more source

