Results 61 to 70 of about 3,418,558 (223)
Disulfide Bond–Modified Proteomics Reveals the Effects of Riboflavin on Protein Folding Dynamics
Riboflavin deficiency impairs oxidative protein folding, causing ER misfolded protein accumulation, CHOP activation, and apoptosis, revealing a role of riboflavin in proteostasis. ABSTRACT Riboflavin is a crucial micronutrient essential for maintaining cellular homeostasis, acting as an important precursor for flavoproteins that utilize flavin ...
Bo Zhang, Shuisheng Hou, Jing Tang
wiley +1 more source
Characterisation of the oxidoreductase Erol-Lß and the misfolding of the secretory pathway substrate HLA-B27 [PDF]
The endoplasmic reticulum (ER) is the site of oxidative folding for proteins entering the secretory pathway. Here, nascent polypeptides acquire disulfide bonds, which confer both stability and functionality on secretory and ER-resident proteins.
Lemin, Andrew James
core
Disulfide-bond-forming (DSB) oxidative folding enzymes are master regulators of virulence that are localized to the periplasm of many Gram-negative bacteria.
Whitten, Andrew E. +11 more
core +1 more source
Summary: The mammalian endoplasmic reticulum (ER) harbors more than 20 members of the protein disulfide isomerase (PDI) family that act to maintain proteostasis.
Chihiro Hirayama +7 more
doaj +1 more source
ABSTRACT Modern biopharmaceutical manufacturing requires purification platforms capable of processing structurally and functionally diverse products while addressing the challenge of removing persistent and high‐risk host cell proteins (HCPs).
Wenning Chu +23 more
wiley +1 more source
Characterising the expression and interactions of the Endoplasmic Reticulum Oxidoreductase Erol β [PDF]
Proteins destined for the secretory pathway and endoplasmic reticulum (ER) resident proteins are targeted to the ER through an N-terminal signal sequence. Proteins then follow a post-translational maturation process to fold into functional proteins.
Gunasekara, Sanjika Dias
core
Mitochondria‐endoplasmic reticulum contact sites (MERCS) are areas where the mitochondria and endoplasmic reticulum closely interact. In this study, we utilize synthetic organelle glues to artificially engineer MERCS for regulating cardiomyocyte development, through which the immature and chemo‐plasticity issues of undifferentiated cells are addressed.
Wei Tang +9 more
wiley +1 more source
Replacement of domain b of human protein disulfide isomerase-related protein with domain b′ of human protein disulfide isomerase dramatically increases its chaperone activity [PDF]
We have reported that human protein disulfide isomerase-related protein (hPDIR) has isomerase and chaperone activities that are lower than those of the human protein disulfide isomerase (hPDI), and that the b domain of hPDIR is critical for its chaperone
Daisuke Iguchi +11 more
core +1 more source
Protein Disulfide Isomerase A4 Is Involved in Genome Uncoating during Human Astrovirus Cell Entry
Although human astroviruses (HAstVs) are important agents of gastroenteritis in young children, the studies aimed at characterizing their biology have been limited, in particular regarding their cell entry process. It has been shown that HAstV serotype 8
Nayeli Aguilar-Hernández +4 more
doaj +1 more source
Secretopathies emerge as a new class of neurocristopathies
Abstract Neural crest cells are a transient embryonic population of cells that give rise to a wide range of structures, including craniofacial cartilage and bone, peripheral neurons and glia, as well as components of the cardiac outflow tract, among others.
Amanda Teixeira +3 more
wiley +1 more source

