Results 81 to 90 of about 41,132 (234)
Protein disulfide isomerases – a way to tackle malaria
Trends in Parasitology, 2023 Protein disulfide isomerases (PDIs) ensure that specific substrate proteins are correctly folded. PDI activity plays an essential role in malaria transmission. Here we provide an overview of the role of PDIs in malaria-causing Plasmodium parasites and outline why PDI inhibition could be a novel way to treat malaria and prevent transmission.
Fiona Angrisano +3 more
openaire +2 more sources
Mass Spectrometry Reviews, EarlyView.ABSTRACT Top‐down proteomics (TDP) characterizes proteoforms in cells, tissues, and biofluids, in discovery mode and on a global scale, requiring analytical tools with high peak capacity for proteoform separation and high sensitivity for proteoform detection, given the extremely high proteoform complexity and wide proteoform concentration dynamic range.
Guijie Zhu +5 more
wiley +1 more source
, 2020 The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Agh R +13 more
core +1 more source
Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases [PDF]
, 2014 Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as protein disulfide isomerase and a mechanism to form disulfides de novo.
Appenzeller-Herzog +22 more
core +1 more source
Multiple protein disulfide isomerases support thrombosis [PDF]
Current Opinion in Hematology, 2018 Purpose of review The present review provides an overview of recent findings on new members of the protein disulfide isomerase (PDI) family required for thrombosis. Recent findings Twenty years ago PDI was shown to mediate platelet aggregation, and 10 years ago PDI was shown to ...
David W, Essex, Yi, Wu
openaire +2 more sources
The Journal of Pathology, EarlyView.Abstract Endoplasmic reticulum stress (ERS) occurs when the protein‐folding capacity of the endoplasmic reticulum (ER) is overwhelmed, triggering the unfolded protein response (UPR) to restore homeostasis. However, severe or persistent ERS can shift the UPR toward pro‐inflammatory, apoptotic, and fibrotic signaling, thereby exacerbating tissue injury ...
Lanlan Song +6 more
wiley +1 more source
Diabetes, Metabolic Syndrome and Obesity, 2020 Chunyan Liu, Yanan Hao, Fei Yin, Jianhui Liu Chongqing Key Laboratory of Medicinal Chemistry & Molecular Pharmacology, Chongqing University of Technology, Chongqing 400054, People’s Republic of ChinaCorrespondence: Jianhui Liu; Fei YinChongqing
Liu C, Hao Y, Yin F, Liu J
doaj
Expression of Functional Human Sialyltransferases ST3Gal1 and ST6Gal1 in Escherichia coli.
PLoS ONE, 2016 Sialyltransferases (STs) are disulfide-containing, type II transmembrane glycoproteins that catalyze the transfer of sialic acid to proteins and lipids and participate in the synthesis of the core structure oligosaccharides of human milk.
Maria Elena Ortiz-Soto, Jürgen Seibel
doaj +1 more source
Inhibition of thiol isomerase activity diminishes endothelial activation of plasminogen, but not of protein C [PDF]
, 2015 Highlights •A range of thiol isomerase enzymes were expressed by HMEC-1 endothelial cells. •Inhibition of thiol isomerases reduced plasminogen activation on HMEC-1 cells.
Gordge, M.P. +7 more
core +1 more source
Proteome Analysis of Corynebacterium diphtheriae–Macrophage Interaction
PROTEOMICS, EarlyView.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