Characterization of two homologous disulfide bond systems involved in virulence factor biogenesis in uropathogenic Escherichia coli CFT073 [PDF]
, 2009 Disulfide bond (DSB) formation is catalyzed by disulfide bond proteins and is critical for the proper folding and functioning of secreted and membrane-associated bacterial proteins.
Totsika, Makrina +3 more
core +2 more sources
Hierarchical formation of disulphide bonds in the immunoglobulin Fc-Fragment is assisted by Protein Disulphide Isomerase [PDF]
, 2004 Antibodies provide an excellent system to study the folding and assembly of all β-sheet proteins and to elucidate the hierarchy of intra/inter chain disulfide bonds formation during the folding process of multimeric and multidomain proteins.
F. Vinci +6 more
core +1 more source
PLoS ONE, 2015 MIS416 is an intact minimal cell wall skeleton derived from Proprionibacterium acnes that is phagocytosed by antigen presenting cells, including dendritic cells (DCs).
Francesco Mainini +4 more
doaj +1 more source
NMR solution structure of a chymotrypsin inhibitor from the Taiwan cobra Naja naja atra [PDF]
, 2013 The Taiwan cobra (Naja naja atra) chymotrypsin inhibitor (NACI) consists of 57 amino acids and is related to other Kunitz-type inhibitors such as bovine pancreatic trypsin inhibitor (BPTI) and Bungarus fasciatus fraction IX (BF9), another chymotrypsin ...
Chang, Long-Sen +3 more
core +2 more sources
iScience, 2021 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
Disulfide bond formation and ToxR activity in Vibrio cholerae. [PDF]
PLoS ONE, 2012 Virulence factor production in Vibrio cholerae is complex, with ToxRS being an important part of the regulatory cascade. Additionally, ToxR is the transcriptional regulator for the genes encoding the major outer membrane porins OmpU and OmpT.
Vera H I Fengler +7 more
doaj +1 more source
Synthesis of the Most Potent Isomer of μ-Conotoxin KIIIA Using Different Strategies
Molecules, 2023 In the chemical synthesis of conotoxins with multiple disulfide bonds, the oxidative folding process can result in diverse disulfide bond connectivities, which presents a challenge for determining the natural disulfide bond connectivities and leads to ...
Xunxun Jian +5 more
doaj +1 more source
The N-terminal shuttle domain of Erv1 determines the affinity for Mia40 and mediates electron transfer to the catalytic Erv1 core in yeast mitochondria [PDF]
, 2010 Erv1 and Mia40 constitute the two important components of the disulfide relay system that mediates oxidative protein folding in the mitochondrial intermembrane space. Mia40 is the import receptor that recognizes the substrates introducing disulfide bonds
Aivaliotis, M. +3 more
core +1 more source
PLoS ONE, 2015 Maternal nicotine exposure has been associated with many adverse fetal and placental outcomes. Although underlying mechanisms remain elusive, recent studies have identified that augmented endoplasmic reticulum (ER) stress is linked to placental ...
Michael K Wong +3 more
doaj +1 more source
The quiescin sulfhydryl oxidase (hQSOX1b) tunes the expression of resistin-like molecule alpha (RELM-α or mFIZZ1) in a wheat germ cell-free extract. [PDF]
PLoS ONE, 2013 Although disulfide bond formation in proteins is one of the most common types of post-translational modifications, the production of recombinant disulfide-rich proteins remains a challenge.
Wael Gad +9 more
doaj +1 more source