Results 81 to 90 of about 3,418,558 (223)
Acta Crystallographica Section F, EarlyView.The high‐resolution structure of the T. aurantiacus xylanase TaXyn10 expressed in Escherichia coli shows that recombinant production combined with split‐intein‐based purification recovers the native fold of TaXyn10 and permits the formation of an N‐terminal pyroglutamate.
Jelena Mijatovic +3 more
wiley +1 more source
Redox Biology, 2017 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
Targeting protein–protein interactions with reversible covalent modalities: Non‐cysteine chemistries
British Journal of Pharmacology, EarlyView.Abstract Protein–protein interactions (PPIs) are central to diverse cellular functions, and represent a rapidly expanding class of therapeutic targets. Advancements in covalent drug design have enabled small‐molecule drugs to overcome challenges associated with engaging these targets, such as limited durations of action and difficult‐to‐drug (expansive,
Ruchira Basu, Steven Fletcher
wiley +1 more source
, 2019 Suppressor of copper sensitivity protein C from Proteus mirabilis (PmScsC) is a homotrimeric disulfide isomerase that plays a role in copper tolerance, which is a key virulence trait of this uropathogen.
Whitten, Andrew E. +9 more
core +1 more source
Reactive oxygen species, antioxidants and the regulation of plant development
The FEBS Journal, EarlyView.The regulation of axillary bud outgrowth by the interplay between phytohormone and redox signals. Axillary bud outgrowth is regulated by cellular energy status and the balance between phytohormones, notably abscisic acid (ABA) and gibberellic acid (GA).
Juwita R. Dewi +2 more
wiley +1 more source
Protein disulfide isomerase : function and mechanism in oxidative protein folding
, 2005 The formation of native intramolecular disulfide bonds is critical for the folding and stability of many secreted proteins. This process involves oxidation of protein thiols to form disulfide bonds as well as rearrangement of any non-native disulfide ...
Ruoyu Xiao (19525993)
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 Role of Oxidative Stress in Periodontitis
Journal of Periodontal Research, EarlyView.Oxidative stress is involved in multiple chemical reactions that take place in different intracellular organelles: mitochondria, rough endoplasmic reticulum, peroxisomes, autophagy, and aging, and can be influenced by exogenous factors: nutrition, physical activity, psychological status, environmental conditions, microbiome, and drugs.
Pedro Bullon +3 more
wiley +1 more source
, 2023 This data file contains images from Western blots and raw data used for the manuscript "Protein disulfide isomerase and extracellular adherence protein (Eap) cooperatively potentiate staphylococcal invasion into endothelial cells"
Muzaffar Hussain (255064) +10 more
core +1 more source
A substrate-driven allosteric switch that enhances PDI catalytic activity
Nature Communications, 2016 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