Results 81 to 90 of about 83,408 (297)
Phytophthora capsici effector PcRD18 targets tomato GSNOR to disrupt NO homeostasis, promoting S‐nitrosylation of immune proteins like RBOHD. This suppresses ROS bursts and promotes pathogen infection. Mutation of the PcRD18‐binding sites of GSNOR avoids pathogen manipulation and offers a strategy to enhance crop resistance. Abstract Nitric oxide (NO),
Tingting Li+8 more
wiley +1 more source
Expression and Localization of Plant Protein Disulfide Isomerase [PDF]
A cDNA clone encoding a putative protein disulfide isomerase (PDI, EC 5.3.4.1) from alfalfa (Medicago sativa L.) was expressed in Escherichia coli cells, and an antiserum was raised against the expressed PDI-active protein. The antiserum recognized a protein of approximately 60 kD in extracts from alfalfa, soybean, and tobacco roots and stems.
Basil S. Shorrosh+3 more
openaire +3 more sources
Protein Profiling of Arabidopsis Roots Treated With Humic Substances: Insights Into the Metabolic and Interactome Networks [PDF]
Background and Aim: Humic substances (HSs) influence the chemical and physical properties of the soil, and are also known to affect plant physiology and nutrient uptake.
Antonio Masi+9 more
core +4 more sources
Essentials Nitric oxide synthesis controls protein disulfide isomerase (PDI) function. Nitric oxide (NO) modulation of PDI controls endothelial thrombogenicity. S‐nitrosylated PDI inhibits platelet function and thrombosis. Nitric oxide maintains vascular
Roelof H. Bekendam+17 more
semanticscholar +1 more source
This study reveals a new mechanism by which PDIA3P1 regulates the progression of esophageal squamous cell carcinoma (ESCC). PDIA3P1 upregulates the expression of GLUT1 and HK2, promoting glycolysis and lactate production. Lactate upregulates the lactylation level of histone H4K8 and activates the transcription of target gene BMP7, ultimately ...
Tao Huang+13 more
wiley +1 more source
Stability and Conformational Resilience of Protein Disulfide Isomerase
Protein disulfide isomerase (PDI) is a redox-dependent protein with oxidoreductase and chaperone activities. It is a U-shaped protein with an abb'xa' structural organization in which the a and a' domains have CGHC active sites, the b and b' domains are involved with substrate binding, and x is a flexible linker. PDI exhibits substantial flexibility and
Jessica Guyette+3 more
openaire +3 more sources
Characterization of the S-Denitrosation Activity of Protein Disulfide Isomerase [PDF]
S-nitrosoglutathione (GSNO) denitrosation activity of recombinant human protein disulfide isomerase (PDI) has been kinetically characterized by monitoring the loss of the S-NO absorbance, using a NO electrode, and with the aid of the fluorogenic NOx probe 2,3-diaminonaphthalene.
Arun Raturi+2 more
openaire +3 more sources
Arginyltransferase, Its Specificity, Putative Substrates, Bidirectional Promoter, and Splicing-derived Isoforms [PDF]
Substrates of the N-end rule pathway include proteins with destabilizing N-terminal residues. Three of them, Asp, Glu, and (oxidized) Cys, function through their conjugation to Arg, one of destabilizing N-terminal residues that are recognized directly by
Brower, Christopher S.+7 more
core +2 more sources
Cytosolic thioredoxin reductase 1 is required for correct disulfide formation in the ER [PDF]
Folding of proteins entering the secretory pathway in mammalian cells frequently requires the insertion of disulfide bonds. Disulfide insertion can result in covalent linkages found in the native structure as well as those that are not, so‐called non ...
Elias SJ Arnér+8 more
core +2 more sources
Distribution of protein disulfide isomerase in rat hepatocytes. [PDF]
We investigated quantitatively the distribution of protein disulfide isomerase (PDI) in rat hepatocytes by immunocytochemistry using a post-embedding protein A-gold technique. In hepatocytes, gold particles were mainly localized in the intracisternal space of the rough and smooth endoplasmic reticulum (ER) and nuclear envelopes.
Shigeo Akagi+5 more
openaire +3 more sources