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Protein disulfide isomerases
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Protein disulfide isomerase (PDI) and PDI-like proteins contain thioredoxin domains that catalyze protein disulfide bond, inhibit aggregation of misfolded proteins, and function in isomerization during protein folding in endoplasmic reticulum and responses during abiotic stresses.Chinese cabbage is widely recognized as an economically important, nutritious vegetable, but its yield is severely hampered by various biotic and abiotic stresses. Because of, it is prime need to identify those genes whose are responsible for biotic and abiotic stress tolerance. PDI family genes are among of them.
20p
vilarryellison
29-10-2021
7
1
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Protein Disulfide Isomerases are thiol oxidoreductase chaperones from thioredoxin superfamily with crucial roles in endoplasmic reticulum proteostasis, implicated in many diseases. The family prototype PDIA1 is also involved in vascular redox cell signaling. PDIA1 is coded by the P4HB gene.
16p
vijeeni2711
30-06-2021
6
1
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Anterior gradient 2 (AGR2) is a protein disulfide isomerase-like protein widely expressed in many normal tissues as well as cancers. In our study, non-neoplastic bronchial epithelial cells as well as non-small cell lung cancer (NSCLC) cells express AGR2 protein.
9p
viamsterdam
18-09-2020
13
1
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The major wheat seed proteins are storage proteins that are synthesized in the rough endoplasmic reticulum (ER) of starchy endosperm cells. Many of these proteins have intra- and intermolecular disulfide bonds.
16p
viminato2711
22-05-2020
16
1
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In eukaryotes, classical protein disulfide isomerases (PDIs) facilitate the oxidative folding of nascent secretory proteins in the endoplasmic reticulum by catalyzing the formation, breakage, and rearrangement of disulfide bonds. Terrestrial plants encode six structurally distinct subfamilies of PDIs.
15p
vihashirama2711
21-05-2020
7
1
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The subject of this research was to investigate the level of expression of genes encoding protein disulfide isomerase (PDI) in cultivars and lines of wheat with different baking value of flour. PDI plays a key role in the formation of disulfide bonds in newly formed proteins.
13p
vishikamaru2711
29-04-2020
10
0
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The goal of our research was demonstrated that multiple molecules in microenvironments of the early osteoarthritis (OA) joint tissue may be actively responded to extracorporeal shockwave therapy (ESWT) treatment, which potentially regulated biological function of chondrocytes and synovial cells in early OA knee.
11p
vicaracas2711
27-11-2019
7
0
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A gene encoding β-mannanase from Aspergillus niger GIM3.452 was amplified and inserted into a pPIC9K vector. The resulting recombinant plasmid, pPIC9K-MAN, was transformed into Pichia pastoris GS115. One strain (GSKM-1) having the highest β-mannanase activity of 26.6 U/mL was obtained.
8p
vikimsa
22-02-2019
16
1
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Protein disulfide isomerase (PDI) and PDI-like genes encode key foldase enzymes that play an important role in disulfide bond formation, isomerization, and many other metabolic functions in plants. Our previous results indicate that the PDI-V expression is tissue-specific and that it is upregulated by powdery mildew and other abiotic stress treatments.
13p
caplock2711
21-02-2019
13
0
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The formation of disulfide bonds in the endoplasmic reti-culum requires protein disulfide isomerase (PDI) and endoplasmic reticulum oxidoreductin 1 (ERO1) that reoxi-dizes PDI. We report here that the expression of the rat, mouse andhumanhomologues ofERO1-Likeproteinabut not of the isoform ERO1-Lbare stimulated by hypoxia in rats vivo and in rat, mouse and human cell cultures.
8p
fptmusic
16-04-2013
56
2
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Protein disulfide oxidoreductases are ubiquitous redox enzymes that catalyse dithiol–disulfide exchange reactions with a CXXC sequence motif at their active site. Adisulfide oxidoreductase, a highly thermostable protein, was isolated from Pyrococcus furiosus(PfPDO), which is characterized by two redox sites (CXXC) and an unusual molecularmass. Its 3D structure at high resolution suggests that it may be related to the multidomain protein disulfide-isomerase (PDI), which is currently known only in eukaryotes....
12p
dell39
03-04-2013
34
2
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Protein disulfide isomerase family proteins are known to play important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disulfide isomerase family genes from soybean leaf (Glycine maxL. Merrill cv. Jack) mRNA by RT-PCR using forward and reverse primers designed from the expressed sequence tag clone sequences.
17p
galaxyss3
21-03-2013
49
3
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Protein disulfide isomerase family proteins play important roles in the fold-ing of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum. In this study, we cloned two similar protein disul-fide isomerase family genes from soybean leaf (Glycine maxL. Merrill. cv Jack). The cDNAs encode proteins of 525 and 551 amino acids, named GmPDIL-1 and GmPDIL-2, respectively.
15p
media19
06-03-2013
31
3
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Adhesive properties of endothelial cells are influenced by the thioldisulfide balance. However, the molecular mechanism of this effect is unclear, although recent observations indicate that integrin receptors may be direct targets for redox modulation. The purpose of this study was to examine whether protein disulfide isomerase (PDI) is directly involved in this pro-cess.
11p
media19
06-03-2013
56
1
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The protein disulfide isomerase is known to play important roles in the folding of nascent polypeptides and in the formation of disulfide bonds in the endoplasmic reticulum (ER). In this study, we cloned a gene of a novel protein disulfide isomerase family from soybean leaf (Glycine maxL. Mer-rill. cv Jack) mRNA.
12p
media19
05-03-2013
37
2
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Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role.
12p
media19
04-03-2013
25
1
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The oxidative folding of disulfide-rich conotoxins is essential for their biological functions.In vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase. To elucidate the physiologic roles of pro-tein disulfide isomerase in the folding of conotoxins, we have cloned a novel full-length protein disulfide isomerase from Conus marmoreus.
10p
media19
04-03-2013
45
2
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Protein disulfide isomerase is the most abundant and best studied of the disulfide isomerases that catalyze disulfide bond formation in the endoplas-mic reticulum, yet the specifics of how it binds substrate have been elusive. Protein disulfide isomerase is composed of four thioredoxin-like domains (abb¢a¢).
10p
vinaphone15
27-02-2013
32
2
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Protein disulfide isomerase (PDI) and other PDI family proteins are mem-bers of the thioredoxin superfamily and are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum (ER). The exact functions of PDI family proteins in plants remain unknown.
12p
vinaphone15
25-02-2013
35
2
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5¢-Deoxy-5¢-methylthioadenosine phosphorylase II fromSulfolobus solfatari-cus (SsMTAPII) and purine nucleoside phosphorylase from Pyrococcus furiosus (PfPNP) are hyperthermophilic purine nucleoside phosphorylases stabilized by intrasubunit disulfide bonds. In their C-terminus, both enzymes harbour a CXC motif analogous to the CXXC motif present at the active site of eukaryotic protein disulfide isomerase.
7p
viettel02
20-02-2013
34
2
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