Results 51 to 60 of about 83,411 (273)
Influence of the Season and Region Factor on Phosphoproteome of Stallion Epididymal Sperm
Epididymal maturation can be defined as a scope of changes occurring during epididymal transit that prepare spermatozoa to undergo capacitation. One of the most common post-translational modifications involved in the sperm maturation process and their ...
Katarzyna Dyrda+3 more
doaj +1 more source
Protein disulfide isomerase as an antithrombotic target [PDF]
Protein disulfide isomerase (PDI) is a ubiquitously expressed oxidoreductase required for proper protein folding. It is highly concentrated in the endoplasmic reticulum, but can also be released into the extracellular environment. Several in vivo thrombosis models have demonstrated that vascular PDI secreted by platelets and endothelial cells is ...
openaire +3 more sources
High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility [PDF]
ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted to consist of two thioredoxinfold domains homologous with the non-catalytic b and b domains of ...
A. Katrine Wallis+52 more
core +4 more sources
Soluble expression of human leukemia inhibitory factor with protein disulfide isomerase in Escherichia coli and its simple purification. [PDF]
Human leukemia inhibitory factor (hLIF) is a multifunctional cytokine that is essential for maintaining the pluripotency of embryonic stem cells. hLIF may be also be useful in aiding fertility through its effects on increasing the implantation rate of ...
Jung-A Song+12 more
doaj +1 more source
Background: Platelet-neutrophil interactions contribute to vascular occlusion and tissue damage in thromboinflammatory disease. Platelet glycoprotein Ib&agr; (GPIb&agr;), a key receptor for the cell-cell interaction, is believed to be constitutively ...
Jing Li+11 more
semanticscholar +1 more source
Folding of small disulfide-rich proteins : clarifying the puzzle [PDF]
Premi a l'excel·lència investigadora. Àmbit de les Ciències Experimentals. 2008The process by which small proteins fold to their native conformations has been intensively studied over the last few decades.
Apuy+73 more
core +2 more sources
Oxidative protein folding is a biological process to obtain a native conformation of a protein through disulfide-bond formation between cysteine residues.
Shunsuke Okada+3 more
doaj +1 more source
N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
Fungal pathogenesis depends on accurate secretion and location of virulence factors which drive host colonization. Protein glycosylation is a common posttranslational modification of cell wall components and other secreted factors, typically required for
Miriam Marín-Menguiano+4 more
semanticscholar +1 more source
Protein disulfide isomerases – a way to tackle malaria
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
The role and mechanism of TXNDC5 in diseases
Thioredoxin domain-containing protein 5 (TXNDC5) is a member of the protein disulfide isomerase (PDI) family. It can promote the formation and rearrangement of disulfide bonds, ensuring proper protein folding. TXNDC5 has three Trx-like domains, which can
Xueling Wang, Haoran Li, Xiaotian Chang
doaj +1 more source