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
The nematode cuticle is an extremely flexible and resilient exoskeleton that permits locomotion via attachment to muscle, confers environmental protection and allows growth by molting.
Johnstone, I. J., Page, A. P.
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Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State [PDF]
The mitochondrial thioredoxin system (NADPH, thioredoxin reductase, thioredoxin) is a major redox regulator. Here we have investigated the redox correlation between this system and the mitochondrial enzyme cyclophilin D.
Bindoli, Alberto+7 more
core +1 more source
The PSI domain of the MET oncogene encodes a functional disulfide isomerase essential for the maturation of the receptor precursor [PDF]
The tyrosine kinase receptor encoded by the MET oncogene has been extensively studied. Surprisingly, one extracellular domain, PSI, evolutionary conserved between plexins, semaphorins, and integrins, has no established function.
Altintas, Dogus Murat+16 more
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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
Generation of a Highly Active Folding Enzyme by Combining a Parvulin-Type Prolyl Isomerase from SurA with an Unrelated Chaperone Domain [PDF]
Parvulins are small prolyl isomerases and serve as catalytic domains of folding enzymes. SurA (survival protein A) from the periplasm of Escherichia coli consists of an inactive (Par1) and an active (Par2) parvulin domain as well as a chaperone domain ...
Geitner, Anne-Juliane+3 more
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Engineered Pathways for Correct Disulfide Bond Oxidation [PDF]
Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking protein disulfide isomerases (PDIs) can use alternative mechanisms for correct disulfide bond formation.
Bardwell, James C. A., Ren, Guoping
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Introduction to protein folding for physicists [PDF]
The prediction of the three-dimensional native structure of proteins from the knowledge of their amino acid sequence, known as the protein folding problem, is one of the most important yet unsolved issues of modern science.
Abagyan R. A.+21 more
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Anterior gradient protein 2 promotes survival, migration and invasion of papillary thyroid carcinoma cells [PDF]
Through a transcriptome microarray analysis, we have isolated Anterior gradient protein 2 (AGR2) as a gene up-regulated in papillary thyroid carcinoma (PTC).
Chiappetta, G+11 more
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The salivary sheath protein myosin from SBPH is critical for the formation of the salivary sheath and feeding. However, myosin functions as a HAMP and triggered plant BAK1‐mediated PTI responses, which include the activation of calcium signaling pathways, MAPK phosphorylation, ROS bursts, and cell death, thereby triggering JA pathway.
Liangxuan Qi+12 more
wiley +1 more source