Results 11 to 20 of about 6,745 (114)

High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility [PDF]

open access: yes, 2013
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 cuticle [PDF]

open access: yes, 2007
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.
core   +1 more source

Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State [PDF]

open access: yes, 2016
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]

open access: yes, 2022
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
core   +2 more sources

Folding of small disulfide-rich proteins : clarifying the puzzle [PDF]

open access: yes, 2006
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]

open access: yes, 2013
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
core   +1 more source

Engineered Pathways for Correct Disulfide Bond Oxidation [PDF]

open access: yes, 2011
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
core   +2 more sources

Introduction to protein folding for physicists [PDF]

open access: yes, 2007
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
core   +3 more sources

Anterior gradient protein 2 promotes survival, migration and invasion of papillary thyroid carcinoma cells [PDF]

open access: yes, 2014
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
core   +1 more source

An Insect Salivary Sheath Protein Triggers Plant Resistance to Insects and Pathogens as a Conserved HAMP

open access: yesAdvanced Science, EarlyView.
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

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