Results 31 to 40 of about 3,418,558 (223)

Prolyl 4-hydroxlase activity is essential for development and cuticle formation in the human infective parasitic nematode Brugia malayi [PDF]

, 2013
Collagen prolyl 4-hydroxylases (C-P4H) are required for formation of extracellular matrices in higher eukaryotes. These enzymes convert proline residues within the repeat regions of collagen polypeptides to 4-hydroxyproline, a modification essential for ...
Page, A., Winter, A., McCormack, G., Myllyharju, J.   +3 more
core   +1 more source

Immunoproteomic to identify antigens in the intestinal mucosa of Crohn's disease patients. [PDF]

PLoS ONE, 2013
Incidences of Crohn disease (CD) have increased significantly in the last decade. Immunoproteomics are a promising method to identify biomarkers of different diseases. In the present study, we used immunoproteomics to study proteins of intestinal mucosal
Zheng Zhou, Haiyan Liu, Guosheng Gu, Gefei Wang, Wenyong Wu, Changle Zhang, Jianan Ren   +6 more
doaj   +1 more source

Redox Control of Exofacial Protein Thiols/Disulfides by Protein Disulfide Isomerase [PDF]

Journal of Biological Chemistry, 1999
Protein disulfide isomerase (PDI) facilitates proper folding and disulfide bonding of nascent proteins in the endoplasmic reticulum and is secreted by cells and associates with the cell surface. We examined the consequence of over- or underexpression of PDI in HT1080 fibrosarcoma cells for the redox state of cell-surface protein thiols/disulfides ...
X M, Jiang, M, Fitzgerald, C M, Grant, P J, Hogg   +3 more
openaire   +2 more sources

‘Something in the way she moves’ : the functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI) [PDF]

, 2017
Protein disulfide isomerase (PDI) has diverse functions in the endoplasmic reticulum as catalyst of redox transfer, disulfide isomerization and oxidative protein folding, as molecular chaperone and in multi-subunit complexes.
Sanghera, Narinder, Römer, Rudolf A., Howard, M., Williamson, Richard A., Howard, Mark J., Wallis, A. Katrine, Jasmine L. Desmond, Walker, Kelly L., Wallis, A., Heal, Jack W., Byrne, Lee J., Richard A. Williamson, Heal, J., Narinder Sanghera, Desmond, J., Wells, S., Rudolf A. Römer, Byrne, L., Freedman, R., Walker, K., Mark J. Howard, Wells, Stephen A., Lee J. Byrne, Freedman, R. B., Stephen A. Wells, A. Katrine Wallis, Romer, R., Desmond, Jasmine L., Kelly L. Walker, Williamson, R., Freedman, Robert B., Jack W. Heal, Sanghera, N., Robert B. Freedman   +33 more
core   +1 more source

Antiretroviral effect of 4-thio-uridylate against human immunodeficiency virus type 1 [PDF]

, 2012
Antiretroviral effect of thiolated nucleotide 4-thio-uridylate (S4UMP, designated as UD29) against human immunodeficiency virus type 1 (HIV-1) have been quantitatively determined in cell-based viral infectivity assays. In syntitium inhibition assay on MT-
Ongrádi, József, Nagy, Károly, Joseph Ongrádi, Kanizsai, Szilvia, Ghidán, Ágoston, Szilvia Kanizsai, Ágoston Ghidán, Károly Nagy, Ongrádi, Joseph   +8 more
core   +3 more sources

Participation of the endoplasmic reticulum protein chaperone thio-oxidoreductase in gonadotropin-releasing hormone receptor expression at the plasma membrane

Brazilian Journal of Medical and Biological Research, 2009
Chaperone members of the protein disulfide isomerase family can catalyze the thiol-disulfide exchange reaction with pairs of cysteines. There are 14 protein disulfide isomerase family members, but the ability to catalyze a thiol disulfide exchange ...
W. Lucca-Junior, J.A. Janovick, P.M. Conn   +2 more
doaj   +1 more source

Protein Disulfide Isomerase and Host-Pathogen Interaction

The Scientific World Journal, 2011
Reactive oxygen species (ROS) production by immunological cells is known to cause damage to pathogens. Increasing evidence accumulated in the last decade has shown, however, that ROS (and redox signals) functionally regulate different cellular pathways ...
Beatriz S. Stolf, Ioannis Smyrnias, Lucia R. Lopes, Alcione Vendramin, Hiro Goto, Francisco R. M. Laurindo, Ajay M. Shah, Celio X. C. Santos   +7 more
doaj   +1 more source

Murine tissue factor coagulant activity is critically dependent on the presence of an intact allosteric disulfide

Haematologica, 2013
Tissue factor activation (decryption) has been proposed to be dependent on the cysteine 186-cysteine 209 allosteric disulfide in the tissue factor extracellular domain.
Lisa G. van den Hengel, Susanne Osanto, Pieter H. Reitsma, Henri H. Versteeg   +3 more
doaj   +1 more source

Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization. [PDF]

PLoS ONE, 2013
BACKGROUND: Tau protein is implicated in the pathogenesis of neurodegenerative disorders such as tauopathies including Alzheimer disease, and Tau fibrillization is thought to be related to neuronal toxicity. Physiological inhibitors of Tau fibrillization
Li-Rong Xu, Xiao-Ling Liu, Jie Chen, Yi Liang   +3 more
doaj   +1 more source

CHAPTER 1.1. Disulfide Bonds in Protein Folding and Stability [PDF]

, 2018
Disulfide bonds are unique among post-translational modifications, as they add covalent crosslinks to the polypeptide chain. Accordingly, they can exert pronounced effects on protein folding and stability. This is of particular importance for secreted or
Sub Cellular Protein Chemistry, Hendershot, Linda M., Feige, Matthias J., Ineke Braakman, Matthias J. Feige, Braakman, Ineke, Cellular Protein Chemistry, Linda M. Hendershot   +7 more
core   +1 more source