Results 91 to 100 of about 41,132 (234)

Branched‐Chain Amino and Keto Acids Reduce Hepatocyte Lipid Droplet Size and Number via Distinct Proteomic Pathways

PROTEOMICS, EarlyView.
ABSTRACT Branched‐chain amino acids (BCAA) and their corresponding keto acids (BCKA) have been associated with changes in hepatic lipid metabolism and the resulting alterations in intracellular triglyceride concentrations. In this study, we utilized a previously established hepatocyte model to investigate the impact of BCAA and BCKA supplementation on ...
Jayasimha R. Daddam, Mounica Sura, Edward Kolodziej, Maria Gojcaj, Zheng Zhou   +4 more
wiley   +1 more source

The protein disulfide isomerase 1 of Phytophthora parasitica (PpPDI1) is associated with the haustoria-like structures and contributes to plant infection [PDF]

, 2015
The protein disulfide isomerase (PDI) is a ubiquitous and multifunction enzyme belonging to the thioredoxin (TRX) superfamily, which can reduce, oxidize, and catalyze dithiol-disulfide exchange reactions.
Biao Gu, Guiyan Huang, Meixiang Zhang, Qiang Zhang, Qinhu Wang, Weixing Shan, Yuling Meng   +6 more
core   +2 more sources

Targeting protein–protein interactions with reversible covalent modalities: Non‐cysteine chemistries

British Journal of Pharmacology, EarlyView.
Abstract Protein–protein interactions (PPIs) are central to diverse cellular functions, and represent a rapidly expanding class of therapeutic targets. Advancements in covalent drug design have enabled small‐molecule drugs to overcome challenges associated with engaging these targets, such as limited durations of action and difficult‐to‐drug (expansive,
Ruchira Basu, Steven Fletcher
wiley   +1 more source

Structure of the non-catalytic domain of the protein disulfide isomerase-related protein (PDIR) reveals function in protein binding.

PLoS ONE, 2013
Protein disulfide isomerases comprise a large family of enzymes responsible for catalyzing the proper oxidation and folding of newly synthesized proteins in the endoplasmic reticulum (ER). Protein disulfide isomerase-related (PDIR) protein (also known as
Roohi Vinaik, Guennadi Kozlov, Kalle Gehring   +2 more
doaj   +1 more source

Proteome Profiling of Breast Tumors by Gel Electrophoresis and Nanoscale Electrospray Ionization Mass Spectrometry [PDF]

, 2008
We have conducted proteome-wide analysis of fresh surgery specimens derived from breast cancer patients, using an approach that integrates size-based intact protein fractionation, nanoscale liquid separation of peptides, electrospray ion trap mass ...
Aebersold R., Boyle E. I., Chong P. K., Cottingham K., Cove D. H., Ezeh U. I., Foran E., Gygi S. P., Ioachim E., Jacobs J. M., Keller A., Laemmli U. K., Lapillonne A., Lin C. S., Liu H., Maclean B., Mathelin C., Metodiev M. V., old W. M., Patterson S. D., Pedrioli P. G., Rauch A., Schmidt A., Sealfon R. S., Seo J., Sheen-Cheen S. M., Silva J., Taylor M. R., Toi M., Wolters D. A., Zhang J.   +30 more
core   +1 more source

ER proteostasis meets mitochondrial function: contact sites as hubs of communication and therapeutic targets

The FEBS Journal, EarlyView.
Proteostasis ensures proper protein folding, modification, and degradation, while its impairment triggers ER stress. Chronic ER stress and maladaptive UPR via the CHOP–ERO1 axis remodel ERMCs, altering calcium signaling and mitochondrial metabolism.
Giorgia Maria Renna, Alessandro Cherubini, Ersilia Varone, Serena Germani, Alice Marrazza, Ester Zito   +5 more
wiley   +1 more source

Golgi-independent routes support protein disulfide isomerase externalization in vascular smooth muscle cells

Redox Biology, 2017
Extracellular pools of intracellular molecular chaperones are increasingly evident. The peri/epicellular(pec) pool of the endoplasmic reticulum redox chaperone protein disulfide isomerase-A1(PDI) is involved in thrombosis and vascular remodeling, while ...
Thaís L.S. Araujo, Carolina G. Fernandes, Francisco R.M. Laurindo   +2 more
doaj   +1 more source

Oxidative protein folding in the mitochondrial intermembrane space [PDF]

, 2010
Disulfide bond formation is a crucial step for oxidative folding and necessary for the acquisition of a protein's native conformation. Introduction of disulfide bonds is catalyzed in specialized subcellular compartments and requires the coordinated ...
Anfinsen CB, Dionisia P. Sideris, Giorda R, Kamitani S, Kostas Tokatlidis   +4 more
core   +1 more source

Selective Inhibition of Protein Disulfide Isomerase by Estrogens

Journal of Biological Chemistry, 1989
Protein disulfide isomerase (PDI) is a multifunctional microsomal enzyme that participates in the formation of protein disulfide bonds. PDI catalyzes the reduction of protein disulfide bonds in the presence of excess reduced glutathione and has been implicated in the reductive degradation of insulin; E.
J C, Tsibris, L T, Hunt, G, Ballejo, W C, Barker, L J, Toney, W N, Spellacy   +5 more
openaire   +2 more sources

Expression and Localization of Plant Protein Disulfide Isomerase [PDF]

Plant Physiology, 1993
A cDNA clone encoding a putative protein disulfide isomerase (PDI, EC 5.3.4.1) from alfalfa (Medicago sativa L.) was expressed in Escherichia coli cells, and an antiserum was raised against the expressed PDI-active protein. The antiserum recognized a protein of approximately 60 kD in extracts from alfalfa, soybean, and tobacco roots and stems.
B. S., Shorrosh, J., Subramaniam, K. R., Schubert, R. A., Dixon   +3 more
openaire   +2 more sources