Results 101 to 110 of about 97,846 (317)

Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated [PDF]

, 2010
The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds ...
Appenzeller-Herzog, Christian, Chin, King-Tung, Ellgaard, Lars, Riemer, Jan, Ron, David, Spiess, Martin, Zito, Ester   +6 more
core   +3 more sources

Proteome Analysis of Corynebacterium diphtheriae–Macrophage Interaction

PROTEOMICS, EarlyView.
ABSTRACT Contact of Corynebacterium diphtheriae with macrophages induces adaptations on both bacterial and cellular sides. The study presented here was aiming to shed light on the simultaneous intracellular adaptation of the bacteria and changes in the proteome of the phagocytes in response to the internalization of C. diphtheriae.
Luca Musella, Jens Möller, Christopher Lischer, Julio Vera‐Gonzalez, Jörg Hofmann, Lisa Ott, Andreas Burkovski   +6 more
wiley   +1 more source

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

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

Biochimica et Biophysica Acta - Proteins and Proteomics, 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.
R. Freedman, Jasmine L Desmond, Lee J. Byrne, J. W. Heal, Mark J. Howard, N. Sanghera, Kelly L. Walker, A. K. Wallis, S. Wells, A. Richard, Williamson, R. A. Römer   +11 more
semanticscholar   +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

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

Inhibition of thiol isomerase activity diminishes endothelial activation of plasminogen, but not of protein C [PDF]

, 2015
Highlights •A range of thiol isomerase enzymes were expressed by HMEC-1 endothelial cells. •Inhibition of thiol isomerases reduced plasminogen activation on HMEC-1 cells.
Gordge, M.P., Gordge, M.P., Kamaludin, N., Kamaludin, N., Shah, C.M., Shah, C.M., Smith, C.L., Smith, C.L.   +7 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