Results 101 to 110 of about 41,132 (234)

The competitive interplay of 12‐oxophytodienoic acid (OPDA), protein thiols, and glutathione

The FEBS Journal, EarlyView.
12‐Oxophytodienoic acid (OPDA) is a phytohormone involved in plant growth and stress defense. Due to its cyclopentenone moiety, OPDA can form Michael adducts with thiol‐containing compounds such as glutathione and cysteine residues of proteins, resulting in alterations of the cellular redox regulatory network.
Madita Knieper, Ruben Schwarz, Lara Vogelsang, Jens Sproß, Armağan Kaya, Maike Bittmann, Harald Gröger, Andrea Viehhauser, Karl‐Josef Dietz   +8 more
wiley   +1 more source

Biogenesis of TNF‐α‐insights into proteostasis and inflammation

The FEBS Journal, EarlyView.
TNF‐α biogenesis, trafficking, and signalling are tightly and reciprocally coupled to cellular proteostasis systems, including ER chaperones and endoplasmic reticulum‐associated degradation. This bidirectional crosstalk determines whether TNF‐α responses are adaptive or proteotoxic.
Bailasan Haidar, Céline Philippe, Eric Chevet, Jiří Zahradník   +3 more
wiley   +1 more source

A substrate-driven allosteric switch that enhances PDI catalytic activity

Nature Communications, 2016
Protein Disulfide Isomerase (PDI) is a prothrombotic, multidomain enzyme with separate substrate binding and catalytic domains. Here, the authors identify a new class of compounds that target the PDI substrate binding site, inducing a conformational ...
Roelof H. Bekendam, Pavan K. Bendapudi, Lin Lin, Partha P. Nag, Jun Pu, Daniel R. Kennedy, Alexandra Feldenzer, Joyce Chiu, Kristina M. Cook, Bruce Furie, Mingdong Huang, Philip J. Hogg, Robert Flaumenhaft   +12 more
doaj   +1 more source

Cloning, expression, purification and characterization of a DsbA-like protein from Wolbachia pipientis [PDF]

, 2008
Wolbachia pipientis are obligate endosymbionts that infect a wide range of insect and other arthropod species. They act as reproductive parasites by manipulating the host reproduction machinery to enhance their own transmission. This unusual phenotype is
Alun Jones, Bardwell, Begoña Heras, Collet, Debarbieux, Edeling, Ellermeier, Ellman, Floate, Gautier Robin, Gordon J. King, Goulding, Gruber, Heras, Hillson, Holmgren, Iñaki Iturbe-Ormaetxe, Jennifer L. Martin, Jeyaprakash, Kadokura, Kelley, Mareike Kurz, Martin, Martin, McCarthy, Messens, Nakamoto, Nathan Cowieson, O’Neill, O’Neill, Patrick Frei, Raina, Riegler, Rietsch, Rudi Glockshuber, Russell Jarrott, Sambrook, Scott L. O’Neill, Studier, Taylor, Taylor, Werren, Wu, Yu   +43 more
core   +1 more source

Stability and Conformational Resilience of Protein Disulfide Isomerase

Biochemistry, 2019
Protein disulfide isomerase (PDI) is a redox-dependent protein with oxidoreductase and chaperone activities. It is a U-shaped protein with an abb'xa' structural organization in which the a and a' domains have CGHC active sites, the b and b' domains are involved with substrate binding, and x is a flexible linker. PDI exhibits substantial flexibility and
Jessica Guyette, Baggio Evangelista, Suren A. Tatulian, Ken Teter   +3 more
openaire   +3 more sources

From the Proteome to Therapeutics: A Multi‐Database Approach to Drug Discovery in Periodontitis—An Exploratory Pilot Study

Journal of Clinical Periodontology, EarlyView.
ABSTRACT Introduction This explanatory pilot study presents a workflow to identify approved drugs, which could be repurposed for periodontitis therapy using salivary proteomics combined with drug‐target database screening. Methods Proteomic analyses of saliva using LC–MS/MS were conducted in two independent settings: a cohort (sub‐study I, N = 187) and
Taisir Bozo, Annette Murr, Birte Holtfreter, Sebastian‐Edgar Baumeister, Peter Meisel, Uwe Völker, Werner Weitschies, Henry Völzke, Philipp Kanzow, Elke Hammer, Manuela Gesell Salazar, Thomas Kocher   +11 more
wiley   +1 more source

Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway

Cells, 2020
Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER).
Philip J. Robinson, Neil J. Bulleid
doaj   +1 more source

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

, 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, Alanen, Barak, Barbato, Brünger, Byrne, Cornilescu, Delaglio, Denisov, Ellgaard, Freedman, Guddat, Holm, Jacobs, Jansen, Jimenez-Roldan, Kemmink, Klappa, Kober, Koradi, Kozlov, Kozlov, Kozlov, Lappi, Laskowski, Laskowski, Li, Lipari, Lipari, Mark J. Howard, Michelle L. Rowe, Nader T. Amin, Neuhaus, Nguyen, Palmer, Piotto, Richard A. Williamson, Rieping, Robert B. Freedman, Rowe, States, Stephen A. Wells, Suhre, Tian, Wallis, Wang, Wang, Waters, Wells, Wells, Williamson, Wim, Wishart   +52 more
core   +5 more sources

The Role of Oxidative Stress in Periodontitis

Journal of Periodontal Research, EarlyView.
Oxidative stress is involved in multiple chemical reactions that take place in different intracellular organelles: mitochondria, rough endoplasmic reticulum, peroxisomes, autophagy, and aging, and can be influenced by exogenous factors: nutrition, physical activity, psychological status, environmental conditions, microbiome, and drugs.
Pedro Bullon, Francesca Giampieri, Beatriz Bullon, Maurizio Battino   +3 more
wiley   +1 more source

Intracellular trafficking, localization, and mobilization of platelet-borne thiol isomerases [PDF]

, 2016
OBJECTIVE: Thiol isomerases facilitate protein folding in the endoplasmic reticulum, and several of these enzymes, including protein disulfide isomerase and ERp57, are mobilized to the surface of activated platelets, where they influence platelet ...
Ali, Marfoua S., Crescente, Marilena, Falet, H., Gibbins, Jon M., Holbrook, Lisa M., Jones, Ian M., Kahr, W. H. A., Li, L., Lo, R. W., Loureiro, Silvia, Pluthero, F. G., Poole, A. W., Schenk, Michael P., Vaiyapuri, Sakthi, Walsh, T. G.   +14 more
core   +2 more sources