Results 91 to 100 of about 3,285 (194)

Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies [PDF]

, 2012
The immunoglobulin (Ig) protein domain is widespread in nature having a well-recognized role in proteins of the immune system. In this review, we describe the proteins containing Ig-like domains in Escherichia coli and entero-bacteria, reporting their ...
Bluhm, Hendrik, Dickel, Christian, Foletti, Sandra, Umansky, Vladimir   +3 more
core   +2 more sources

Comparative Analysis of Heat Exposure‐Induced Molecular Changes in Two Turtle Species with Contrasting Thermal Adaptations

Integrative Zoology, EarlyView.
Protein processing in the endoplasmic reticulum is highlighted in response to heat stress in Platysternon megacephalum. Under heat stress, the up‐regulation of genes such as CHOP in protein processing in the endoplasmic reticulum pathway, along with the suppression of energy and lipid metabolism and the up‐regulation of JARID2 expression, leads to ...
Jian Hong, Yangchun Gao, Jiaxuan Li, Yan Ge, Yufeng Wei, Youqiang Yin, Qianru Liang, Shiping Gong   +7 more
wiley   +1 more source

ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor [PDF]

, 2013
ERdj5 is a member of the protein disulfide isomerase family of proteins localized to the endoplasmic reticulum (ER) of mammalian cells. To date, only a limited number of substrates for ERdj5 are known.
Braakman, Ineke, Bulleid, Neil John, Oka, Ojore Benedict Valentine, Pringle, Marie Anne, Schopp, Isabel Myriam   +4 more
core   +1 more source

DsbG, a Protein Disulfide Isomerase with Chaperone Activity [PDF]

Journal of Biological Chemistry, 2000
DsbG, a protein disulfide isomerase present in the periplasm of Escherichia coli, is shown to function as a molecular chaperone. Stoichiometric amounts of DsbG are sufficient to prevent the thermal aggregation of two classical chaperone substrate proteins, citrate synthase and luciferase.
F, Shao, M W, Bader, U, Jakob, J C, Bardwell   +3 more
openaire   +2 more sources

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

Oxidative Stress in Fungi: Its Function in Signal Transduction, Interaction with Plant Hosts, and Lignocellulose Degradation

Biomolecules, 2015
In this review article, we want to present an overview of oxidative stress in fungal cells in relation to signal transduction, interaction of fungi with plant hosts, and lignocellulose degradation.
Michael Breitenbach, Manuela Weber, Mark Rinnerthaler, Thomas Karl, Lore Breitenbach-Koller   +4 more
doaj   +1 more source

Compact Conformations of Human Protein Disulfide Isomerase

PLoS ONE, 2014
Protein disulfide isomerase (PDI) composed of four thioredoxin-like domains a, b, b', and a', is a key enzyme catalyzing oxidative protein folding in the endoplasmic reticulum. Large scale molecular dynamics simulations starting from the crystal structures of human PDI (hPDI) in the oxidized and reduced states were performed.
Shang Yang, Xi Wang, Lei Cui, Xiang Ding, Lili Niu, Fuquan Yang, Chao Wang, Chih-Chen Wang, Jizhong Lou   +8 more
openaire   +4 more sources

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

Protein folding and conformational stress in microbial cells producing recombinant proteins : a host comparative overview [PDF]

, 2008
Different species of microorganisms including yeasts, filamentous fungi and bacteria have been used in the past 25 years for the controlled production of foreign proteins of scientific, pharmacological or industrial interest. A major obstacle for protein
Baumann, Kristin, Branduardi, Paola, Dragosits, Martin, Ferrer, Pau, Gasser, Brigitte, Giuliani, Maria, Lang, Christine, Mattanovich, Diethard, Parrilli, Ermenegilda, Porro, Danilo, Rinas, Ursula, Rodríguez-Carmona, Escarlata, Saloheimo, Markku, Tutino, Maria Luisa, Villaverde Corrales, Antonio   +14 more
core   +5 more sources

Conformational Resilience of Protein Disulfide Isomerase

The FASEB Journal, 2019
Protein disulfide isomerase (PDI) is a 57 kDa protein with both oxidoreductase and chaperone activities that is mainly localized to the endoplasmic reticulum. It is a U‐shaped protein with an abb'xa’ structural organization where the a and
Jessica Guyette, Baggio Evangelista, Suren A. Tatulian, Ken Teter   +3 more
openaire   +1 more source