Results 11 to 20 of about 7,369 (220)

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

Arteriosclerosis, Thrombosis, and Vascular Biology, 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   +4 more sources

Atypical protein disulfide isomerases (PDI): Comparison of the molecular and catalytic properties of poplar PDI-A and PDI-M with PDI-L1A. [PDF]

PLoS ONE, 2017
Protein disulfide isomerases are overwhelmingly multi-modular redox catalysts able to perform the formation, reduction or isomerisation of disulfide bonds. We present here the biochemical characterization of three different poplar PDI isoforms.
Benjamin Selles, Flavien Zannini, Jérémy Couturier, Jean-Pierre Jacquot, Nicolas Rouhier   +4 more
doaj   +2 more sources

Recent advances in vascular thiol isomerases: insights into structures, functions in thrombosis and antithrombotic inhibitor development [PDF]

Thrombosis Journal
Vascular thiol isomerases (VTIs) encompass proteins such as protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERp5), ERp46, ERp57, ERp72, thioredoxin-related transmembrane protein 1 (TMX1), and TMX4, and play pivotal functions in ...
Longguang Jiang, Cai Yuan, Robert Flaumenhaft, Mingdong Huang   +3 more
doaj   +2 more sources

Functional Differences in Yeast Protein Disulfide Isomerases [PDF]

The Journal of Cell Biology, 2001
PDI1 is the essential gene encoding protein disulfide isomerase in yeast. The Saccharomyces cerevisiae genome, however, contains four other nonessential genes with homology to PDI1: MPD1, MPD2, EUG1, and EPS1. We have investigated the effects of simultaneous deletions of these genes. In several cases, we found that the ability of the PDI1 homologues to
P, Nørgaard, V, Westphal, C, Tachibana, L, Alsøe, B, Holst, J R, Winther   +5 more
openaire   +4 more sources

Thiol isomerase ERp18 enhances platelet activation and arterial thrombosis [PDF]

Research and Practice in Thrombosis and Haemostasis
Background: Thiol isomerases regulate the thiol-disulfide exchange of functional proteins in cells. Using genetically modified mouse models and inhibitors, we and others demonstrated that 7 thiol isomerases (ERp57, protein diisulfide isomerase, ERp72 ...
Chao He, Aizhen Yang, Keyu Lv, Yuxin Zhang, Zhenzhen Zhao, Yi Lu, Chao Fang, Yue Han, Depei Wu, Miao Jiang, Jingyu Zhang, Yi Wu   +11 more
doaj   +2 more sources

Structural, functional and proteomic changes of proteins during rice yellowing [PDF]

Food Chemistry: X
High temperature storage (40 °C, 60 % relative humidity, 6 months) induces rice yellowing and affects protein properties. Physiochemical analysis revealed increased disulfide bonds, particle size, and surface hydrophobicity in yellowed rice protein ...
Yuqian Liu, Yanan Qv, Jingyu Sun, Xiao Zheng, Victoria Anthony Uyanga, Yawen Wang, Yu Cui, Caiyun Tang, Jinguang Liu, Yilun Chen   +9 more
doaj   +2 more sources

Unveiling the thioredoxin fold: a systematic review and bioinformatic analysis of protein disulfide isomerase and Dsb family proteins [PDF]

Frontiers in Bioinformatics
IntroductionProtein Disulfide Isomerases (PDIs) and bacterial Dsb proteins are key members of the thioredoxin-fold superfamily, essential for oxidative protein folding in eukaryotic and prokaryotic systems, respectively.
Daniel Cuevas Ortiz, Karen Werner, Maria Fernanda Frias Mayo, Pablo A. Cárdenas Arredondo, Gabriela F. García Manzano, Cristina Revilla-Monsalve, Héctor Retana, Nelly F. Altamirano-Bustamante, Myriam M. Altamirano-Bustamante   +8 more
doaj   +2 more sources

Substrate recognition by the protein disulfide isomerases [PDF]

The FEBS Journal, 2007
Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role.
Hatahet Feras, Ruddock Lloyd
openaire   +4 more sources

Protein disulfide isomerase A6 (PDIA6) is essential for acrosome biogenesis and male fertility in mice [PDF]

Cell Communication and Signaling
Background The family of protein disulfide isomerases (PDIs) are thiol oxidoreductases located predominantly in the endoplasmic reticulum that catalyze thiol-disulfide exchange for normal protein folding.
Xiaofeng Yan, Yaqiong Zhang, Aizhen Yang, Yufeng Hou, Raymond B. Birge, Jinxing Lv, Yi Wu   +6 more
doaj   +2 more sources

Decoding PDI diversity: Insights into structure, domains, and functionality in sorghum [PDF]

Computational and Structural Biotechnology Journal
Proteins play indispensable roles in cellular function, acting as both structural components and catalysts for essential biological processes. Their proper folding into three-dimensional structures is critical for functionality. To ensure correct folding,
Carla F. López-Gómez, Marc T. Morris, Karen Massel, Millicent Smith, Peter Crisp, Gerhard Schenk, Ian D. Godwin   +6 more
doaj   +2 more sources