Results 1 to 10 of about 21,311 (187)

The role and mechanism of TXNDC5 in disease progression

Frontiers in Immunology
Thioredoxin domain containing protein-5 (TXNDC5), also known as endothelial protein-disulfide isomerase (Endo-PDI), is confined to the endoplasmic reticulum through the structural endoplasmic reticulum retention signal (KDEL), is a member of the PDI ...
Mingxia Jiao, Mingxia Jiao, Yeyong Zhang, Xie Song, Xie Song, Bing Xu, Bing Xu   +6 more
doaj   +1 more source

Distinct roles and actions of protein disulfide isomerase family enzymes in catalysis of nascent-chain disulfide bond formation

iScience, 2021
Summary: The mammalian endoplasmic reticulum (ER) harbors more than 20 members of the protein disulfide isomerase (PDI) family that act to maintain proteostasis.
Chihiro Hirayama, Kodai Machida, Kentaro Noi, Tadayoshi Murakawa, Masaki Okumura, Teru Ogura, Hiroaki Imataka, Kenji Inaba   +7 more
doaj   +1 more source

Protein Disulfide Isomerase A4 Is Involved in Genome Uncoating during Human Astrovirus Cell Entry

Viruses, 2020
Although human astroviruses (HAstVs) are important agents of gastroenteritis in young children, the studies aimed at characterizing their biology have been limited, in particular regarding their cell entry process. It has been shown that HAstV serotype 8
Nayeli Aguilar-Hernández, Lena Meyer, Susana López, Rebecca M. DuBois, Carlos F. Arias   +4 more
doaj   +1 more source

Geniposide Balances the Redox Signaling to Mediate Glucose-Stimulated Insulin Secretion in Pancreatic β-Cells

Diabetes, Metabolic Syndrome and Obesity, 2020
Chunyan Liu, Yanan Hao, Fei Yin, Jianhui Liu Chongqing Key Laboratory of Medicinal Chemistry & Molecular Pharmacology, Chongqing University of Technology, Chongqing 400054, People’s Republic of ChinaCorrespondence: Jianhui Liu; Fei YinChongqing
Liu C, Hao Y, Yin F, Liu J
doaj  

Expression of Functional Human Sialyltransferases ST3Gal1 and ST6Gal1 in Escherichia coli.

PLoS ONE, 2016
Sialyltransferases (STs) are disulfide-containing, type II transmembrane glycoproteins that catalyze the transfer of sialic acid to proteins and lipids and participate in the synthesis of the core structure oligosaccharides of human milk.
Maria Elena Ortiz-Soto, Jürgen Seibel
doaj   +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

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

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

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

Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast

Scientific Reports, 2023
Oxidative protein folding in the endoplasmic reticulum (ER) is driven mainly by protein disulfide isomerase PDI and oxidoreductin Ero1. Their activity is tightly regulated and interconnected with the unfolded protein response (UPR).
Arianna Palma, Lukas A. Rettenbacher, Antti Moilanen, Mirva Saaranen, Christian Pacheco-Martinez, Brigitte Gasser, Lloyd Ruddock   +6 more
doaj   +1 more source