Results 101 to 110 of about 83,411 (273)

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

open access: yesCells, 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

von Willebrand factor is dimerized by protein disulfide isomerase.

open access: yesBlood, 2016
Multimeric von Willebrand factor (VWF) is essential for primary hemostasis. The biosynthesis of VWF high-molecular-weight multimers requires spatial separation of each step because of varying pH value requirements.
Svenja Lippok   +16 more
semanticscholar   +1 more source

Thiol-Disulfide Isomerization in Thrombospondin: Effects of Conformation and Protein Disulfide Isomerase [PDF]

open access: yesBlood, 1997
AbstractThiol-disulfide isomerization in thrombospondin may affect the function of this adhesive protein. Two assays were developed to analyze the determinants of thiol-disulfide exchange and to correlate this exchange with thrombospondin conformation.
Evelyn M. Huang   +3 more
openaire   +2 more sources

EFP1 is an ER stress-induced glycoprotein which interacts with the pro-apoptotic protein Par-4 [PDF]

open access: yes, 2009
We have isolated the rat ortholog of EFP1 (EF-hand binding protein 1) as a novel interaction partner of the pro-apoptotic protein Par-4 (prostate apoptosis response-4).
Appel, Sarah   +5 more
core   +1 more source

Expression of active human sialyltransferase ST6GalNAcI in Escherichia coli [PDF]

open access: yes, 2009
Georgios Skretas, Sean Carroll, and George Georgiou are with the Department of Chemical Engineering, University of Texas at Austin, Austin, TX 78712, USA -- George Georgiou is with the Department of Biomedical Engineering, University of Texas at Austin ...
Carroll, Sean   +5 more
core   +3 more sources

Crystal Structure of Imaginal Disc Growth Factor-2 [PDF]

open access: yes, 2002
Imaginal disc growth factor-2 (IDGF-2) is a member of a recently described family of Drosophila melanogaster-soluble polypeptide growth factors that promote cell proliferation in imaginal discs.
Llera, Andrea Sabina   +3 more
core   +1 more source

Distribution of protein disulfide isomerase in rat hepatocytes. [PDF]

open access: yesJournal of Histochemistry & Cytochemistry, 1988
We investigated quantitatively the distribution of protein disulfide isomerase (PDI) in rat hepatocytes by immunocytochemistry using a post-embedding protein A-gold technique. In hepatocytes, gold particles were mainly localized in the intracisternal space of the rough and smooth endoplasmic reticulum (ER) and nuclear envelopes.
Shigeo Akagi   +5 more
openaire   +3 more sources

Engineered Pathways for Correct Disulfide Bond Oxidation [PDF]

open access: yes, 2011
Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking protein disulfide isomerases (PDIs) can use alternative mechanisms for correct disulfide bond formation.
Bardwell, James C. A., Ren, Guoping
core   +2 more sources

Protein Disulfide Isomerase Modulates the Activation of Thyroid Hormone Receptors

open access: yesFrontiers in Endocrinology, 2019
Thyroid hormone receptors (TRs) are responsible for mediating thyroid hormone (T3 and T4) actions at a cellular level. They belong to the nuclear receptor (NR) superfamily and execute their main functions inside the cell nuclei as hormone-regulated ...
Jessica L. O. Campos   +17 more
doaj   +1 more source

Kinetic-based trapping by intervening sequence variants of the active sites of protein-disulfide isomerase identifies platelet protein substrates

open access: yesJournal of Biological Chemistry, 2017
Thiol isomerases such as protein-disulfide isomerase (PDI) direct disulfide rearrangements required for proper folding of nascent proteins synthesized in the endoplasmic reticulum.
Jack D. Stopa   +4 more
semanticscholar   +1 more source

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