Results 91 to 100 of about 83,411 (273)

Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44. [PDF]

, 2008
Sulfatase modifying factor 1 (SUMF1) encodes for the formylglicine generating enzyme, which activates sulfatases by modifying a key cysteine residue within their catalytic domains. SUMF1 is mutated in patients affected by multiple sulfatase deficiency, a
Annunziata F., BALLABIO, ANDREA, Cosma M. P., Cozzolino M., FRALDI, ALESSANDRO, Lombardi A., MONTI, MARIA, PUCCI, PIETRO, Sitia R., Spampanato C., Zito E.   +10 more
core   +1 more source

Novel Protein Disulfide Isomerase Inhibitor with Anticancer Activity in Multiple Myeloma.

Cancer Research, 2016
Multiple myeloma cells secrete more disulfide bond-rich proteins than any other mammalian cell. Thus, inhibition of protein disulfide isomerases (PDI) required for protein folding in the endoplasmic reticulum (ER) should increase ER stress beyond repair ...
S. Vatolin, James G. Phillips, B. Jha, Shravya Govindgari, Jennifer Hu, D. Grabowski, Yvonne Parker, D. Lindner, F. Zhong, C. Distelhorst, Mitchell R. Smith, C. Cotta, Yan Xu, S. Chilakala, Rebecca R Kuang, Samantha Tall, F. Reu   +16 more
semanticscholar   +1 more source

Expression and Localization of Plant Protein Disulfide Isomerase [PDF]

Plant Physiology, 1993
A cDNA clone encoding a putative protein disulfide isomerase (PDI, EC 5.3.4.1) from alfalfa (Medicago sativa L.) was expressed in Escherichia coli cells, and an antiserum was raised against the expressed PDI-active protein. The antiserum recognized a protein of approximately 60 kD in extracts from alfalfa, soybean, and tobacco roots and stems.
Basil S. Shorrosh, Richard A. Dixon, J. Subramaniam, Karel R. Schubert   +3 more
openaire   +3 more sources

Pancreas specific protein disulfide isomerase, PDIp, is in transient contact with secretory proteins during late stages of translocation [PDF]

, 1997
Protein disulfide isomerase (PDI) and an additional lumenal protein of dog pancreas microsomes were previously observed to be in transient contact with secretory proteins during late stages of their co- or posttranslational translocation into these ...
Bacher, Connolly, Connolly, Desilva, Dierks, Görlich, Görlich, Hartmann, High, High, Holmgren, Klappa, Klappa, Krieg, Krieg, Kurzchalia, LaMantia, Miller, Nicchitta, Noiva, Oliver, Puig, Thrift, Van, Wiech, Wiedmann   +25 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

Characterization of the S-Denitrosation Activity of Protein Disulfide Isomerase [PDF]

Journal of Biological Chemistry, 2005
S-nitrosoglutathione (GSNO) denitrosation activity of recombinant human protein disulfide isomerase (PDI) has been kinetically characterized by monitoring the loss of the S-NO absorbance, using a NO electrode, and with the aid of the fluorogenic NOx probe 2,3-diaminonaphthalene.
Arun Raturi, Bulent Mutus, Inga Sliskovic   +2 more
openaire   +3 more sources

A Protein Disulfide Isomerase Controls Neuronal Migration through Regulation of Wnt Secretion

Cell Reports, 2019
Summary: Appropriate Wnt morphogen secretion is required to control animal development and homeostasis. Although correct Wnt globular structure is essential for secretion, proteins that directly mediate Wnt folding and maturation remain uncharacterized ...
Nanna Torpe, Sandeep Gopal, Oguzhan Baltaci, Lorenzo Rella, Ava Handley, Hendrik C. Korswagen, Roger Pocock   +6 more
doaj  

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

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

Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides

Proceedings of the National Academy of Sciences of the United States of America, 2016
Significance The majority of secreted proteins contain disulfide bonds that provide structural stability in the extracellular environment. The formation of correct disulfide bonds is assisted by the enzyme protein disulfide isomerase (PDI). Most secreted
Helena Safavi-Hemami, Qing Li, R. L. Jackson, A. Song, Wouter Boomsma, P. Bandyopadhyay, Christian W. Gruber, A. Purcell, M. Yandell, B. Olivera, L. Ellgaard   +10 more
semanticscholar   +1 more source