Results 21 to 30 of about 3,392,726 (209)

Autodegradation of Protein Disulfide Isomerase [PDF]

Bioscience, Biotechnology, and Biochemistry, 1999
Protein disulfide isomerase (PDI) and its degradation products were found in HepG2, COS-1, and CHO-K1 cells. Whether or not the products were formed through autodegradation of PDI was examined, since PDI contains the CGHC motif, which is the active center of proteolytic activity in ER-60 protease.
URADE, Reiko, YASUNISHI, Ayako, OKUDO, Hirokazu, MORIYAMA, Tatsuya, KITO, Makoto   +4 more
openaire   +2 more sources

PDI-Regulated Disulfide Bond Formation in Protein Folding and Biomolecular Assembly

Molecules, 2020
Disulfide bonds play a pivotal role in maintaining the natural structures of proteins to ensure their performance of normal biological functions. Moreover, biological molecular assembly, such as the gluten network, is also largely dependent on the ...
Jiahui Fu, Jihui Gao, Zhongxin Liang, Dong Yang   +3 more
doaj   +1 more source

Comparative Genome Analyses of Plant Rust Pathogen Genomes Reveal a Confluence of Pathogenicity Factors to Quell Host Plant Defense Responses

Plants, 2022
Switchgrass rust caused by Puccinia novopanici (P. novopanici) has the ability to significantly affect the biomass yield of switchgrass, an important biofuel crop in the United States. A comparative genome analysis of P.
Raja Sekhar Nandety, Upinder S. Gill, Nick Krom, Xinbin Dai, Yibo Dong, Patrick X. Zhao, Kirankumar S. Mysore   +6 more
doaj   +1 more source

Protein disulfide isomerase in cardiovascular disease [PDF]

Experimental & Molecular Medicine, 2020
AbstractProtein disulfide isomerase (PDI) participates in the pathogenesis of numerous diseases. Increasing evidence indicates that intravascular cell-derived PDI plays an important role in the initiation and progression of cardiovascular diseases, including thrombosis and vascular inflammation.
Bei Xiong, Vishwanath Jha, Jeong-Ki Min, Jaehyung Cho   +3 more
openaire   +3 more sources

Inhibition of Protein Disulfide Isomerase in Thrombosis [PDF]

Basic & Clinical Pharmacology & Toxicology, 2016
AbstractThis MiniReview addresses our current understanding of the mechanisms by which protein disulfide isomerase (PDI) mediates thrombus formation and discusses the potential of blocking thrombosis by targeting PDI. Thiol isomerases are ubiquitous oxidoreductases primarily localized to the endoplasmic reticulum (ER) where they serve a critical role ...
Roelof H, Bekendam, Robert, Flaumenhaft
openaire   +2 more sources

Roles of Protein Disulfide Isomerase in Breast Cancer [PDF]

Cancers, 2022
Protein disulfide isomerase (PDI) is the endoplasmic reticulum (ER)’s most abundant and essential enzyme and serves as the primary catalyst for protein folding. Due to its apparent role in supporting the rapid proliferation of cancer cells, the selective blockade of PDI results in apoptosis through sustained activation of UPR pathways. The functions of
Suhui Yang, Chanel Jackson, Eduard Karapetyan, Pranabananda Dutta, Dulcie Kermah, Yong Wu, Yanyuan Wu, John Schloss, Jaydutt V. Vadgama   +8 more
openaire   +2 more sources

Protein disulfide isomerases as CSF biomarkers for the neuronal response to tau pathology [PDF]

, 2023
IntroductionCerebrospinal fluid (CSF) biomarkers for specific cellular disease processes are lacking for tauopathies. In this translational study we aimed to identify CSF biomarkers reflecting early tau pathology-associated unfolded protein response (UPR)
Henrik Zetterberg, Zetterberg, H., David J. Irwin, Marta del Campo, Scheper, Wiep; id_orcid, August B. Smit, van Ziel, A.M., Marta Jorge‐Oliva, Charlotte E. Teunissen, Tijms, Betty M., Teunissen, Charlotte E., Anna Maria van Ziel, del Campo, M., Pieter Jelle Visser, Jorge-Oliva, Marta, Johan Gobom, Lemstra, Afina W., Li, Ka Wan; id_orcid, Scheper, W., Campo, Marta del, Teunissen, C.E., van Ziel, Anna Maria, Wolzak, K., Blennow, K., Visser, Pieter Jelle, Wiep Scheper, Chen-Ploktkin, Alice, Lisa Vermunt, Pijnenburg, Y., Smit, A.B., Visser, P.J., Ka Wan Li, Wiesje van der Flier, Li, K.W., Vermunt, L., Pijnenburg, Yolande, Irwin, D.J., Kaj Blennow, Afina W. Lemstra, Vermunt, Lisa, Alice Chen‐Ploktkin, Wolzak, Kimberly; id_orcid, Zetterberg, Henrik, Lemstra, A.W., Gobom, J., Betty M. Tijms, Gobom, Johan, Kimberly Wolzak, Yolande Pijnenburg, Jorge-Oliva, M., Chen-Ploktkin, A., Blennow, Kaj, Smit, August B., van der Flier, Wiesje, van der Flier, W., Irwin, David J., Tijms, B.M.   +56 more
core   +3 more sources

The Lord of the Rings: Cysteine bonds crosslink the tail of siphovirus. [PDF]

Protein Sci
Abstract Long, non‐contractile tails composed of helical hexameric protein repeats that assemble into continuous tubular structures characterize siphoviruses. The siphovirus tail tube protein gp39 contains two cysteine residues per monomer. Cryo‐electron microscopy revealed that these cysteines are oriented toward the interface between the rings, which
Povilonienė S, Sasnauskas G, Tamulaitienė G, Labutytė G, Talaikis M, Mikšys A, Zajančkauskaitė A, Truncaitė L, Meškys R, Časaitė V.   +9 more
europepmc   +2 more sources

Structural and Functional Characterization of a Novel Family of Cyclophilins, the AquaCyps [PDF]

, 2016
Cyclophilins are ubiquitous cis-trans-prolyl isomerases (PPIases) found in all kingdoms of life. Here, we identify a novel family of cyclophilins, termed AquaCyps, which specifically occurs in marine Alphaproteobacteria, but not in related terrestric ...
Timm Maier, Franz X Schmid, Maier, Timm, Philipp A. M. Schmidpeter (453850), Jakob, Roman P., Johanna R. Koch (2825327), Schmidpeter, Philipp A. M., Franz X. Schmid (1748071), Schmid, Franz X., Philipp A M Schmidpeter, Johanna R Koch, Roman P. Jakob (1637830), Roman P Jakob, Koch, Johanna R., Timm Maier (1637839)   +14 more
core   +2 more sources

Interaction of Calreticulin with Protein Disulfide Isomerase [PDF]

Journal of Biological Chemistry, 1995
We report here that calreticulin interacts with protein disulfide isomerase (PDI). The PDI-calreticulin complex can be dissociated by Zn(2+)-iminodiacetate-substituted Sepharose-agarose chromatography, suggesting that these interactions may be Zn2+-dependent.
S, Baksh, K, Burns, C, Andrin, M, Michalak   +3 more
openaire   +2 more sources