Results 41 to 50 of about 207,078 (211)

Nitrogen Dioxide at Ambient Concentrations Induces Nitration and Degradation of PYR/PYL/RCAR Receptors to Stimulate Plant Growth: A Hypothetical Model

Plants, 2019
Exposing Arabidopsis thaliana (Arabidopsis) seedlings fed with soil nitrogen to 10−50 ppb nitrogen dioxide (NO2) for several weeks stimulated the uptake of major elements, photosynthesis, and cellular metabolisms to more than double the biomass of ...
Misa Takahashi, Hiromichi Morikawa
doaj   +1 more source

Regulation of Dual Activity of Ascorbate Peroxidase 1 From Arabidopsis thaliana by Conformational Changes and Posttranslational Modifications

Frontiers in Plant Science, 2021
Ascorbate peroxidase (APX) is an important reactive oxygen species (ROS)-scavenging enzyme, which catalyzes the removal of hydrogen peroxide (H2O2) to prevent oxidative damage.
Shubhpreet Kaur, Shubhpreet Kaur, Prapti Prakash, Prapti Prakash, Dong-Ho Bak, Sung Hyun Hong, Chuloh Cho, Moon-Soo Chung, Jin-Hong Kim, Jin-Hong Kim, Sungbeom Lee, Sungbeom Lee, Hyoung-Woo Bai, Hyoung-Woo Bai, Sang Yeol Lee, Byung Yeoup Chung, Seung Sik Lee, Seung Sik Lee   +17 more
doaj   +1 more source

Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase

, 2008
Nitration of tyrosine residues has been observed during various acute and chronic inflammatory diseases. However, the mechanism of tyrosine nitration and the nature of the proteins that become tyrosine nitrated during inflammation remain unclear. Here we
Kita, H., Schwarz, Heinz, Markus Schirle, Ralph S. Pero, Shimokawa, H., Alina Petre, Döring, Gerd, Thiyagarajan, N., Gabriel Bellon, Schirle, M. ; https://orcid.org/, Acharya, K., Alfred Doyle, Doyle, Alfred, Schumm, Michael, Schirle, Markus, Martina Ulrich, Przybylski, Michael, Prömm, F., Acharya, K Ravi, Checkel, James, Simon, H., Przybylski, M., Gerd Döring, Tsutsui, Masato, Bellon, Gabriel, Heinz Schwarz, Doyle, A., Tsutsui, M., Ulrich, M., Masato Tsutsui, Petre, Alina, Youhnovski, Nikolay, Hirohito Kita, Nethaji Thiyagarajan, Schmid-Grendelmeier, Peter, Petre, A., Nikolay Youhnovski, Peter Schmid-Grendelmeier, Pero, R., K. Ravi Acharya, Youhnovski, N., Lee, J., Hiroaki Shimokawa, Shimokawa, Hiroaki, Michael Przybylski, Schumm, M., Kita, Hirohito, Acharya, K. Ravi, Petre, Brînduşa-Alina, Bellon, G., Ulrich, Martina, Pero, Ralph S, Thiyagarajan, Nethaji, Simon, Hans-Uwe, Lee, James J, Hans-Uwe Simon, Schwarz, H., Prömm, Franziska, Döring, G., James Checkel, Schmid-Grendelmeier, P., Checkel, J., Michael Schumm, Pero, Ralph S., Lee, James J., Franziska Prömm, James J. Lee   +66 more
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RNA and mRNA Nitration as a Novel Metabolic Link in Potato Immune Response to Phytophthora infestans

Frontiers in Plant Science, 2018
Peroxynitrite (ONOO-) exhibits a well-documented nitration activity in relation to proteins and lipids; however, the interaction of ONOO- with nucleic acids remains unknown in plants.
Karolina Izbiańska, Jolanta Floryszak-Wieczorek, Joanna Gajewska, Barbara Meller, Daniel Kuźnicki, Magdalena Arasimowicz-Jelonek   +5 more
doaj   +1 more source

Copper-Catalyzed Tyrosine Nitration

, 2016
Tyrosine nitration, often observed during neurodegenerative disorders under nitrative stress, is usually considered to be induced chemically either by nitric oxide and oxygen forming nitrogen dioxide or by the decomposition of peroxynitrite.
Liang Qiao (34983), Yu Lu (11575), Hubert H. Girault (1413781), Baohong Liu (1413787)   +3 more
core   +1 more source

Selective nitration of Hsp90 acts as a metabolic switch promoting tumor cell proliferation

Redox Biology
Tumors develop in an oxidative environment characterized by peroxynitrite production and downstream protein tyrosine (Y) nitration. We showed that tyrosine nitration supports schwannoma cell proliferation and regulates cell metabolism in the inheritable ...
Isabelle E. Logan, Kyle T. Nguyen, Tilottama Chatterjee, Bhagyashree Manivannan, Ngozi P. Paul, Sharon R. Kim, Evelyn M. Sixta, Lydia P. Bastian, Carrie Marean-Reardon, Matthias A. Karajannis, Cristina Fernández-Valle, Alvaro G. Estevez, Maria Clara Franco   +12 more
doaj   +1 more source

Proteolytic Degradation of Tyrosine Nitrated Proteins

Archives of Biochemistry and Biophysics, 2000
Tyrosine nitration is a covalent posttranslational protein modification that has been detected under several pathological conditions. This study reports that nitrated proteins are degraded by chymotrypsin and that protein nitration enhances susceptibility to degradation by the proteasome.
J M, Souza, I, Choi, Q, Chen, M, Weisse, E, Daikhin, M, Yudkoff, M, Obin, J, Ara, J, Horwitz, H, Ischiropoulos   +9 more
openaire   +2 more sources

Tyrosine Nitration Impairs Mammalian Aldolase A Activity [PDF]

Molecular & Cellular Proteomics, 2004
Protein tyrosine nitration increases in vivo as a result of oxidative stress and is elevated in numerous inflammatory-associated diseases. Mammalian fructose-1,6-bisphosphate aldolases are tyrosine nitrated in lung epithelial cells and liver, as well as in retina under different inflammatory conditions.
Thomas, Koeck, Bruce, Levison, Stanley L, Hazen, John W, Crabb, Dennis J, Stuehr, Kulwant S, Aulak   +5 more
openaire   +2 more sources

Biochemical characterization of reactive nitrogen species by eosinophil peroxidase in tyrosine nitration [PDF]

, 2007
It is well known that eosinophils are involved in tyrosine nitration. In this study, we evaluated tyrosine nitration by rat eosinophils isolated from peritoneal fl uid and constituent eosinophils in the stomach.
Takigawa, Tomoko, Kurosawa, Carmen M., Wang, Da-Hong, Kambayashi, Yasuhiro, Ogino, Keiki, Hibino, Yuri, Ichimura, Hiroshi, Takemoto, Kei, Hitomi, Yoshiaki   +8 more
core   +1 more source

Glyoxalase I is inactivated by nitration of its tyrosine residues

, 1985
Glyoxalase I, an anti-cancer target enzyme, catalyses the detoxification of the cytotoxic hemithiolacetal formed between methylglyoxal and glutathione (GSH) by rearrangement to S-D-lactoylglutathione, which, in a reaction catalysed glyoxalase II, is ...
Carrington, S. J., Douglas, K. T.; id_orcid   +1 more
core   +7 more sources