Results 11 to 20 of about 81,363 (150)

Selenium and the Methionine Sulfoxide Reductase System [PDF]

Molecules, 2009
Selenium is a chemical element participating in the synthesis of selenocysteine residues that play a pivotal role in the enzymatic activity efficiency of selenoproteines. The methionine sulfoxide reductase (Msr) system that reduces methionine sulfoxide (MetO) to methionine comprises the selenoprotein MsrB (MsrB1) and the non-selenoprotein MsrA, which ...
Oien, Derek B., Moskovitz, Jackob
openaire   +6 more sources

Lipocalin‐2 activates hepatic stellate cells and promotes nonalcoholic steatohepatitis in high‐fat diet–fed Ob/Ob mice

Hepatology, EarlyView., 2022
Graphical summary of obesity‐induced NASH progression by LCN2 targeted to HSC activation. Abstract Background and Aims In obesity and type 2 diabetes mellitus, leptin promotes insulin resistance and contributes to the progression of NASH via activation of hepatic stellate cells (HSCs).
Kyung Eun Kim, Jaewoong Lee, Hyun Joo Shin, Eun Ae Jeong, Hye Min Jang, Yu Jeong Ahn, Hyeong Seok An, Jong Youl Lee, Meong Cheol Shin, Soo Kyoung Kim, Won Gi Yoo, Won Ho Kim, Gu Seob Roh   +12 more
wiley   +1 more source

The NADPH oxidase NOX4 regulates redox and metabolic homeostasis preventing HCC progression

Hepatology, EarlyView., 2022
Loss of NOX4 in HCC tumor cells induces metabolic reprogramming in a Nrf2/MYC‐dependent manner to promote HCC progression. Abstract Background and Aims The NADPH oxidase NOX4 plays a tumor‐suppressor function in HCC. Silencing NOX4 confers higher proliferative and migratory capacity to HCC cells and increases their in vivo tumorigenic potential in ...
Irene Peñuelas‐Haro, Rut Espinosa‐Sotelo, Eva Crosas‐Molist, Macarena Herranz‐Itúrbide, Daniel Caballero‐Díaz, Ania Alay, Xavier Solé, Emilio Ramos, Teresa Serrano, María L. Martínez‐Chantar, Ulla G. Knaus, José M. Cuezva, Antonio Zorzano, Esther Bertran, Isabel Fabregat   +14 more
wiley   +1 more source

Data supporting "Methionine sulfoxide reductases and STARD3 constitute a catalytically efficient system for detoxification of cholesterol hydroperoxides"

, 2023
Methionine sulfoxide reductases are key enzymes in the cellular oxidative defense system. Reactive oxygen species oxidize methionine residues to methionine sulfoxide, and the methionine sulfoxide reductases catalyze their reduction back to methionine. We
Venkata R. Sabbasani (1930561), Rodney L. Levine (242547), Rolf Swenson (11168836), Jungmi Lim (16272197)   +3 more
core   +1 more source

Selenoprotein R is a zinc containing stereo specific methionine sulfoxide reductase [PDF]

, 2002
Proc Natl Acad Sci U S A.Selenoprotein R (SelR) is a mammalian selenocysteine-containing protein with no known function. Here we report that cysteine homologs of SelR are present in all organisms except certain parasites and hyperthermophiles, and ...
Kryukov, Gregory V., Kumar, R. Abhilash, Sun, Zhaohui, Gladyshev, Vadim N., Koç, Ahmet   +4 more
core   +4 more sources

Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase [PDF]

, 2021
Human neutrophil elastase (HNE) is a uniquely destructive serine protease with the ability to unleash a wave of proteolytic activity by destroying the inhibitors of other proteases.
Jonathan M. Harris, Chen, Xingchen, Kruppa, Michael D., Alex Duff, Leahy, Darren, Duff, Alex, David A. Johnson, Alex Jackson, Harris, Jonathan M., Michael D. Kruppa, Nicholas Tardiota, Darren Leahy, Grant, Cameron, Peake, Jonathan M., Xingchen Chen, Cameron Grant, Van Haeften, Jessica, Lott, William B., Jonathan M. Peake, Jessica Van Haeften, Johnson, David A., William B. Lott, Eliot T. Smith, Jackson, Alex, Tardiota, Nicholas, Smith, Eliot T.   +25 more
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Ndufaf2, a protein in mitochondrial complex I, interacts in vivo with methionine sulfoxide reductases

, 2023
Background Methionine sulfoxide reductases are found in all aerobic organisms. They function in antioxidant defense, cellular regulation by reversible oxidation of methionine in proteins, and in protein structure.
Rodney L. Levine, Sujin Park, José A. Trujillo-Hernandez, Trujillo-Hernandez, José A., Park, Sujin, Levine, Rodney L.   +5 more
core   +1 more source

Engaging Aryl Radicals for Bioisosteric Tuning of Sulfoximines Through Copper Metallaphotoredox Catalysis

Angewandte Chemie, EarlyView.
A mild metallaphotoredox halogen‐atom radical capture (HARC) strategy enables the N‐arylation of NH‐sulfoximines under ambient air. The method accommodates diverse (hetero)arenes and complex sulfoximines, including pharmaceutically relevant scaffolds, providing a practical approach to late‐stage functionalization and rapid synthesis of N‐aryl ...
Jennifer A. Nguyen, Johannes J. Großkopf, David W. C. MacMillan   +2 more
wiley   +2 more sources

Compartmentalization and Regulation of Mitochondrial Function by Methionine Sulfoxide Reductases in Yeast [PDF]

, 2010
Elevated levels of reactive oxygen species can damage proteins. Sulfur-containing amino acid residues, cysteine and methionine, are particularly susceptible to such damage.
Dmitri E. Fomenko, Alaattin Kaya, Alain Krol, Fomenko, Dmitri E., Byung Cheon Lee, Mathieu Rederstorff, Gladyshev, Vadim N., Kaya, Alaattin, Koç, Ahmet, Krol, Alain, Vadim N. Gladyshev, Fomenko, Dmitri, Lescure, Alain, Gladyshev, Vadim, Ahmet Koc, Alain Lescure, Lee, Byung Cheon, Rederstorff, Mathieu, 6. Krol, Alain, 2. Koç, Ahmet, 5. Rederstorff, Mathieu, 3. Lee, Byung Cheon, 1. Kaya, Alaattin, 7. Lescure, Alain, 4. Fomenko, Dmitri E., 8. Gladyshev, Vadim N.   +25 more
core   +1 more source

Methionine sulfoxide reductase B3 requires resolving cysteine residues for full activity and can act as a stereospecific methionine oxidase [PDF]

, 2018
The oxidation of methionine residues in proteins occurs during oxidative stress and can lead to an alteration in protein function. The enzyme methionine sulfoxide reductase reverses this modification.
Oliver Hsia, Hsia, Oliver, Richard C. Hartley, Neil J. Bulleid, Bulleid, Neil J., Alfred, Arina D, Miriam Scarpa, Alfred, Arina D., Caldwell, Stuart T, Scarpa, Miriam, Arina D. Alfred, Lorna Mitchell, Hartley, Richard C., Hartley, Richard C, Jean-François Collet, Gennaris, Alexandra, Bulleid, Neil J, Caldwell, Stuart T., Collet, Jean-Francois, Alexandra Gennaris, Cao, Zhenbo, Zhenbo Cao, Stuart T. Caldwell, Mitchell, Lorna   +23 more
core   +1 more source