Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Markus Dagnell"'
Autor:
Jaime James, Yifei Chen, Clara M Hernandez, Florian Forster, Markus Dagnell, Qing Cheng, Amir A Saei, Hassan Gharibi, Gonzalo Fernandez Lahore, Annika Åstrand, Rajneesh Malhotra, Bernard Malissen, Roman A Zubarev, Elias SJ Arnér, Rikard Holmdahl
Publikováno v:
eLife, Vol 11 (2022)
Chronic autoimmune diseases are associated with mutations in PTPN22, a modifier of T cell receptor (TCR) signaling. As with all protein tyrosine phosphatases, the activity of PTPN22 is redox regulated, but if or how such regulation can modulate infla
Externí odkaz:
https://doaj.org/article/e84e04b732424594be1fff342674675b
Publikováno v:
Antioxidants, Vol 10, Iss 1, p 111 (2021)
Protein tyrosine phosphatases (PTPs) can be regulated by several redox-dependent mechanisms and control growth factor-activated receptor tyrosine kinase phosphorylation cascades. Reversible oxidation of PTPs is counteracted by reductive enzymes, incl
Externí odkaz:
https://doaj.org/article/85e15afbd24f4c4b8c31ad247d284cd5
Autor:
Charles Spruck, Olle Sangfelt, Martin Widschwendter, Steven I. Reed, Dan Grander, Hans Nordgren, Per Sangfelt, Fredrik Petersson, Susanne Egyhazi, Johan Hansson, Mohammad Reza Zali, Babak Noori Nayer, Sepideh Zabihi Nejad, Markus Dagnell, Martin Corcoran, Elisabeth Mueller-Holzner, Christian Marth, Dimitra Dofou, Heidi Fiegl, Diana Cepeda, Alena Maljukova, Kathleen Klotz, Sophia Apostolidou, Natalie von der Lehr, Dahui Sun, Shahab Akhoondi
The ubiquitin-proteasome system is a major regulatory pathway of protein degradation and plays an important role in cellular division. Fbxw7 (or hCdc4), a member of the F-box family of proteins, which are substrate recognition components of the multi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f23907af830a4be9a61f44daaab6df85
https://doi.org/10.1158/0008-5472.c.6496770
https://doi.org/10.1158/0008-5472.c.6496770
Autor:
Charles Spruck, Olle Sangfelt, Martin Widschwendter, Steven I. Reed, Dan Grander, Hans Nordgren, Per Sangfelt, Fredrik Petersson, Susanne Egyhazi, Johan Hansson, Mohammad Reza Zali, Babak Noori Nayer, Sepideh Zabihi Nejad, Markus Dagnell, Martin Corcoran, Elisabeth Mueller-Holzner, Christian Marth, Dimitra Dofou, Heidi Fiegl, Diana Cepeda, Alena Maljukova, Kathleen Klotz, Sophia Apostolidou, Natalie von der Lehr, Dahui Sun, Shahab Akhoondi
Supplementary Table 1 from FBXW7/hCDC4 Is a General Tumor Suppressor in Human Cancer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::393ecf68db5a7048c1c006ed29fe6c1b
https://doi.org/10.1158/0008-5472.22371378.v1
https://doi.org/10.1158/0008-5472.22371378.v1
Autor:
Jaime James, Yifei Chen, Clara M Hernandez, Florian Forster, Markus Dagnell, Qing Cheng, Amir A Saei, Hassan Gharibi, Gonzalo Fernandez Lahore, Annika Åstrand, Rajneesh Malhotra, Bernard Malissen, Roman A Zubarev, Elias SJ Arnér, Rikard Holmdahl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ff5dbe62ae25e2880ce34bc2ae73f5a4
https://doi.org/10.7554/elife.74549.sa2
https://doi.org/10.7554/elife.74549.sa2
Autor:
Jaime James, Yifei Chen, Clara M. Hernandez, Florian Forster, Markus Dagnell, Qing Cheng, Amir A. Saei, Hassan Gharibi, Gonzalo Fernandez Lahore, Annika Åstrand, Rajneesh Malhotra, Bernard Malissen, Roman A. Zubarev, Elias S.J. Arnér, Rikard Holmdahl
Chronic autoimmune diseases are associated with mutations in PTPN22, a modifier of T cell receptor signaling. As with all protein tyrosine phosphatases the activity of PTPN22 is redox regulated, but if or how such regulation can modulate inflammatory
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::40311d5aa672083ccd8782106032146d
https://doi.org/10.1101/2021.12.02.470976
https://doi.org/10.1101/2021.12.02.470976
Autor:
Elias S.J. Arnér, Benoit Boivin, Syed Husain Mustafa Rizvi, Paul E. Pace, Qing Cheng, Markus Dagnell, Christine C. Winterbourn
Publikováno v:
Journal of Biological Chemistry. 294:12330-12338
Protein-tyrosine phosphatases (PTPs) counteract protein tyrosine phosphorylation and cooperate with receptor-tyrosine kinases in the regulation of cell signaling. PTPs need to undergo oxidative inhibition for activation of cellular cascades of protei
Autor:
Takaaki Akaike, Edward E. Schmidt, Justin R. Prigge, Elias S.J. Arnér, Tsuyoshi Takata, Tomoaki Ida, N. Balog, Yosuke Funato, Péter Nagy, Yoshito Kumagai, Qing Cheng, Hiroaki Miki, Yumi Abiko, Markus Dagnell, Éva Dóka, Akira Nishimura, Jon M. Fukuto, B. Espinosa, Nho Cong Luong
Publikováno v:
Science Advances
Thioredoxin system–mediated persulfidation of Cys residues controls protein function and protects them from oxidative stress.
Irreversible oxidation of Cys residues to sulfinic/sulfonic forms typically impairs protein function. We found that p
Irreversible oxidation of Cys residues to sulfinic/sulfonic forms typically impairs protein function. We found that p
Autor:
Iryna Kolosenko, Jianping Liu, Lars-Olof Johansson, Wang Qian, B. Espinosa, Sander Busker, K. Pokrovskaja Tamm, Elias S.J. Arnér, Sanaz Attarha, Brent D. G. Page, Martin Haraldsson, Dan Grandér, Markus Dagnell
Publikováno v:
Science Advances
Redox regulation of STAT3 is targeted by direct inhibition of TrxR1, illuminating a promising link for therapeutic development.
Because of its key role in cancer development and progression, STAT3 has become an attractive target for developing n
Because of its key role in cancer development and progression, STAT3 has become an attractive target for developing n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c1ddddf8c178f54a926413bea7cc21f
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-169887
http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-169887
Publikováno v:
Antioxidants
Antioxidants, Vol 10, Iss 111, p 111 (2021)
Volume 10
Issue 1
Antioxidants, Vol 10, Iss 111, p 111 (2021)
Volume 10
Issue 1
Protein tyrosine phosphatases (PTPs) can be regulated by several redox-dependent mechanisms and control growth factor-activated receptor tyrosine kinase phosphorylation cascades. Reversible oxidation of PTPs is counteracted by reductive enzymes, incl