Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Benjamin Suenkel"'
Autor:
Frank Fischer, Melanie Gertz, Benjamin Suenkel, Mahadevan Lakshminarasimhan, Mike Schutkowski, Clemens Steegborn
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e45098 (2012)
Sirtuins are protein deacylases regulating metabolism and aging processes, and the seven human isoforms are considered attractive therapeutic targets. Sirtuins transfer acyl groups from lysine sidechains to ADP-ribose, formed from the cosubstrate NAD
Externí odkaz:
https://doaj.org/article/f21bde9097c041aeb954e9c91d43ddf5
Autor:
Melanie Gertz, Giang Thi Tuyet Nguyen, Frank Fischer, Benjamin Suenkel, Christine Schlicker, Benjamin Fränzel, Jana Tomaschewski, Firouzeh Aladini, Christian Becker, Dirk Wolters, Clemens Steegborn
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e49761 (2012)
Sirtuins are protein deacetylases regulating metabolism, stress responses, and aging processes, and they were suggested to mediate the lifespan extending effect of a low calorie diet. Sirtuin activation by the polyphenol resveratrol can mimic such li
Externí odkaz:
https://doaj.org/article/c93d1a1c9fc94297b6220370147c8d3d
Autor:
Benjamin Suenkel, Sergio Valente, Clemens Zwergel, Sandra Weiss, Elisabetta Di Bello, Rossella Fioravanti, Michele Aventaggiato, João A. Amorim, Neha Garg, Surinder Kumar, David B. Lombard, Tuo Hu, Pankaj K. Singh, Marco Tafani, Carlos M. Palmeira, David Sinclair, Antonello Mai, Clemens Steegborn
Publikováno v:
Journal of medicinal chemistry. 65(20)
Sirtuins are NAD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3afd0c8aa27ecec7cea363831015b0c9
https://pubmed.ncbi.nlm.nih.gov/36228194
https://pubmed.ncbi.nlm.nih.gov/36228194
Autor:
Pablo Porras, Erich E. Wanker, Melanie Kny, Jens Fielitz, Thomas Sommer, Xiaoxi Zhu, Rebekka Migotti, Marcel Nowak, Gunnar Dittmar, Franziska Schmidt, Benjamin Suenkel
Publikováno v:
Journal of Cell Science.
The muscle-specific RING-finger protein MuRF1 (also known as TRIM63) constitutes a bona fide ubiquitin ligase that routes proteins like several different myosin heavy chain proteins (MyHC) to proteasomal degradation during muscle atrophy. In two unbi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51c980fd0df2659fca04767aaefbc203
https://doi.org/10.1242/jcs.233395
https://doi.org/10.1242/jcs.233395
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 23:143-146
Sirtuins are NAD(+) consuming protein deacylases involved in many cellular processes from DNA-repair to metabolism. Their contribution to age-related and metabolic diseases makes them attractive pharmaceutical targets. Few pharmacological inhibitors
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a70909315981c9ef5ecf5030fad3ea7
https://doi.org/10.1016/j.bmcl.2012.10.136
https://doi.org/10.1016/j.bmcl.2012.10.136
Autor:
Benjamin Suenkel, Clemens Steegborn
Lysine acetylation is long known as a regulatory posttranslational modification of histone proteins and is emerging as a ubiquitous intracellular protein modification. Additional lysine acylations such as succinylation and glutarylation have also bee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a285818854737b1217bc8e073b95bf91
https://doi.org/10.1016/bs.mie.2015.12.004
https://doi.org/10.1016/bs.mie.2015.12.004
Autor:
Christine Schlicker, Frank Fischer, Benjamin Fränzel, Christian F. W. Becker, Clemens Steegborn, Benjamin Suenkel, Melanie Gertz, Firouzeh Aladini, Dirk Wolters, Giang Thi Tuyet Nguyen, Jana Tomaschewski
Publikováno v:
PLoS ONE, Vol 7, Iss 11, p e49761 (2012)
PLoS ONE
PLoS ONE
Sirtuins are protein deacetylases regulating metabolism, stress responses, and aging processes, and they were suggested to mediate the lifespan extending effect of a low calorie diet. Sirtuin activation by the polyphenol resveratrol can mimic such li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf965774407699098c975705aac3f7d8
http://europepmc.org/articles/PMC3504108?pdf=render
http://europepmc.org/articles/PMC3504108?pdf=render
Autor:
Mike Schutkowski, Benjamin Suenkel, Mahadevan Lakshminarasimhan, Clemens Steegborn, Melanie Gertz, Frank Fischer
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e45098 (2012)
PLoS ONE
PLoS ONE
Sirtuins are protein deacylases regulating metabolism and aging processes, and the seven human isoforms are considered attractive therapeutic targets. Sirtuins transfer acyl groups from lysine sidechains to ADP-ribose, formed from the cosubstrate NAD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3aa1e0d78a7010f3dd8a774ecc7e0748
http://europepmc.org/articles/PMC3446968?pdf=render
http://europepmc.org/articles/PMC3446968?pdf=render
Autor:
Benjamin Suenkel, Steegborn C
Publikováno v:
Europe PubMed Central
Lysine acetylation is long known as a regulatory posttranslational modification of histone proteins and is emerging as a ubiquitous intracellular protein modification. Additional lysine acylations such as succinylation and glutarylation have also bee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::6669f0652842a921e81475cf64484de0
http://europepmc.org/abstract/med/27372754
http://europepmc.org/abstract/med/27372754