Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Mark A, Nakasone"'
Autor:
Alena Kroupova, Valentina A. Spiteri, Zoe J. Rutter, Hirotake Furihata, Darren Darren, Sarath Ramachandran, Sohini Chakraborti, Kevin Haubrich, Julie Pethe, Denzel Gonzales, Andre J. Wijaya, Maria Rodriguez-Rios, Manon Sturbaut, Dylan M. Lynch, William Farnaby, Mark A. Nakasone, David Zollman, Alessio Ciulli
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-14 (2024)
Abstract The ubiquitin E3 ligase cereblon (CRBN) is the target of therapeutic drugs thalidomide and lenalidomide and is recruited by most targeted protein degraders (PROTACs and molecular glues) in clinical development. Biophysical and structural inv
Externí odkaz:
https://doaj.org/article/70479f877d614c148e6f8203f19d4b2d
Autor:
Victor H. Villar, Maria Francesca Allega, Ruhi Deshmukh, Tobias Ackermann, Mark A. Nakasone, Johan Vande Voorde, Thomas M. Drake, Janina Oetjen, Algernon Bloom, Colin Nixon, Miryam Müller, Stephanie May, Ee Hong Tan, Lars Vereecke, Maude Jans, Gillian Blancke, Daniel J. Murphy, Danny T. Huang, David Y. Lewis, Thomas G. Bird, Owen J. Sansom, Karen Blyth, David Sumpton, Saverio Tardito
Publikováno v:
NATURE CHEMICAL BIOLOGY
Villar, V H, Allega, M F, Deshmukh, R, Ackermann, T, Nakasone, M A, Voorde, J V, Drake, T, Oetjen, J, Bloom, A, Nixon, C, Vereecke, L, Jans, M, Blancke, G, Bird, T G, Lewis, D, Sansom, O J, Blyth, K, Sumpton, D & Tardito, S 2022, ' Hepatic glutamine synthetase controls N5-methylglutamine in homeostasis and cancer ', Nature Chemical Biology . https://doi.org/10.1038/s41589-022-01154-9
Villar, V H, Allega, M F, Deshmukh, R, Ackermann, T, Nakasone, M A, Voorde, J V, Drake, T, Oetjen, J, Bloom, A, Nixon, C, Vereecke, L, Jans, M, Blancke, G, Bird, T G, Lewis, D, Sansom, O J, Blyth, K, Sumpton, D & Tardito, S 2022, ' Hepatic glutamine synthetase controls N5-methylglutamine in homeostasis and cancer ', Nature Chemical Biology . https://doi.org/10.1038/s41589-022-01154-9
Glutamine synthetase (GS) activity is conserved from prokaryotes to humans, where the ATP-dependent production of glutamine from glutamate and ammonia is essential for neurotransmission and ammonia detoxification. Here, we show that mammalian GS uses
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d644a6f88baef6ab2fcb6f68543200e9
https://doi.org/10.1038/s41589-022-01154-9
https://doi.org/10.1038/s41589-022-01154-9
Autor:
Mark A. Nakasone, Karolina A. Majorek, Mads Gabrielsen, Gary J. Sibbet, Brian O. Smith, Danny T. Huang
Publikováno v:
Nature Chemical Biology. 18:422-431
Ubiquitin (Ub) chain types govern distinct biological processes. K48-linked polyUb chains target substrates for proteasomal degradation, but the mechanism of Ub chain synthesis remains elusive due to the transient nature of Ub handover. Here, we pres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::59b00b065e84f7df0c09e6f054c06098
https://doi.org/10.1038/s41589-021-00952-x
https://doi.org/10.1038/s41589-021-00952-x
Autor:
Oliver Hsia, Matthias Hinterndorfer, Angus D. Cowan, Kentaro Iso, Tasuku Ishida, Ramasubramanian Sundaramoorthy, Mark A. Nakasone, Andrea Rukavina, Koraljka Husnjak, Martin Wegner, Alejandro Correa-Sáez, Conner Craigon, Chiara Maniaci, Andrea Testa, Manuel Kaulich, Ivan Dikic, Georg E. Winter, Alessio Ciulli
Targeted protein degradation is a drug modality represented by compounds that recruit a target to an E3 ubiquitin ligase to promote target ubiquitination and proteasomal degradation. Historically, the field distinguishes monovalent degraders from bif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::106f28b55a66af1eca1fd1fb3f153a05
https://doi.org/10.1101/2023.02.14.528511
https://doi.org/10.1101/2023.02.14.528511
Publikováno v:
Life science alliance. 5(12)
ARF tumor suppressor protein is a key regulator of the MDM2-p53 signaling axis. ARF interferes with MDM2-mediated ubiquitination and degradation of p53 by sequestering MDM2 in the nucleolus and preventing MDM2-p53 interaction and nuclear export of p5
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49a63480fa2ce1b254c1f46c72957a86
https://pubmed.ncbi.nlm.nih.gov/35944929
https://pubmed.ncbi.nlm.nih.gov/35944929
Autor:
Mark A, Nakasone, Karolina A, Majorek, Mads, Gabrielsen, Gary J, Sibbet, Brian O, Smith, Danny T, Huang
Publikováno v:
Nature chemical biology. 18(4)
Ubiquitin (Ub) chain types govern distinct biological processes. K48-linked polyUb chains target substrates for proteasomal degradation, but the mechanism of Ub chain synthesis remains elusive due to the transient nature of Ub handover. Here, we pres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::a423c870b00a52268d7ef3f5190bcd0f
https://pubmed.ncbi.nlm.nih.gov/35027744
https://pubmed.ncbi.nlm.nih.gov/35027744
Autor:
Brian O. Smith, Gary J. Sibbet, Chatrin Chatrin, David Sumpton, Mads Gabrielsen, Syed Feroj Ahmed, Danny T. Huang, Mark A. Nakasone, Lori Buetow
Publikováno v:
Science Advances
The C-terminal RING and DTC domains of mammalian Deltex proteins catalyze ADP-ribosylation at the C terminus of ubiquitin.
Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of nume
Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of nume
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3f05735803f347e349100b8c131a59d
https://pubmed.ncbi.nlm.nih.gov/32948590
https://pubmed.ncbi.nlm.nih.gov/32948590
Autor:
Mark A. Nakasone, Wissam Mansour, Ashraf Brik, Suman Kumar Maity, Somasekhar Bondalapati, Michael H. Glickman
Publikováno v:
Chemistry - A European Journal. 21:7360-7364
Modification of ubiquitin by phosphorylation extends the signaling possibilities of this dynamic signal, as it could affect the activity of ligases and the processing of ubiquitin chains by deubiquitinases. The first chemical synthesis of phosphoryla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5dd6286f9b55fdacd369a9395811a79
https://doi.org/10.1002/chem.201500540
https://doi.org/10.1002/chem.201500540
Autor:
Rina Rosenzweig, Rajesh Singh, Farid El Oualid, Michał Chojnacki, David Fushman, Michael H. Glickman, Fabian Glaser, Dharjath S. Hameed, Lewis E. Kay, Wissam Mansour, Mark A. Nakasone, Zanlin Yu, Huib Ovaa
Publikováno v:
CELL CHEMICAL BIOLOGY, 24(4), 443
Ubiquitin (Ub) signaling is a diverse group of processes controlled by covalent attachment of small protein Ub and polyUb chains to a range of cellular protein targets. The best documented Ub signaling pathway is the one that delivers polyUb proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a2f383a5c26b1ecdebf3968ff5d7a19b
http://hdl.handle.net/1887/114544
http://hdl.handle.net/1887/114544
Autor:
David Fushman, Mark A. Nakasone, Ashraf Brik, Donald S. Kirkpatrick, Steven P. Gygi, Noa Reis, Michael H. Glickman, Peter Siman, Daoning Zhang, Daria Krutauz
Publikováno v:
Nature chemical biology
A frame-shift mutation in the transcript of the ubiquitin-B gene leads to a C-terminally extended ubiquitin, UBB+1. UBB+1 has been considered to inhibit proteasomes, and as such to be the underlying cause for toxic protein buildup correlated with cer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f09201056a9dd6c8868ac6f7c097ab1f
http://europepmc.org/articles/PMC4466224
http://europepmc.org/articles/PMC4466224