Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Nicolas Huguenin-Dezot"'
Autor:
Nicolas Huguenin-Dezot, Virginia De Cesare, Julien Peltier, Axel Knebel, Yosua Adi Kristaryianto, Daniel T. Rogerson, Yogesh Kulathu, Matthias Trost, Jason W. Chin
Publikováno v:
Cell Reports, Vol 16, Iss 4, Pp 1180-1193 (2016)
Ubiquitin is post-translationally modified by phosphorylation at several sites, but the consequences of these modifications are largely unknown. Here, we synthesize multi-milligram quantities of ubiquitin phosphorylated at serine 20, serine 57, and s
Externí odkaz:
https://doaj.org/article/b5b139d187af49c2bc7b15568d7770ec
Autor:
Claire Dickson, Adam J Fletcher, Marina Vaysburd, Ji-Chun Yang, Donna L Mallery, Jingwei Zeng, Christopher M Johnson, Stephen H McLaughlin, Mark Skehel, Sarah Maslen, James Cruickshank, Nicolas Huguenin-Dezot, Jason W Chin, David Neuhaus, Leo C James
Publikováno v:
eLife, Vol 7 (2018)
Cell surface Fc receptors activate inflammation and are tightly controlled to prevent autoimmunity. Antibodies also simulate potent immune signalling from inside the cell via the cytosolic antibody receptor TRIM21, but how this is regulated is unknow
Externí odkaz:
https://doaj.org/article/5202b947b0ec499ebb78db70bf28d54e
Autor:
Shan Tang, Adam T. Beattie, Lucie Kafkova, Gianluca Petris, Nicolas Huguenin-Dezot, Marc Fiedler, Matthew Freeman, Jason W. Chin
Publikováno v:
Nature
Hydrolase enzymes, including proteases, are encoded by 2–3% of the genes in the human genome and 14% of these enzymes are active drug targets1. However, the activities and substrate specificities of many proteases—especially those embedded in mem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb94aaefa718ed2175ff02656d11181c
https://doi.org/10.1038/s41586-022-04414-9
https://doi.org/10.1038/s41586-022-04414-9
Autor:
Bhumrapee Eiamthong, Piyachat Meesawat, Thanakrit Wongsatit, Jariya Jitdee, Raweewan Sangsri, Maturada Patchsung, Kanokpol Aphicho, Surased Suraritdechachai, Nicolas Huguenin‐Dezot, Shan Tang, Wipa Suginta, Boonchoat Paosawatyanyong, M. Madan Babu, Jason W. Chin, Danaya Pakotiprapha, Worawan Bhanthumnavin, Chayasith Uttamapinant
Publikováno v:
Angewandte Chemie International Edition. 61
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f46d71cfa9d756bb118044667036c3aa
https://doi.org/10.1002/anie.202210188
https://doi.org/10.1002/anie.202210188
Autor:
Bhumrapee Eiamthong, Piyachat Meesawat, Thanakrit Wongsatit, Jariya Jitdee, Raweewan Sangsri, Maturada Patchsung, Kanokpol Aphicho, Surased Suraritdechachai, Nicolas Huguenin‐Dezot, Shan Tang, Wipa Suginta, Boonchoat Paosawatyanyong, M. Madan Babu, Jason W. Chin, Danaya Pakotiprapha, Worawan Bhanthumnavin, Chayasith Uttamapinant
Publikováno v:
Angewandte Chemie. 134
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::07a5312736a4307c6e84e18d21a1de7f
https://doi.org/10.1002/ange.202210188
https://doi.org/10.1002/ange.202210188
Autor:
Bhumrapee Eiamthong, Piyachat Meesawat, Thanakrit Wongsatit, Jariya Jitdee, Raweewan Sangsri, Maturada Patchsung, Kanokpol Aphicho, Surased Suraritdechachai, Nicolas Huguenin‐Dezot, Shan Tang, Wipa Suginta, Boonchoat Paosawatyanyong, M. Madan Babu, Jason W. Chin, Danaya Pakotiprapha, Worawan Bhanthumnavin, Chayasith Uttamapinant
Publikováno v:
Angewandte Chemie (International ed. in English). 61(37)
We report a bioinformatic workflow and subsequent discovery of a new polyethylene terephthalate (PET) hydrolase, which we named MG8, from the human saliva metagenome. MG8 has robust PET plastic degradation activities under different temperature and s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35cf9f98f1bb95e3857e36806ec8da7e
https://pubmed.ncbi.nlm.nih.gov/35656865
https://pubmed.ncbi.nlm.nih.gov/35656865
Autor:
Jason W. Chin, Mohan Mahesh, Graham W. Heberlig, T.M. Schmeing, Christopher N. Boddy, Nicolas Huguenin-Dezot, D.P. Nguyen, Mark H. Dornan, D.A. Alonzo
Publikováno v:
Nature. 565(7737)
Many enzymes catalyse reactions that proceed through covalent acyl-enzyme (ester or thioester) intermediates1. These enzymes include serine hydrolases2,3 (encoded by one per cent of human genes, and including serine proteases and thioesterases), cyst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bbea4bfd4d9e8440fa77111fb3d197b
https://pubmed.ncbi.nlm.nih.gov/30814698
https://pubmed.ncbi.nlm.nih.gov/30814698
Autor:
Mark W. Richards, Nicolas Huguenin-Dezot, Richard Bayliss, Manjeet Mukherjee, Sarah R. Sabir, Jason W. Chin, James R. Ault, Andrew M. Fry, Laura O'Regan, Anastasia Zhuravleva, Josephina Sampson
Publikováno v:
Science Signaling. 11
Hsp72 is a member of the 70-kD heat shock family of molecular chaperones (Hsp70s) that comprise a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD) connected by a linker that couples the exchange of adenosine diphosphate (ADP) for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::839e38e8e645593f67f9730d4401ae02
https://doi.org/10.1126/scisignal.aao2464
https://doi.org/10.1126/scisignal.aao2464
Autor:
Michael Shaofei Zhang, Simon Brunner, Nicolas Huguenin-Dezot, Alexandria Deliz Liang, Wolfgang Schmied, Daniel Rogerson, Jason Chin
Publikováno v:
Protocol Exchange.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::42ce610027dba49816698e82308e12c5
https://doi.org/10.1038/protex.2017.046
https://doi.org/10.1038/protex.2017.046
Autor:
Susan M. Hancock, Kaihang Wang, Tamanna Haq, Nicolas Huguenin-Dezot, Agne Kazlauskaite, Jason W. Chin, Andrew M. Fry, Daniel T. Rogerson, Richard Bayliss, Miratul M. K. Muqit, Amit Sachdeva
Publikováno v:
Nature chemical biology. 11(7)
A newly engineered phosphoserine synthetase/tRNA pair allows quantitative insertion of phosphoserine or, when coupled with metabolic rewiring, a non-hydrolyzable analog into protein sequences, leading to high yields of modified constructs for functio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edf76e7b0630b72dc6377ed7d6b91e3b
https://pubmed.ncbi.nlm.nih.gov/26451426
https://pubmed.ncbi.nlm.nih.gov/26451426