Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Marcus L, Hemshorn"'
Autor:
Grace D. Galles, Daniel T. Infield, Colin J. Clark, Marcus L. Hemshorn, Shivani Manikandan, Frederico Fazan, Ali Rasouli, Emad Tajkhorshid, Jason D. Galpin, Richard B. Cooley, Ryan A. Mehl, Christopher A. Ahern
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Aromatic amino acids in proteins support ligand binding and protein stability. To parse the physiocochemical roles of aromatic interactions, here Galles, Infield and co-authors identify pyrrolysine-based aminoacyl-tRNA synthetases that enable the enc
Externí odkaz:
https://doaj.org/article/bf16f9a0529447d48911d7bab7bf37ef
Autor:
Longteng Tang, Riley M. Bednar, Nikita D. Rozanov, Marcus L. Hemshorn, Ryan A. Mehl, Chong Fang
Publikováno v:
Natural Sciences, Vol 2, Iss 4, Pp n/a-n/a (2022)
Abstract The development of bioorthogonal fluorogenic probes constitutes a vital force to advance life sciences. Tetrazine‐encoded green fluorescent proteins (GFPs) show high bioorthogonal reaction rate and genetic encodability but suffer from low
Externí odkaz:
https://doaj.org/article/5bb1da02a4f843db8c78ec7064008817
Autor:
Longteng Tang, Riley M. Bednar, Nikita D. Rozanov, Marcus L. Hemshorn, Ryan A. Mehl, Chong Fang
Publikováno v:
Natural sciences (Weinheim, Germany). 2(4)
The development of bioorthogonal fluorogenic probes constitutes a vital force to advance life sciences. Tetrazine-encoded green fluorescent proteins (GFPs) show high bioorthogonal reaction rate and genetic encodability, but suffer from low fluorogeni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c8d611df52c55c703c5283eed31898e
https://pubmed.ncbi.nlm.nih.gov/36440454
https://pubmed.ncbi.nlm.nih.gov/36440454
Autor:
Savanna, Avila-Crump, Marcus L, Hemshorn, Chloe M, Jones, Lea, Mbengi, Kyle, Meyer, Joshua A, Griffis, Subhashis, Jana, Grace E, Petrina, Vinayak V, Pagar, P Andrew, Karplus, E James, Petersson, John J, Perona, Ryan A, Mehl, Richard B, Cooley
Publikováno v:
ACS chemical biology. 17(12)
Genetic code expansion (GCE) technologies commonly use the pyrrolysyl-tRNA synthetase (PylRS)/tRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::af6e02321884d3130d15c09b8a7410dd
https://pubmed.ncbi.nlm.nih.gov/36383641
https://pubmed.ncbi.nlm.nih.gov/36383641
Autor:
null Longteng Tang, null Riley M. Bednar, null Nikita D. Rozanov, null Marcus L. Hemshorn, null Ryan A. Mehl, null Chong Fang
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::256ec4a98dcaae4b1db7fe31d1cb9b0f
https://doi.org/10.1002/ntls.20220028/v2/response1
https://doi.org/10.1002/ntls.20220028/v2/response1
Autor:
Grace D. Galles, Daniel T. Infield, Colin J. Clark, Marcus L. Hemshorn, Shivani Manikandan, Frederico Fazan, Ali Rasouli, Emad Tajkhorshid, Jason D. Galpin, Richard B. Cooley, Ryan A. Mehl, Christopher A. Ahern
The aromatic side-chains of phenylalanine, tyrosine, and tryptophan interact with their environments via both hydrophobic and electrostatic interactions. Determining the extent to which these contribute to protein function and stability is not possib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::41718907172f5f0d3383b2ac2a5a8dff
https://doi.org/10.1101/2022.04.12.488046
https://doi.org/10.1101/2022.04.12.488046