Zobrazeno 1 - 10
of 163
pro vyhledávání: '"E. Neil G. Marsh"'
Autor:
Ayesha M. Patel, Karl J. Koebke, Timothy J. Grunkemeyer, Colleen M. Riordan, Youngsoo Kim, Ryan C. Bailey, E. Neil G. Marsh
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-8 (2022)
Abstract Viperin is a radical S-adenosylmethionine enzyme that catalyzes the formation of the antiviral ribonucleotide, 3’-deoxy-3’,4’-didehydroCTP. The enzyme is conserved across all kingdoms of life, and in higher animals viperin is localized
Externí odkaz:
https://doaj.org/article/bf20f6509eeb4dff83e8abb04e467a1d
Autor:
P. Takunda Chazovachii, Madeline J. Somers, Michael T. Robo, Dimitris I. Collias, Martin I. James, E. Neil G. Marsh, Paul M. Zimmerman, Jose F. Alfaro, Anne J. McNeil
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-6 (2021)
For many polymers, recycling via mechanical processes is not feasible and these materials are destined for landfills or incineration. Here the authors show an open-loop recycling method for superabsorbent polymers that involves decrosslinking via hyd
Externí odkaz:
https://doaj.org/article/af1d534e721c4e378519f0aa001aa604
Publikováno v:
Current Research in Microbial Sciences, Vol 1, Iss , Pp 1-6 (2020)
Fluorescent tools such as green fluorescent protein (GFP) have been used extensively as reporters in biochemistry and microbiology, but GFP and other conventional fluorescent proteins are restricted to aerobic environments. This limitation precludes
Externí odkaz:
https://doaj.org/article/d8cf9706412347389d5aaa7c5bac68bb
Publikováno v:
Frontiers in Molecular Biosciences, Vol 6 (2019)
The design of metal-binding sites in proteins that combine high affinity with high selectivity for the desired metal ion remains a challenging goal. Recently, a protein designed to display femtomolar affinity for UO22+, dubbed “Super Uranyl-binding
Externí odkaz:
https://doaj.org/article/f786cc78ea5d4079bc60a8d8db5374ed
Autor:
E. Neil G. Marsh
Publikováno v:
Frontiers in Chemistry, Vol 4 (2016)
Externí odkaz:
https://doaj.org/article/0644c4b52ab440a7b9be6fcb074c9e33
Publikováno v:
Biochemistry. 62:53-61
Ferulic acid decarboxylase (FDC) catalyzes the reversible carboxylation of various substituted phenylacrylic acids to produce the correspondingly substituted styrenes and CO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e16e2002f19d8e622bdcd902704ebec3
https://doi.org/10.1021/acs.biochem.2c00460
https://doi.org/10.1021/acs.biochem.2c00460
Autor:
Aathmaja Anandhi Rangarajan, Karl J. Koebke, E. Neil G. Marsh, Nicole M. Koropatkin, Hannah E. Chia, Julie S. Biteen
Publikováno v:
ACS Chemical Biology. 16:2109-2115
Bilin-binding fluorescent proteins like UnaG-bilirubin are noncovalent ligand-dependent reporters for oxygen-free microscopy but are restricted to blue and far-red fluorescence. Here we describe a high-throughput screening approach to provide a new U
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38b5ec723578b137c8c21394f7b15f0a
https://doi.org/10.1021/acschembio.1c00391
https://doi.org/10.1021/acschembio.1c00391
Autor:
E. Neil G. Marsh, Prathamesh M. Datar
Publikováno v:
ACS Catalysis. 11:11723-11732
Phenazine-1-carboxylic acid decarboxylase (PhdA) is a member of the expanding class of prenylated-FMN-dependent (prFMN) decarboxylase enzymes. These enzymes have attracted interest for their abilit...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::610324821256ff6b75490136318c68e7
https://doi.org/10.1021/acscatal.1c03040
https://doi.org/10.1021/acscatal.1c03040
Autor:
E Neil G, Marsh
Publikováno v:
Methods in enzymology. 669
Adenosylcobalamin- (AdoCbl) dependent enzyme reactions involved the transfer of hydrogen atoms between the 5'-carbon of the coenzyme and the substrates and products of the reaction. Tritium and deuterium kinetic isotope effect measurements are, there
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::dc71dcbb0dd83a0677b9d50e0cc26672
https://pubmed.ncbi.nlm.nih.gov/35644170
https://pubmed.ncbi.nlm.nih.gov/35644170
Publikováno v:
J Biol Chem
Heme oxygenase-2 (HO2) and -1 (HO1) catalyze heme degradation to biliverdin, CO, and iron, forming an essential link in the heme metabolism network. Tight regulation of the cellular levels and catalytic activities of HO1 and HO2 is important for main
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88010c4444dc2e1d950e0fe032d92ede
https://doi.org/10.1074/jbc.ra120.014919
https://doi.org/10.1074/jbc.ra120.014919