Zobrazeno 1 - 10
of 147
pro vyhledávání: '"Ninian J. Blackburn"'
Autor:
Katherine W. Rush, Karsten A. S. Eastman, William M. Kincannon, Ninian J. Blackburn, Vahe Bandarian
Publikováno v:
Journal of the American Chemical Society. 145:10167-10177
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e7b3575ecfc4800a9115019ae84b4c0f
https://doi.org/10.1021/jacs.3c00831
https://doi.org/10.1021/jacs.3c00831
Publikováno v:
Biochemistry. 61(8)
Peptidylglycine monooxygenase (PHM) is essential for the posttranslational amidation of neuroendocrine peptides. An important aspect of the PHM mechanism is the complete coupling of oxygen reduction to substrate hydroxylation, which implies no oxygen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cad794a7534bbafaa1f6fa136fa310c3
https://pubmed.ncbi.nlm.nih.gov/35380039
https://pubmed.ncbi.nlm.nih.gov/35380039
Publikováno v:
Protein Science. 32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fcd5f76711afa5b28662752825a03573
https://doi.org/10.1002/pro.4615
https://doi.org/10.1002/pro.4615
Autor:
Florencia Emiliani, Damián Alvarez-Paggi, Luciano A. Abriata, Alejandro J. Vila, Kelly N. Chacón, Daniel H. Murgida, Marcos N. Morgada, Ninian J. Blackburn
Publikováno v:
Inorganic Chemistry. 58:15687-15691
CuA centers perform efficient long-range electron transfer. The electronic structure of native CuA sites can be described by a double-potential well with a dominant σu* ground state in fast equilibrium with a less populated πu ground state. Here, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::840eb05aa0a7da380e093688c6329cd2
https://doi.org/10.1021/acs.inorgchem.9b01868
https://doi.org/10.1021/acs.inorgchem.9b01868
Publikováno v:
Biochemistry
The M-centers of the mononuclear monooxygenases peptidylglycine monooxygenase (PHM) and dopamine β-monooxygenase (DBM) bind and activate dioxygen on route to substrate hydroxylation. Recently we reported the rational design of a protein-based model
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f44136fc819bee6b4e585eba1a5004db
https://doi.org/10.1021/acs.biochem.9b00823
https://doi.org/10.1021/acs.biochem.9b00823
Publikováno v:
Biochemistry
Mononuclear copper monooxygenases peptidylglycine monooxygenase (PHM) and dopamine β-monooxygenase (DBM) catalyze the hydroxylation of high energy C-H bonds utilizing a pair of chemically distinct copper sites (CuH and CuM) separated by 11 A. In ear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aece85f0713ee7ff2e9a0c37ed47cc8b
https://doi.org/10.1021/acs.biochem.9b00312
https://doi.org/10.1021/acs.biochem.9b00312
Publikováno v:
J Inorg Biochem
An important question is whether consensus mechanisms for copper monooxygenase enzymes such as peptidylglycine monooxygenase (PHM) and dopamine β-monooxygenase (DBM) generated via computational and spectroscopic approaches account for important expe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::68b49f9fb4da3a08b6cb49c412c759be
https://doi.org/10.1016/j.jinorgbio.2022.111780
https://doi.org/10.1016/j.jinorgbio.2022.111780
Autor:
Sebastian Valenzuela, George M. Burslem, Natalie A. Schibrowsky, Michael Grasso, Stefanie D. Boyd, Tiffany Tsang, Donita C. Brady, Ye-Jin Kim, Duane D. Winkler, Katherine B. Alwan, Gavin J. Bond, Maria Matson Dzebo, Pernilla Wittung-Stafshede, Ronen Marmorstein, Ninian J. Blackburn
Publikováno v:
J Biol Chem
Normal physiology relies on the precise coordination of intracellular signaling pathways that respond to nutrient availability to balance cell growth and cell death. The canonical mitogen-activated protein kinase pathway consists of the RAF-MEK-ERK s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::019c4c44385c920877cf741e0808a1c9
https://pubmed.ncbi.nlm.nih.gov/34715128
https://pubmed.ncbi.nlm.nih.gov/34715128
Autor:
Duane D. Winkler, Pernilla Wittung-Stafshede, Donita C. Brady, Maria Matson Dzebo, Natalie A. Schibrowsky, Tiffany Tsang, Megan L. Matthews, Michael Grasso, Ye-Jin Kim, Stefanie D. Boyd, Ninian J. Blackburn, Katherine B. Alwan, Ronen Marmorstein, Sebastian Valenzuela, Gavin J. Bond, George M. Burslem
SummaryNormal physiology relies on the precise coordination of intracellular signal transduction pathways that respond to nutrient availability to balance cell growth and cell death. We recently established a critical mechanistic function for the red
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbfcbcf3d25c5ce6b9ab23b519f21f51
Autor:
C.D. Kline, Katarzyna Rudzka, Betty A. Eipper, Richard E. Mains, Sandra B. Gabelli, S. Maheshwari, L.M. Amzel, C. Shimokawa, Ninian J. Blackburn
Publikováno v:
Communications Biology, Vol 1, Iss 1, Pp 1-11 (2018)
The structures of metalloproteins that use redox-active metals for catalysis are usually exquisitely folded in a way that they are prearranged to accept their metal cofactors. Peptidylglycine α-hydroxylating monooxygenase (PHM) is a dicopper enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::338981b0c7d41dcef07bb105b5da554b
http://link.springer.com/article/10.1038/s42003-018-0082-y
http://link.springer.com/article/10.1038/s42003-018-0082-y