Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Steven O. Mansoorabadi"'
Publikováno v:
Journal of the American Chemical Society. 144:3381-3385
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6e451eb88e569e9d712d6fc77d1f168b
https://doi.org/10.1021/jacs.2c00678
https://doi.org/10.1021/jacs.2c00678
Autor:
Steven O. Mansoorabadi, Shuxin Li, Eta A. Isiorho, Chidinma L. Odili, Victoria L. Owens, Patrick H. Donnan
Publikováno v:
The Journal of Biological Chemistry
Heme oxygenases (HOs) play a critical role in recouping iron from the labile heme pool. The acquisition and liberation of heme iron are especially important for the survival of pathogenic bacteria. All characterized HOs, including those belonging to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::897d1c96471b401b8ef44458dcca4344
http://europepmc.org/articles/PMC8131568
http://europepmc.org/articles/PMC8131568
Autor:
Douglas C. Goodwin, Steven O. Mansoorabadi, Patrick H. Donnan, Patrick G. Sahrmann, Kenneth M. Merz
Publikováno v:
Journal of chemical information and modeling. 60(10)
MRP.py is a Python-based parametrization program for covalently modified amino acid residues for molecular dynamics simulations. Charge derivation is performed via an RESP charge fit, and force constants are obtained through rewriting of either prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3b0e7b3fbfcd9a494f538c1869102b9
https://pubmed.ncbi.nlm.nih.gov/32672967
https://pubmed.ncbi.nlm.nih.gov/32672967
Publikováno v:
Biochemistry. 57:295-299
The bioluminescence reaction in dinoflagellates involves the oxidation of an open-chain tetrapyrrole by the enzyme dinoflagellate luciferase (LCF). The activity of LCF is tightly regulated by pH, where the enzyme is essentially inactive at pH ∼8 an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c27f79ff5882c8b47166d4f9ef94951e
https://doi.org/10.1021/acs.biochem.7b00873
https://doi.org/10.1021/acs.biochem.7b00873
Autor:
Steven O. Mansoorabadi, Phong D. Ngo
Publikováno v:
ChemPhotoChem. 1:383-387
Ubiquitous in the world's oceans, dinoflagellates are capable of fantastic displays of bright blue bioluminescence. This luminosity is a consequence of the oxidation of an open-chain tetrapyrrole, dinoflagellate luciferin (LH2), by the enzyme dinofla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ed973e088e9664ecde785f9e3ea02bba
https://doi.org/10.1002/cptc.201700060
https://doi.org/10.1002/cptc.201700060
Publikováno v:
Biochemistry
Oxalate:ferredoxin oxidoreductase (OOR) is an unusual member of the thiamine pyrophosphate (TPP)-dependent 2-oxoacid:ferredoxin oxidoreductase (OFOR) family in that it catalyzes the coenzyme A (CoA)-independent conversion of oxalate into 2 equivalent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6e2ed59479e187bc706a44e4912f45d
https://doi.org/10.1021/acs.biochem.7b00222
https://doi.org/10.1021/acs.biochem.7b00222
Publikováno v:
Science. 354:339-342
Methyl-coenzyme M reductase (MCR) is the key enzyme of methanogenesis and anaerobic methane oxidation. The activity of MCR is dependent on the unique nickel-containing tetrapyrrole known as coenzyme F430. We used comparative genomics to identify the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97c23bd547e891ea2862b8e16a96be55
https://doi.org/10.1126/science.aag2947
https://doi.org/10.1126/science.aag2947
Publikováno v:
Encyclopedia of Inorganic and Bioinorganic Chemistry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::817b343fc41d635d01c96da69a6ca0c7
https://doi.org/10.1002/9781119951438.eibc2488
https://doi.org/10.1002/9781119951438.eibc2488
Autor:
Meilan Wu, Peng Gao, Zhihua Tao, Hung-wen Liu, Steven O. Mansoorabadi, Liang Guo, Sai Venkatesh Pingali
Publikováno v:
Biochemistry
Poly(ADP-ribose) polymerase-1 (PARP-1) is a nuclear protein that plays key roles in several fundamental cellular processes. PARP-1 catalyzes the polymerization of nicotinamide adenine dinucleotide on itself and other acceptor proteins, forming long b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1cbe29832d57ccd16ea8078c6d49bf2
https://doi.org/10.1021/bi401439n
https://doi.org/10.1021/bi401439n
Autor:
Jake LeVieux, Reid M. McCarty, Steven O. Mansoorabadi, Yung Nan Liu, Yasushi Ogasawara, Hak Joong Kim, Hung-wen Liu
Publikováno v:
Journal of the American Chemical Society. 135:8093-8096
The existence of cobalamin (Cbl)-dependent enzymes that are members of the radical S-adenosyl-l-methionine (SAM) superfamily was previously predicted on the basis of bioinformatic analysis. A number of these are Cbl-dependent methyltransferases, but
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43f61af5a1ec3f49baf164fc3f018f5f
https://doi.org/10.1021/ja312641f
https://doi.org/10.1021/ja312641f