Zobrazeno 1 - 10
of 52
pro vyhledávání: '"William N. Lanzilotta"'
Autor:
Jonathan V. Dietz, Mathilda M. Willoughby, Robert B. Piel, III, Teresa A. Ross, Iryna Bohovych, Hannah G. Addis, Jennifer L. Fox, William N. Lanzilotta, Harry A. Dailey, James A. Wohlschlegel, Amit R. Reddi, Amy E. Medlock, Oleh Khalimonchuk
Publikováno v:
Redox Biology, Vol 46, Iss , Pp 102125- (2021)
Heme is an essential cofactor required for a plethora of cellular processes in eukaryotes. In metazoans the heme biosynthetic pathway is typically partitioned between the cytosol and mitochondria, with the first and final steps taking place in the mi
Externí odkaz:
https://doaj.org/article/b5b8982ff5e84ce3a38023b6ecfea0bd
Publikováno v:
Biochemistry. 62:1191-1196
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::32518892191d8a5a412354179a283b20
https://doi.org/10.1021/acs.biochem.2c00474
https://doi.org/10.1021/acs.biochem.2c00474
Autor:
Liju G. Mathew, Dominik K. Haja, Clayton Pritchett, Winston McCormick, Robbie Zeineddine, Leo S. Fontenot, Mario E. Rivera, John Glushka, Michael W. W. Adams, William N. Lanzilotta
Publikováno v:
J Biol Inorg Chem
Five tungstopterin-containing oxidoreductases were characterized from the hyperthermophile Pyrococcus furiosus. Each enzyme catalyzes the reversible conversion of one or more aldehydes to the corresponding carboxylic acid, but they have different spe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::344eddf2d44d509e6d0c71c885c079dd
https://europepmc.org/articles/PMC10293930/
https://europepmc.org/articles/PMC10293930/
Autor:
Jeong Yeh Yang, Jeremy L. Praissman, William N. Lanzilotta, Digantkumar Chapla, Stephanie M. Halmo, Lance Wells, Danish Singh, Kelley W. Moremen
Publikováno v:
Acta Crystallogr D Struct Biol
The canonical O-mannosylation pathway in humans is essential for the functional glycosylation of α-dystroglycan. Disruption of this post-translational modification pathway leads to congenital muscular dystrophies. The first committed step in the con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff7326c4c34501a64be5101443d29689
https://doi.org/10.1107/s2059798321001261
https://doi.org/10.1107/s2059798321001261
Publikováno v:
Biochemistry
Increasing antibiotic resistance, and a growing recognition of the importance of the human microbiome, demand that new therapeutic targets be identified. Characterization of metabolic pathways that are unique to enteric pathogens represents a promisi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89e9d46b5565c613d4443a2f5c07eb9b
https://doi.org/10.1021/acs.biochem.0c00950
https://doi.org/10.1021/acs.biochem.0c00950
Insight into the Function of Active Site Residues in the Catalytic Mechanism of Human Ferrochelatase
Autor:
Harry A. Dailey, Wided Najahi-Missaoui, Mesafint T. Shiferaw, Amy E. Medlock, Angela N. Albetel, William N. Lanzilotta
Publikováno v:
Biochem J
Ferrochelatase catalyzes the insertion of ferrous iron into a porphyrin macrocycle to produce the essential cofactor, heme. In humans this enzyme not only catalyzes the terminal step, but also serves a regulatory step in the heme synthesis pathway. O
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::132eb0c55547d6c359416bfc51548459
https://europepmc.org/articles/PMC9138182/
https://europepmc.org/articles/PMC9138182/
Publikováno v:
Biochemistry. 58:4641-4654
ChuW, ChuX, and ChuY are contiguous genes downstream from a single promoter that are expressed in the enteric pathogen Escherichia coli O157:H7 when iron is limiting. These genes, and the corresponding proteins, are part of a larger heme uptake and u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::283e3a92760ae954f14d7e3aca82b3d9
https://doi.org/10.1021/acs.biochem.9b00841
https://doi.org/10.1021/acs.biochem.9b00841
Publikováno v:
ACS Bio & Med Chem Au. 2:655-655
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4534a22f5af3a0a890658e19466c68b7
https://doi.org/10.1021/acsbiomedchemau.2c00025
https://doi.org/10.1021/acsbiomedchemau.2c00025
Publikováno v:
J Inorg Biochem
Radical S-adenosylmethionine (SAM) enzymes utilize a [4Fe-4S](1+) cluster and S-(5′-adenosyl)-L-methionine, (SAM), to generate a highly reactive radical and catalyze what is arguably the most diverse set of chemical reactions for any known enzyme f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb1a036650162428ca5902639bbfc166
https://doi.org/10.1016/j.jinorgbio.2021.111636
https://doi.org/10.1016/j.jinorgbio.2021.111636
Autor:
Alecia T. Dent, Therese Albert, Marley Brimberry, Pierre Moënne-Loccoz, A Wilks, William N. Lanzilotta
Publikováno v:
Biochemistry. 60:2844-2844
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3a0228f1d85814558a52f3c0a74e2230
https://doi.org/10.1021/acs.biochem.1c00597
https://doi.org/10.1021/acs.biochem.1c00597