Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Joseph M, Pennington"'
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Siroheme is an essential bacterial iron tetrapyrrole used by siroheme-dependent sulfite and nitrite reductases. Here the authors shed light on the catalytic mechanisms of siroheme synthase through the structures of the bifunctional dehydrogenase/chel
Externí odkaz:
https://doaj.org/article/ea8b31747188498a8b3a178dfb2ba7c0
Autor:
Ahmed S. Fahad, Morgan R. Timm, Bharat Madan, Katherine E. Burgomaster, Kimberly A. Dowd, Erica Normandin, Matías F. Gutiérrez-González, Joseph M. Pennington, Matheus Oliveira De Souza, Amy R. Henry, Farida Laboune, Lingshu Wang, David R. Ambrozak, Ingelise J. Gordon, Daniel C. Douek, Julie E. Ledgerwood, Barney S. Graham, Leda R. Castilho, Theodore C. Pierson, John R. Mascola, Brandon J. DeKosky
Publikováno v:
Frontiers in Immunology, Vol 12 (2021)
The re-emergence of Zika virus (ZIKV) caused widespread infections that were linked to Guillain-Barré syndrome in adults and congenital malformation in fetuses, and epidemiological data suggest that ZIKV infection can induce protective antibody resp
Externí odkaz:
https://doaj.org/article/f95e6840712f42789ca64171182a652b
Autor:
Isabel Askenasy, M. Elizabeth Stroupe, Christopher B. Stanley, Angela M. Tavolieri, Lauren McGarry, Daniel T. Murray, Joseph M. Pennington
Publikováno v:
Journal of Structural Biology. 205:170-179
This is the first X-ray crystal structure of the monomeric form of sulfite reductase (SiR) flavoprotein (SiRFP-60) that shows the relationship between its major domains in an extended position not seen before in any homologous diflavin reductases. Sm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b3e4478b69ae5464a69316f5e0b2d9d
https://doi.org/10.1016/j.jsb.2019.01.001
https://doi.org/10.1016/j.jsb.2019.01.001
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
Nature Communications
Nature Communications
Siroheme is the central cofactor in a conserved class of sulfite and nitrite reductases that catalyze the six-electron reduction of sulfite to sulfide and nitrite to ammonia. In Salmonella enterica serovar Typhimurium, siroheme is produced by a trifu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d3602999edb265a1620a275c48c6a21
https://doi.org/10.1038/s41467-020-14722-1
https://doi.org/10.1038/s41467-020-14722-1
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1866:933-940
The siroheme-containing subunit from the multimeric hemoflavoprotein NADPH-dependent sulfite reductase (SiR/SiRHP) catalyzes the six electron-reduction of SO32- to S2-. Siroheme is an iron-containing isobacteriochlorin that is found in sulfite and ho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d27176f792d2d63bb58e2ce86228864b
https://doi.org/10.1016/j.bbapap.2018.05.013
https://doi.org/10.1016/j.bbapap.2018.05.013
Publikováno v:
Biophysical Journal. 118:534a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b7d0d2a69d6e85aa0dc4c54119fa442c
https://doi.org/10.1016/j.bpj.2019.11.2928
https://doi.org/10.1016/j.bpj.2019.11.2928
Autor:
Weifeng Shang, M. Elizabeth Stroupe, Isabel Askenasy, Yeqing Tao, Alan G. Marshall, Joseph M. Pennington, Nicolas L. Young
Publikováno v:
Journal of Biological Chemistry. 290:19319-19333
Assimilatory NADPH-sulfite reductase (SiR) from Escherichia coli is a structurally complex oxidoreductase that catalyzes the six-electron reduction of sulfite to sulfide. Two subunits, one a flavin-binding flavoprotein (SiRFP, the α subunit) and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bea116c8e24658deac150f3a938e0d18
https://doi.org/10.1074/jbc.m115.662379
https://doi.org/10.1074/jbc.m115.662379
Autor:
Deborah A. Sarkes, David A. Kingery, Joshua M. Kogot, Joseph M. Pennington, Dimitra N. Stratis-Cullum, Paul M. Pellegrino
Publikováno v:
Journal of Molecular Recognition
Bacterial peptide display libraries enable the rapid and efficient selection of peptides that have high affinity and selectivity toward their targets. Using a 15-mer random library on the outer surface of Escherichia coli (E.coli), high-affinity pept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ee89ab19fb2c35b4fc031742c4ecb18
https://doi.org/10.1002/jmr.2400
https://doi.org/10.1002/jmr.2400
Autor:
Joshua M. Kogot, Dimitra N. Stratis-Cullum, Joseph M. Pennington, Deborah A. Sarkes, Paul M. Pellegrino
Publikováno v:
Advances in Bioscience and Biotechnology. :40-45
Peptide biosensor reagents are emerging as an alternative to typical antibody-based detection methods. Peptides can be rapidly isolated using bacterial display methods for new and emerging biothreats and can be chemically synthesized for rapid, large
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2c28b2008db9c9aba1bcc42f9a8f7492
https://doi.org/10.4236/abb.2014.51007
https://doi.org/10.4236/abb.2014.51007
Publikováno v:
Biophysical Journal. 108(2)
Sulfur reduction is a fundamental biological process in most bacteria and plants. As a model system we study the Escherichia coli assimilatory sulfite reductase (aSiR), an ∼800kD complex that catalyzes the concerted six-electron reduction of sulfit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77858cd02563eae3dec9da79ba6c38f5