Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Christine L. Hagan"'
Autor:
Erin M. Flaherty, Christopher J. Woodilla, Cameron L. Curley, Thomas P. Fedrigoni, Christine L. Hagan
Publikováno v:
Biochemistry. 60(39)
Contact-dependent inhibition (CDI) is a mechanism of interbacterial competition in Gram-negative bacteria. The critical component of CDI systems is a large protein named CdiA; it forms a filament on the bacterial cell surface and contains a toxin dom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12ea1c5f169b03bc28ff97095dd9188d
https://pubmed.ncbi.nlm.nih.gov/34541845
https://pubmed.ncbi.nlm.nih.gov/34541845
Autor:
David Tomasek, Marcin Grabowicz, Thomas J. Silhavy, Christine L. Hagan, Joseph S. Wzorek, Michael D. Mandler, Daniel Kahne, James Lee, Elizabeth M. Hart, Mary D May, Holly A. Sutterlin
Publikováno v:
Proceedings of the National Academy of Sciences. 115:2359-2364
The β-barrel assembly machine (Bam) complex folds and inserts integral membrane proteins into the outer membrane of Gram-negative bacteria. The two essential components of the complex, BamA and BamD, both interact with substrates, but how the two co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e31d4feedd5d8c18c61981536bdfa67c
https://doi.org/10.1073/pnas.1711727115
https://doi.org/10.1073/pnas.1711727115
Publikováno v:
Proceedings of the National Academy of Sciences. 112:2011-2016
The protein complex that assembles integral membrane β-barrel proteins in the outer membranes of Gram-negative bacteria is an attractive target in the development of new antibiotics. This complex, the β-barrel assembly machine (Bam), contains two e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7085fda14bfdb1c2fdfb330d4d20a247
https://doi.org/10.1073/pnas.1415955112
https://doi.org/10.1073/pnas.1415955112
The Bam complex assembles β-barrel proteins into the outer membrane (OM) of Gram-negative bacteria. These proteins comprise cylindrical β-sheets with long extracellular loops and create pores to allow passage of nutrients and waste products across
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8aae7ec2c17dd80161ed80279d485a4e
https://europepmc.org/articles/PMC5347601/
https://europepmc.org/articles/PMC5347601/
Publikováno v:
Biochemistry. 52:6108-6113
The Bam machine assembles β-barrel membrane proteins into the outer membranes of Gram-negative bacteria. The central component of the Bam complex, BamA, is a β-barrel that is conserved in prokaryotes and eukaryotes. We have previously reported an i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d420c64ba361b203cfb0d567e6eb725a
https://doi.org/10.1021/bi400865z
https://doi.org/10.1021/bi400865z
Autor:
Janet R. Kumita, Christine L. Hagan, Mireille Dumoulin, Mark R. Wilson, Carol V. Robinson, Gemma L. Caddy, Justin J. Yerbury, Stephen Poon, Elise M. Stewart, Christopher M. Dobson
We have studied the effects of the extracellular molecular chaperone, clusterin, on the in vitro aggregation of mutational variants of human lysozyme, including one associated with familial amyloid disease. The aggregation of the amyloidogenic varian
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::283c3ad3c4acbcc560204431876758f3
https://doi.org/10.1016/j.jmb.2007.02.095
https://doi.org/10.1016/j.jmb.2007.02.095
Autor:
Minkoo, Ahn, Christine L, Hagan, Ana, Bernardo-Gancedo, Erwin, De Genst, Francisco N, Newby, John, Christodoulou, Anne, Dhulesia, Mireille, Dumoulin, Carol V, Robinson, Christopher M, Dobson, Janet R, Kumita
Publikováno v:
Biophysical journal. 111(11)
The conversion of human lysozyme into amyloid fibrils is associated with a rare but fatal hereditary form of nonneuropathic systemic amyloidosis. The accumulation of large amounts of aggregated protein is thought to be initiated by the formation of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ac943af1bf6f9b74763dde90ba6632db
https://pubmed.ncbi.nlm.nih.gov/27926837
https://pubmed.ncbi.nlm.nih.gov/27926837
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 109(9)
The outer membrane (OM) of Gram-negative bacteria such as Escherichia coli contains lipoproteins and integral β-barrel proteins (outer-membrane proteins, OMPs) assembled into an asymmetrical lipid bilayer. Insertion of β-barrel proteins into the OM
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b66771120c591aa632d0734fd6eb43fb
https://pubmed.ncbi.nlm.nih.gov/22331884
https://pubmed.ncbi.nlm.nih.gov/22331884
Autor:
Christine L. Hagan, Daniel Kahne
β-barrel proteins are folded and inserted into the outer membranes of E. coli by the multi-protein Bam complex. The Bam complex has been purified and functionally reconstituted in vitro. Here we report assay conditions for this reconstitution that i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c7a1ad2b79beb90a75df9683bfd1fe8
https://europepmc.org/articles/PMC3192448/
https://europepmc.org/articles/PMC3192448/
Publikováno v:
Annual review of biochemistry. 80
β-barrel membrane proteins perform important functions in the outer membranes (OMs) of Gram-negative bacteria and of the mitochondria and chloroplasts of eukaryotes. The protein complexes that assemble these proteins in their respective membranes ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6fce621891dba98ea2ba830bc308d33
https://pubmed.ncbi.nlm.nih.gov/21370981
https://pubmed.ncbi.nlm.nih.gov/21370981