Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Julie Scanlan"'
Autor:
Julie Scanlan, Richard Guillonneau, Mark R. Cunningham, Sahanara Najmin, Michaela A. Mausz, Andrew Murphy, Leanne L. Murray, Limei Zhang, Deepak Kumaresan, Yin Chen
Publikováno v:
mBio, Vol 13, Iss 3 (2022)
ABSTRACT Methane is a potent greenhouse gas in the atmosphere, and its concentration has continued to increase in recent decades. Aerobic methanotrophs, bacteria that use methane as the sole carbon source, are an important biological sink for methane
Externí odkaz:
https://doaj.org/article/40e51c77d8814624bd170dec07c2b864
Autor:
Julie, Scanlan, Richard, Guillonneau, Mark R, Cunningham, Sahanara, Najmin, Michaela A, Mausz, Andrew, Murphy, Leanne L, Murray, Limei, Zhang, Deepak, Kumaresan, Yin, Chen
Publikováno v:
mBio. 13(3)
Methane is a potent greenhouse gas in the atmosphere, and its concentration has continued to increase in recent decades. Aerobic methanotrophs, bacteria that use methane as the sole carbon source, are an important biological sink for methane, and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d30215f5b648b43e5c7e58fdd0e4bd7a
https://pubmed.ncbi.nlm.nih.gov/35575546
https://pubmed.ncbi.nlm.nih.gov/35575546
Publikováno v:
Microbiology. 149:1771-1784
The methanotrophic bacteriumMethylosinus trichosporiumOB3b converts methane to methanol using two distinct forms of methane monooxygenase (MMO) enzyme: a cytoplasmic soluble form (sMMO) and a membrane-bound form (pMMO). The transcription of these two
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccd6399a277671d32888137e7f6f91a1
https://doi.org/10.1099/mic.0.26060-0
https://doi.org/10.1099/mic.0.26060-0
Autor:
Julie Scanlan, Stéphane Vuilleumier, Jeremy D. Semrau, Ashraf Y.Z. Khalifa, Brittani C. Freemeier, Bipin S. Baral, Alan A. DiSpirito, Sheeja Jagadevan, Alexey Vorobev, Daniel H. Haft, Nathan L. Bandow, Brandt H. Bergman, J. Colin Murrell
Publikováno v:
Environmental Microbiology.
Biological oxidation of methane to methanol by aerobic bacteria is catalysed by two different enzymes, the cytoplasmic or soluble methane monooxygenase (sMMO) and the membrane-bound or particulate methane monooxygenase (pMMO). Expression of MMOs is c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fc530ba43777ebea26426af488eebc28
https://doi.org/10.1111/1462-2920.12150
https://doi.org/10.1111/1462-2920.12150
Autor:
Jeremy D, Semrau, Sheeja, Jagadevan, Alan A, DiSpirito, Ashraf, Khalifa, Julie, Scanlan, Brandt H, Bergman, Brittani C, Freemeier, Bipin S, Baral, Nathan L, Bandow, Alexey, Vorobev, Daniel H, Haft, Stéphane, Vuilleumier, J Colin, Murrell
Publikováno v:
Environmental microbiology. 15(11)
Biological oxidation of methane to methanol by aerobic bacteria is catalysed by two different enzymes, the cytoplasmic or soluble methane monooxygenase (sMMO) and the membrane-bound or particulate methane monooxygenase (pMMO). Expression of MMOs is c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::486e427f4e7a116830527d41d902558c
https://pubmed.ncbi.nlm.nih.gov/23682956
https://pubmed.ncbi.nlm.nih.gov/23682956
Autor:
Gareth Jones, Ian Benton, Natalie Meara, Mithun Murthy, Elpida Phitidis, Stephen Scott, James Finnerty, Julie Scanlan
Publikováno v:
C38. ADVANCES IN ASTHMA AND COPD SCREENING AND MONITORING.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e29e52e5db4a2645841db9d840460bc9
https://doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4325
https://doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a4325
Autor:
Miriam Land, Mike S. M. Jetten, Natalia Mikhailova, Huzuki Teshima, Susan Lucas, K.D. Kits, Julie Scanlan, Lin Peters, Ioanna Pagani, Nikos C. Kyrpides, James Han, Alla Lapidus, Lisa Y. Stein, Cliff Han, Michael Cunliffe, Martin G. Klotz, Jan Fang Cheng, Rich Boden, Natalia Ivanova, Lauren Hauser, Stéphane Vuilleumier, Roxanne Tapia, Samuel Pitluck, Hélène Moussard, J. C. Murrell, Lynne Goodwin, T. Woyke
Publikováno v:
Journal of Bacteriology, 193, 24, pp. 7001-7002
Journal of Bacteriology, 193, 7001-7002
Journal of Bacteriology, 193, 7001-7002
Methylomonas methanica MC09 is a mesophilic, halotolerant, aerobic, methanotrophic member of the Gammaproteobacteria , isolated from coastal seawater. Here we present the complete genome sequence of this strain, the first available from an aerobic ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66560aeea323270a12ae3ffb545ff37c
https://hdl.handle.net/2066/91654
https://hdl.handle.net/2066/91654
Autor:
M. Tanvir Rahman, Yin Chen, J. Colin Murrell, Julie Scanlan, Andrew T. Crombie, Hendrik Schäfer, Lijiang Song
Methylocella silvestris BL2, a facultative methane utilizer, can grow on monomethylamine (MMA) as a sole carbon and nitrogen source. No activity of MMA dehydrogenase was detectable. Instead, this bacterium utilizes a methylated amino acid pathway (γ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e086589e3a5696ae752333e6786601c
https://europepmc.org/articles/PMC2897447/
https://europepmc.org/articles/PMC2897447/
Publikováno v:
FEMS microbiology letters. 301(2)
Methanotrophs oxidize methane to methanol using the enzyme methane monooxygenase. Methylosinus trichosporium OB3b has two such enzymes: a membrane-bound particulate methane monooxygenase (pMMO) and a soluble, cytoplasmic methane monooxygenase (sMMO).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dac766ca32f992c3c72b4cf1bb6c36cc
https://pubmed.ncbi.nlm.nih.gov/19878324
https://pubmed.ncbi.nlm.nih.gov/19878324
Publikováno v:
Microbiology (Reading, England). 152(Pt 10)
The soluble methane monooxygenase, (sMMO) is a key enzyme for methane oxidation, and is found in only some methanotrophs, including Methylosinus sporium 5. sMMO expression is regulated at the level of transcription from a sigma(54) promoter by a copp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77184d4b0d07574be9bc8647402f77a6
https://pubmed.ncbi.nlm.nih.gov/17005974
https://pubmed.ncbi.nlm.nih.gov/17005974