Results 71 to 80 of about 1,225 (122)

Kampen om det 'naturlige'(anm.)

open access: yesKvinder, Køn & Forskning, 2000
Bryld, Mette, Lykke, Nina
openaire   +1 more source

Environmental regulation of the anaerobic oxidation of methane: a comparison of ANME‐I and ANME‐II communities

open access: yesEnvironmental Microbiology, 2004
Summary The anaerobic oxidation of methane (AOM) is one of the major sinks for methane on earth and is known to be mediated by at least two phylogenetically different groups of anaerobic methanotrophic Archaea (ANME‐I and ANME‐II).
Nauhaus, K.   +3 more
openaire   +4 more sources

Phylogenetic and functional diverse ANME-1 thrive in Arctic hydrothermal vents. [PDF]

open access: yesFEMS Microbiology Ecology, 2022
The methane-rich areas, the Loki's Castle vent field and the Jan Mayen vent field at the Arctic Mid Ocean Ridge (AMOR), host abundant niches for anaerobic methane-oxidizers, which are predominantly filled by members of the ANME-1.
Cedric Jasper Hahn   +2 more
exaly   +2 more sources

Evolutionary diversification of methanotrophic ANME-1 archaea and their expansive virome [PDF]

open access: yesNature Microbiology, 2023
ANME-1 archaea are important because of their ability to metabolize methane through anaerobic oxidation. Here the authors use metagenomics on hydrothermal samples from the Gulf of California to characterize a family of ANME-1 and its virome.
Mart Krupovic   +2 more
exaly   +3 more sources

Composition and Metabolic Potential of Fe(III)-Reducing Enrichment Cultures of Methanotrophic ANME-2a Archaea and Associated Bacteria

open access: yesMicroorganisms, 2023
The key microbial group involved in anaerobic methane oxidation is anaerobic methanotrophic archaea (ANME). From a terrestrial mud volcano, we enriched a microbial community containing ANME-2a, using methane as an electron donor, Fe(III) oxide ...
Alexandra Klyukina, Alexander Merkel
exaly   +2 more sources

Enrichment of ANME-1 from Eckernförde Bay sediment on thiosulfate, methane and short-chain fatty acids

open access: yesJournal of Biotechnology, 2012
The microorganisms involved in sulfate-dependent anaerobic oxidation of methane (AOM) have not yet been isolated. In an attempt to stimulate the growth of anaerobic methanotrophs and associated sulfate reducing bacteria (SRB), Eckernförde Bay sediment ...
Alfons Stams   +2 more
exaly   +2 more sources

Evaluation and optimization of PCR primers for selective and quantitative detection of marine ANME subclusters involved in sulfate-dependent anaerobic methane oxidation [PDF]

open access: yesApplied Microbiology and Biotechnology, 2017
Since the discovery that anaerobic methanotrophic archaea (ANME) are involved in the anaerobic oxidation of methane coupled to sulfate reduction in marine sediments, different primers and probes specifically targeting the 16S rRNA gene of these archaea ...
Alfons Stams   +2 more
exaly   +2 more sources
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ANM: Automated network management system

IEEE Network, 1988
A description is given of the automated network management (ANM) system, which assists the network operator and analyst in understanding and controlling complex internets. The ANM system provides an integrated set of tools for real-time monitoring, control, and analysis of internets consisting of diverse network entities such as internet gateways ...
Mertin Feridun   +3 more
openaire   +1 more source

Subgroup Characteristics of Marine Methane-Oxidizing ANME-2 Archaea and Their Syntrophic Partners as Revealed by Integrated Multimodal Analytical Microscopy.

open access: yesApplied and Environmental Microbiology, 2018
Phylogenetically diverse environmental ANME archaea and sulfate-reducing bacteria cooperatively catalyze the anaerobic oxidation of methane oxidation (AOM) in multicelled consortia within methane seep environments.
Victoria Orphan   +2 more
exaly   +2 more sources

Repurposing AS1411 for constructing ANM-PROTACs

Cell Chemical Biology
Proteolysis-targeting chimeras (PROTACs) are heterobifunctional molecules consisting of two ligands joined by a linker, enabling them to simultaneously bind with an E3 ligase and a protein of interest (POI) and trigger proteasomal degradation of the POI.
Xuekun, Fu   +12 more
openaire   +2 more sources

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