Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Gudmundur Eggertsson"'
Autor:
Gudmundur O. Hreggvidsson, Jakob K. Kristjansson, Gudmundur Eggertsson, Sigrídur H. Thorbjarnardóttir, Thorarinn Blondal, Snaedis H. Bjornsdottir, Solveig K. Petursdottir, Sigridur Hjorleifsdottir
Publikováno v:
Extremophiles. 10:1-16
Rhodothermus marinus has been the subject of many studies in recent years. It is a thermohalophilic bacterium and is the only validly described species in the genus Rhodothermus. It is not closely related to other well-known thermophiles and is the o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::467462c2918d5c1af11a119b278e8f68
https://doi.org/10.1007/s00792-005-0466-z
https://doi.org/10.1007/s00792-005-0466-z
Autor:
Snaedis H. Bjornsdottir, Sveinn Ernstsson, Astridur Palsdottir, Zophonías O. Jónsson, Sigrídur H. Thorbjarnardóttir, Gudmundur Eggertsson
Publikováno v:
Plasmid. 49:188-191
Here we report the identification and nucleotide sequence analysis of pRM21, a plasmid isolated from the thermophilic eubacterium Rhodothermus marinus. pRM21 consists of 2935 bp, has a G + C content of 58.2% and one major open reading frame whose ded
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c682cb8892abc5da9494da3515e772a0
https://doi.org/10.1016/s0147-619x(02)00152-x
https://doi.org/10.1016/s0147-619x(02)00152-x
Autor:
Sigrídur H. Thorbjarnardóttir, Gudmundur Eggertsson, Magnús M. Kristjánsson, Olafur T. Magnusson, Jóhanna Arnórsdóttir, Rúna B. Smáradóttir
Publikováno v:
European Journal of Biochemistry. 269:5536-5546
The gene encoding a subtilisin-like serine proteinase in the psychrotrophic Vibrio sp. PA44 has been successfully cloned, sequenced and expressed in Escherichia coli. The gene is 1593 basepairs and encodes a precursor protein of 530 amino acid residu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4055f05fb9c0dba1fcb3be8507db4531
https://doi.org/10.1046/j.1432-1033.2002.03259.x
https://doi.org/10.1046/j.1432-1033.2002.03259.x
Autor:
Olle Holst, S. Halldórsdóttir, Maher Abou-Hachem, S. H. Thorbjarnadóttir, Gudmundur O. Hreggvidsson, E. Nordberg Karlsson, K. B. Wicher, Gudmundur Eggertsson
Publikováno v:
Applied Microbiology and Biotechnology. 55:578-584
The thermostable cellulase Cel12A from Rhodothermus marinus was produced at extremely low levels when expressed in Escherichia coli and was cytotoxic to the cells. In addition, severe aggregation occurred when moderately high concentrations of the en
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec223339b2e81fbb74c7ef0e430bf2dc
https://doi.org/10.1007/s002530000559
https://doi.org/10.1007/s002530000559
Autor:
Gudmundur Eggertsson, Winston Lin, Dieter Söll, Constantinos Stathopoulos, David E. Graham, Ivana Celic, Ute C. Vothknecht, Kwang Won Hong, Tong Li, William B. Whitman, Paul J. Haney, Hyun Soo Kim, Makoto Kitabatake, Alan W. Curnow
Publikováno v:
FEBS Letters. 462:302-306
With the exception of the methanogenic archaea Methanococcus jannaschii and Methanobacterium thermoautotrophicum ΔH, all organisms surveyed contain orthologs of Escherichia coli cysteinyl-tRNA synthetase (CysRS). The characterization of CysRS-encodi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f31e968c27d484fdc25794d4df697df7
https://doi.org/10.1016/s0014-5793(99)01550-1
https://doi.org/10.1016/s0014-5793(99)01550-1
Autor:
Olafur H. Fridjonsson, Gudmundur O. Hreggvidsson, Gudmundur Eggertsson, Snaedis H. Bjornsdottir
The aim of this work was to develop an approach for chromosomal engineering of the thermophile Rhodothermus marinus . A selection strategy for R. marinus had previously been developed; this strategy was based on complementing a restriction-negative t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a5b7bd17349a883147b5b397035872c
https://europepmc.org/articles/PMC3147443/
https://europepmc.org/articles/PMC3147443/
Publikováno v:
Current Microbiology. 39:103-105
A Rhodothermus marinus gene, hemB, coding for 5-aminolevulinic acid (ALA) dehydratase (ALAD) has been cloned and sequenced. The reading frame of the hemB gene is 1020 base pairs encoding a protein of 340 amino acids with a calculated molecular mass o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::83d834baf4e1da269cdcd021934f7679
https://doi.org/10.1007/s002849900427
https://doi.org/10.1007/s002849900427
Autor:
Gudmundur Eggertsson, Sunna Helgadóttir, Magnús M. Kristjánsson, Sigrídur H. Thorbjarnardóttir, Jóhanna Arnórsdóttir
Publikováno v:
Biochimica et biophysica acta. 1774(6)
A subtilisin-like serine proteinase from a psychrotrophic Vibrio species (VPR) shows distinct cold adapted traits regarding stability and catalytic properties, while sharing high sequence homology with enzymes adapted to higher temperatures. Based on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b94110844315a3482e1cba92081b012
https://pubmed.ncbi.nlm.nih.gov/17490920
https://pubmed.ncbi.nlm.nih.gov/17490920
Publikováno v:
Extremophiles : life under extreme conditions. 11(2)
The construction of a shuttle cloning system for Rhodothermus marinus and Escherichia coli is described. It is based on the shuttle vector pRM3000, which contains a multiple cloning site as well as the shuttle marker trpB and TrpB(-) recipients of bo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99eb0a39c104206c6aa86d1795353119
https://pubmed.ncbi.nlm.nih.gov/17124556
https://pubmed.ncbi.nlm.nih.gov/17124556
Autor:
Gudmundur Eggertsson, E Kaiste, Olle Holst, Gudmundur O. Hreggvidsson, Jakob K. Kristjansson, Astridur Palsdottir
Publikováno v:
Scopus-Elsevier
An extracellular endo-β-1,4-glucanase purified from Rhodothermus marinus was active on carboxymethyl cellulose but not on Avicel, Sigmacell 10 cellulose, granular cellulose, p-nitrophenyl-β-D-cellobioside, or 4-methylumbelliferyl-β-D-eellobioside.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1d07e161e0c98f4dec15059218fc2c0
https://doi.org/10.1128/.62.8.3047-3049.1996
https://doi.org/10.1128/.62.8.3047-3049.1996