Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Lars Skjeldal"'
Publikováno v:
Biochemical and Biophysical Research Communications. 435:202-208
Sorbitol dehydrogenase inhibitors have been found to prevent, or alleviate, various secondary complications of diabetes mellitus. In the present study, the effects of nucleosides and nucleotides on the rate of sorbitol oxidation catalyzed by the shee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50c72633d3835f6e0f8d049c1e2a3eb8
https://doi.org/10.1016/j.bbrc.2013.04.081
https://doi.org/10.1016/j.bbrc.2013.04.081
Publikováno v:
Chemistry & Biodiversity. 5:2014-2022
A new isolation procedure for Kalata polypeptides from the tropical plant Oldenlandia affinis DC is described. Fractions were screened by thin-layer chromatography, and Van Urk positive fractions were tested for oxytocic activity in estrogenized rat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de44360244e374fd3bc5864390df61e6
https://doi.org/10.1002/cbdv.200890184
https://doi.org/10.1002/cbdv.200890184
Autor:
Zakhar O. Shenkarev, Alexander S. Arseniev, Lars Skjeldal, Kirill D. Nadezhdin, Vladimir A. Sobol, Ekaterina N. Lyukmanova
Publikováno v:
Journal of Inorganic Biochemistry. 102:1246-1256
The cyclotides are the family of hydrophobic bioactive plant peptides, characterized by a circular protein backbone and three knot forming disulfide bonds. It is believed that membrane activity of the cyclotides underlines their antimicrobial, cytoto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c86b3775e727e30fcac60543a7ae6a8f
https://doi.org/10.1016/j.jinorgbio.2008.01.018
https://doi.org/10.1016/j.jinorgbio.2008.01.018
Autor:
Sunithi Gunasekera, Lars Skjeldal, Nathalie Grob, Adam A. Strömstedt, Ulf Göransson, Per Eugen Kristiansen
Publikováno v:
Biochimica et biophysica acta. 1858(6)
The cyclic cystine knot plant peptides called cyclotides are active against a wide variety of organisms. This is primarily achieved through membrane binding and disruption, in part deriving from a high affinity for phosphatidylethanolamine (PE) lipid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd4fb9a0efe1e0e1def47fde81603c32
https://pubmed.ncbi.nlm.nih.gov/26878982
https://pubmed.ncbi.nlm.nih.gov/26878982
Autor:
Lars Skjeldal, Julija Romanuka, Sudarslal Sadasivan Nair, Alan G. Marshall, Carol L. Nilsson, Mark R. Emmett, Martin Billeter
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1764:1568-1576
Kalata peptides are isolated from an African medicinal plant, Oldenlandia affinis, an aqueous decoction of which can be ingested to accelerate uterine contraction during childbirth. The closely packed disulfide core of kalata peptides confers unusual
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5349dc1a56eba3f7ceeb946715bc0054
https://doi.org/10.1016/j.bbapap.2006.07.009
https://doi.org/10.1016/j.bbapap.2006.07.009
Autor:
Alexander S. Arseniev, A.G. Sobol, Zakhar O. Shenkarev, Kirill D. Nadezhdin, Vladimir A. Sobol, Lars Skjeldal
Publikováno v:
FEBS Journal. 273:2658-2672
Cyclotides are a family of bioactive plant peptides that are characterized by a circular protein backbone and three conserved tightly packed disulfide bonds. The antimicrobial and hemolytic properties of cyclotides, along with the relative hydrophobi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::835426cf70198dd7c4cb6d7443625fc1
https://doi.org/10.1111/j.1742-4658.2006.05282.x
https://doi.org/10.1111/j.1742-4658.2006.05282.x
Autor:
Jurgen F. Doreleijers, Luke A. Moe, John L. Markley, Brian F. Volkman, William M. Westler, Francis C. Peterson, Lars Skjeldal, Brian G. Fox, Jeremie D. Pikus
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 9:945-953
Toluene 4-monooxygenase, a four-protein complex from Pseudomonas mendocina KR1, catalyzes the NADH- and O(2)-dependent hydroxylation of toluene to form p-cresol. The solution structure of the 112-amino-acid Rieske ferredoxin component, T4moC, was det
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40291aa969035a450b2e806af75c8364
https://doi.org/10.1007/s00775-004-0594-4
https://doi.org/10.1007/s00775-004-0594-4
Autor:
Anne Carine Østvold, Tormod Skauge, Lars Skjeldal, Henrik W. Anthonsen, Kirsten Grundt, Henrik S. Huitfeldt
Publikováno v:
Archives of Biochemistry and Biophysics. 407:168-175
We have studied the DNA-binding properties of a NUCKS-derived, synthetic peptide containing an extended GRP motif. This peptide binds to random-sequence DNA, but did not bind preferentially to poly(dA–dT). A synthetic peptide with the same amino ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3da3b5da0b26966de3842c1872ab4f03
https://doi.org/10.1016/s0003-9861(02)00513-1
https://doi.org/10.1016/s0003-9861(02)00513-1
Publikováno v:
JBIC Journal of Biological Inorganic Chemistry. 7:810-814
Carbon monoxide dehydrogenase (CODH) from Rhodospirillum rubrum reversibly catalyzes the oxidation of CO to CO(2) at the active site C-cluster. In this article, the reduction of CO(2) to formate is reported as a slow side reaction catalyzed by both N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50e0196cb9dba87722324404fa5f16fe
https://doi.org/10.1007/s00775-002-0365-z
https://doi.org/10.1007/s00775-002-0365-z
Autor:
Thorny Cecilie Bie, Andersen, Kjersti, Lindsjø, Cecilie Dahl, Hem, Lise, Koll, Per Eugen, Kristiansen, Lars, Skjeldal, Amy H, Andreotti, Anne, Spurkland
Publikováno v:
BMC Biotechnology
Background Signalling proteins often contain several well defined and conserved protein domains. Structural analyses of such domains by nuclear magnetic spectroscopy or X-ray crystallography may greatly inform the function of proteins. A limiting ste
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7687b6ee37ab05702c7335649bb588c8
https://pubmed.ncbi.nlm.nih.gov/24423197
https://pubmed.ncbi.nlm.nih.gov/24423197