Zobrazeno 1 - 7 of 7 pro vyhledávání: '"Katharina H. Surinya"'
1
Disulfide-containing peptides from the glandular skin secretions of froglets of the genus Crinia: Structure, activity and evolutionary trends
Autor: Ian F. Musgrave, John H. Bowie, Tara L. Pukala, Michael J. Tyler, Jason Doyle, Rebecca J. Jackway, Vita M. Maselli, Stephen C. Donnellan, Katharina H. Surinya-Johnson, Yanqin Liu, Lyndon E. Llewellyn
Publikováno v: Regulatory Peptides. 151:80-87
The skin secretions of Crinia signifera, C. riparia and C. deserticola contain bioactive disulfide-containing peptides. Signiferin 1 (RLCIPYIIPC-OH) from C. signifera and C. deserticola) contracts smooth muscle at a concentration of 10(-9) M, and eff
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ccc2c207ee62584467a474227d47bf3
https://doi.org/10.1016/j.regpep.2008.06.004
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2
An Investigation of the Ligand Binding Properties and Negative Cooperativity of Soluble Insulin-like Growth Factor Receptors
Autor: John C. Wallace, Leah J. Cosgrove, Filomena Occhiodoro, Katharina H. Surinya, Geoffrey L. Francis, Grant W. Booker, Kenneth Siddle, Briony E. Forbes
Publikováno v: Journal of Biological Chemistry. 283:5355-5363
To investigate the interaction of the insulin-like growth factor (IGF) ligands with the insulin-like growth factor type 1 receptor (IGF-1R), we have generated two soluble variants of the IGF-1R. We have recombinantly expressed the ectodomain of IGF-1
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4fe994827a26cf3013af4d29fb6cf527
https://doi.org/10.1074/jbc.m707054200
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3
Conserved Glu40 and Glu433 of the biotin carboxylase domain of yeast pyruvate carboxylase I isoenzyme are essential for the association of tetramers
Autor: Abdussalam Adina-Zada, Steven W. Polyak, W. Wallace Cleland, Grant W. Booker, Katharina H. Surinya, Sarawut Jitrapakdee, Cvetan Stojkoski, Paul V. Attwood, Roger Smyth, John C. Wallace
Publikováno v: The International Journal of Biochemistry & Cell Biology. 39:2120-2134
The native form of pyruvate carboxylase is an alpha4 tetramer but the tetramerisation domain of each subunit is currently unknown. To identify this domain we co-expressed yeast pyruvate carboxylase 1 isozyme (Pyc1) with an N-terminal myc tag, togethe
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61581fbd23fe8830b1afd16e28f94c2e
https://doi.org/10.1016/j.biocel.2007.06.006
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4
Transcriptional Regulation of the Human Erythroid 5-Aminolevulinate Synthase Gene
Autor: Brian K. May, Timothy C. Cox, Katharina H. Surinya
Publikováno v: Journal of Biological Chemistry. 272:26585-26594
We have characterized the 5′-flanking region of the human erythroid-specific 5-amino levulinate synthase (ALAS) gene (the ALAS2 gene) and shown that the first 300 base pairs of promoter sequence gives maximal expression in erythroid cells. Transcri
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::39afb158e63f21440522cf8d073307ec
https://doi.org/10.1074/jbc.272.42.26585
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5
Host-defence peptide profiles of the skin secretions of interspecific hybrid tree frogs and their parents, female Litoria splendida and male Litoria caerulea
Autor: Steve Donnellan, Rebecca J. Jackway, John H. Bowie, Jason Doyle, Terry Bertozzi, Tara L. Pukala, Lyndon E. Llewellyn, Michael J. Tyler, Katharina H. Surinya-Johnson, Yanquin Liu
Publikováno v: The FEBS journal. 273(15)
Five healthy adult female first-generation hybrid tree frogs were produced by interspecific breeding of closely related tree frogs Litoria splendida and L. caerulea in a cage containing large numbers of males and females of both species. Phylogenetic
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f8c7dc5784f47a43311a56b96f5ff17
https://pubmed.ncbi.nlm.nih.gov/16824041
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6
Identification and characterization of a conserved erythroid-specific enhancer located in intron 8 of the human 5-aminolevulinate synthase 2 gene
Autor: Brian K. May, Timothy C. Cox, Katharina H. Surinya
Publikováno v: The Journal of biological chemistry. 273(27)
Thirty five kilobases of sequence encompassing the human erythroid 5-aminolevulinate synthase (ALAS2) gene have been determined. Analysis revealed a very low GC content, few repetitive elements, and evidence for the insertion of a reverse-transcribed
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2780ebcbba7f843c13127e4189483291
https://pubmed.ncbi.nlm.nih.gov/9642238
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