Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Gity Behravan"'
Autor:
Jürgen Schleucher, Gity Behravan, Janusz Zdunek, Sybren S. Wijmenga, Per-Olof Lycksell, Martin Lundqvist, Hans Ippel, Göran Larsson
Publikováno v:
Journal of Molecular Biology. 288:689-703
The solution structure of the homeodomain of the rat insulin-gene enhancer protein isl-1. Comparison with other homeodomains.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2133d75f758484320b71885a74ed0cd9
https://doi.org/10.1006/jmbi.1999.2718
https://doi.org/10.1006/jmbi.1999.2718
Publikováno v:
Protein Engineering Design and Selection. 10:1327-1331
Isl-1 is a member of a family of Homeodomains containing proteins that possess an N-terminal pair of zinc binding LIM domains. The Isl-1 gene in rat codes for a protein that binds to the insulin gene enhancer and is also involved in regulation of amy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d753d02c8d0d39cf5f66a161d41705be
https://doi.org/10.1093/protein/10.11.1327
https://doi.org/10.1093/protein/10.11.1327
Publikováno v:
European Journal of Biochemistry. 211:821-827
The catalytic mechanism of carbonic anhydrase includes the reaction of a zinc-bound hydroxide ion with the CO2 substrate. This hydroxide ion is part of a hydrogen-bonded network involving the conserved amino acid residues Thr199, Glu106 and Tyr7. To
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2750ab3e140522fafa20b12f3be2ac3
https://doi.org/10.1111/j.1432-1033.1993.tb17614.x
https://doi.org/10.1111/j.1432-1033.1993.tb17614.x
Publikováno v:
European Journal of Biochemistry. 198:589-592
Site-specific mutagenesis has been used to replace amino acid residues in the active site of human carbonic anhydrase II with residues characterizing carbonic anhydrases I. Previous studies of [Thr200----His]isoenzyme II [Behravan, G., Jonsson, B.-H.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ff8220b548e4fe1cad31d6f91375153
https://doi.org/10.1111/j.1432-1033.1991.tb16054.x
https://doi.org/10.1111/j.1432-1033.1991.tb16054.x
Publikováno v:
European Journal of Biochemistry. 195:393-396
The active-site residue Thr200 in human carbonic anhydrase II has been replaced by several different amino acids by site-directed mutagenesis. The CO2 hydration and 4-nitrophenyl acetate hydrolase activities of these variants have been measured, as w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f2f67fcd7b27054db7ff7209d845a37
https://doi.org/10.1111/j.1432-1033.1991.tb15718.x
https://doi.org/10.1111/j.1432-1033.1991.tb15718.x
Autor:
Jürgen Schleucher, Janusz Zdunek, Göran Larsson, Martin Lundqvist, Sybren S. Wijmenga, Per-Olof Lycksell, Gity Behravan, Johannes H. Ippel
Publikováno v:
Journal of Biomolecular NMR. 12:357-359
Key words: Isl-1, homeodomain, protein, DNA-binding, NMR assignmentBiological contextTheinsulin geneenhancerbindingprotein, Isl-1, bindsspecifically to a transcription activation domain of theinsulin gene in rat (Karlsson et al., 1990), acts asa pos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d3c7bb852c68ee44810d563757e2795c
https://doi.org/10.1023/a:1008264829781
https://doi.org/10.1023/a:1008264829781
Publikováno v:
Biochimica et biophysica acta. 1264(3)
Mouse and Escherichia coli ribonucleotide reductases (RR) both belong to the same class of RR, where the enzyme consists of two non-identical subunits, proteins R1 and R2. A transient free radical was observed by EPR spectroscopy in the mouse RR reac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0596cb7b94e4ece164bb44cdb4f2ed85
https://pubmed.ncbi.nlm.nih.gov/8547320
https://pubmed.ncbi.nlm.nih.gov/8547320
Publikováno v:
Biochemistry. 34(13)
Mammalian ribonucleotide reductase consists of two nonidentical subunits, proteins R1 and R2, each inactive alone. The R1 protein binds the ribonucleotide substrates while the R2 protein contains a binuclear iron center and a tyrosyl free radical, es
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71a4415025d3d36abbacd661f3d56831
https://pubmed.ncbi.nlm.nih.gov/7703240
https://pubmed.ncbi.nlm.nih.gov/7703240
Publikováno v:
European journal of biochemistry. 190(2)
The active sites of carbonic anhydrases I contain a unique histidine residue at sequence position 200. To test the hypothesis that His200 is essential for the isoenzyme-specific catalytic and inhibitor-binding properties of carbonic anhydrases I, a v
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddaef5528485f6ce630aa349334060a9
https://pubmed.ncbi.nlm.nih.gov/2114290
https://pubmed.ncbi.nlm.nih.gov/2114290
Autor:
Cecilia Forsman, Gity Behravan, Annika Osterman, Bengt-Harald Jonsson, Curt R. Enzell, Jan-Eric Berg, Mihály Bartók, István Pelczer, György Dombi
Publikováno v:
Acta chemica Scandinavica. Series B: Organic chemistry and biochemistry. 42(5)
cDNA encoding human carbonic anhydrase II has been isolated and its nucleotide sequence determined. Expression of the isolated carbonic anhydrase gene in Escherichia coli from a plasmid containing the tac promoter yielded an active enzyme at a level
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d9a218c001c381b0a6f3d1904327f59
https://pubmed.ncbi.nlm.nih.gov/2850697
https://pubmed.ncbi.nlm.nih.gov/2850697