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pro vyhledávání: '"MIERKE, D. F."'
Autor:
Sun, C.1, Mierke, D. F.1,2 dale_mierke@brown.edu
Publikováno v:
Journal of Peptide Research. Mar2005, Vol. 65 Issue 3, p411-417. 7p.
Autor:
Saviano M., Isernia C., Bassarello C., Di Lello P., Mierke D. F., GALDIERO, STEFANIA, BENEDETTI, ETTORE, PEDONE, CARLO
Publikováno v:
The journal of peptide research : official journal of the American Peptide Society. 65(2)
The Antennapedia homeodomain structure consists of four helices. The helices II and III are connected by a tripeptide that forms a turn, and constitute the well-known helix-turn-helix motif. The recognition helix penetrates the DNA major groove, give
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::634397a02c8a749e17487f46ff453797
https://pubmed.ncbi.nlm.nih.gov/15705164
https://pubmed.ncbi.nlm.nih.gov/15705164
The heptadecapeptides bombolitin I and bombolitin III are two members of a series of biologically active peptides postulated to be membrane active. In order to understand the effects of the membrane on the secondary structure of the peptides, we have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10561::336ee464384d59a3f1e10ac9fa203af8
http://olympias.lib.uoi.gr/jspui/handle/123456789/22845
http://olympias.lib.uoi.gr/jspui/handle/123456789/22845
The heptadecapeptides bombolitin I and bombolitin III are two of a series of peptides postulated to be biologically active within a membrane environment. In the preceding paper [Bairaktari, E., Mierke, D.F., Mammi, S., & Peggion, E. (1990) Biochemist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10561::f4daaf4fdab5b2ecbe4e9876cc5219cd
http://olympias.lib.uoi.gr/jspui/handle/123456789/22844
http://olympias.lib.uoi.gr/jspui/handle/123456789/22844
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