Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Helga Plagens"'
Publikováno v:
Nucleic Acids Research. 25:701-712
The sequenced genomes of the two closely related bacteria Mycoplasma genitalium and Mycoplasma pneumoniae were compared with emphasis on genome organization and coding capacity. All the 470 proposed open reading frames (ORFs) of the smaller M.genital
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1078a36fe86967e043f9f4edbb3e0dc6
https://doi.org/10.1093/nar/25.4.701
https://doi.org/10.1093/nar/25.4.701
Publikováno v:
Nucleic Acids Research. 24:4420-4449
The entire genome of the bacterium Mycoplasma pneumoniae M129 has been sequenced. It has a size of 816,394 base pairs with an average G+C content of 40.0 mol%. We predict 677 open reading frames (ORFs) and 39 genes coding for various RNA species. Of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9812d0bc608edfc4850eef770c1fbe37
https://doi.org/10.1093/nar/24.22.4420
https://doi.org/10.1093/nar/24.22.4420
Publikováno v:
Gene. 171(1)
The gene coding for the P200 protein of the bacterium, Mycoplasma pneumoniae (Mp), was cloned and sequenced. The sequence-derived data and biochemical data indicated that P200 has several features in common with the well characterized cytadherence-as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f4a3bd50af6b46acf2de524de8d4e92
https://pubmed.ncbi.nlm.nih.gov/8675035
https://pubmed.ncbi.nlm.nih.gov/8675035
Autor:
Richard Herrmann, Laurie Barsh Dirksen, Helmut Hilbert, Thomas Proft, Helga Plagens, Duncan C. Krause
Publikováno v:
Gene. 171(1)
Mycoplasma pneumoniae (Mp) cytadherence requires the proper anchoring of cytadhesin proteins in the mycoplasmal membrane at an attachment organelle through their interaction with a cytoskeleton-like network of accessory proteins that includes HMW1 an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::019ed3d4813568e3fe08f33dd461854d
https://pubmed.ncbi.nlm.nih.gov/8675025
https://pubmed.ncbi.nlm.nih.gov/8675025
Publikováno v:
Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 362:539-548
The sequence analysis of the monomeric hemoglobin CTT IV is given. The primary structure was determined by automatic Edman degradation of the protein and of peptides obtained by enzymatical or by chemical cleavages. The protein chain consists of 136
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c8af5fb8c40b9e7b6fbcb1247a6a6c59
https://doi.org/10.1515/bchm2.1981.362.1.539
https://doi.org/10.1515/bchm2.1981.362.1.539