Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Paul Patrick James Dunn"'
Publikováno v:
Parasitology. 113:439-448
SUMMARYWe have isolated and sequenced cDNA clones fromEimeria tenellaandEimeria maximawhich encode proteins that share homology with a recently described family of calmodulin-domain protein kinases. The primary sequence data show that each of the pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a3d206287aae5b04db124615794006a4
https://doi.org/10.1017/s0031182000081506
https://doi.org/10.1017/s0031182000081506
Publikováno v:
Molecular and Biochemical Parasitology. 79:195-206
A 50 kDa acidic protein, which is found within the microneme organelles of Eimeria tenella sporozoites and merozoites and called E. tenella mic-2, was cloned by immunoscreening of a cDNA expression library. The expression of the protein and its mRNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb2e6764bbec946aa01c3a0bcb7ea982
https://doi.org/10.1016/0166-6851(96)02662-x
https://doi.org/10.1016/0166-6851(96)02662-x
Publikováno v:
Molecular and Biochemical Parasitology. 70:211-215
Heat-shock protein (hsp) are a large and ubiquitous family of polypeptides which have been well conserved in evolution and which have a number of cellular roles [1,2]. They are known to ‘chaperone’ the transport, folding and assembly of precursor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94c42a4e47d3fa21afe89999775f576c
https://doi.org/10.1016/0166-6851(95)00014-r
https://doi.org/10.1016/0166-6851(95)00014-r
Publikováno v:
Parasitology Research. 82:566-568
cDNA clones for homologues of a molecular chaperone of the endoplasmic reticulum called the immunoglobulin heavy-chain binding protein (BiP) have been isolated from Eimeria maxima and E. tenella sporozoite cDNA libraries. The E. tenella cDNA clone is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9440fafb1244c86f49a3114d1dc11ad5
https://doi.org/10.1007/s004360050163
https://doi.org/10.1007/s004360050163
Genomic organisation and developmentally regulated expression of an apicomplexan aspartyl proteinase
Autor:
Karen J. Billington, Rachel Ryan, Fiona M. Tomley, Paul Patrick James Dunn, Létitia Jean, Janene M. Bumstead, Pierre Péry
Publikováno v:
Gene
Gene, Elsevier, 2001, 262, pp.129-136
Gene, Elsevier, 2001, 262, pp.129-136
The cDNA for an aspartyl proteinase, termed eimepsin, was isolated from an Eimeria tenella sporulated oocyst library and the deduced amino acid sequence found to be almost identical to a previously described aspartyl proteinase from E. acervulina (97
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01241feb8b08d110dfc44fd4fe0caa8e
https://hal.inrae.fr/hal-02671171
https://hal.inrae.fr/hal-02671171
