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Giulietta Minozzi Maria Grazia De Iorio Fiorentina Palazzo Gustavo Gandini Stefano Biffani Gianluigi Paolillo Elena Ciani Vincenzo Di Marco Lo Presti Alessandra Stella John L. Williams 《Animal genetics》2023,54(1):78-81
Mycobacterium avium ssp. paratuberculosis (MAP), causes Johne's disease (JD), or paratuberculosis, a chronic enteritis of ruminants, which in goats is characterized by ileal lesions. The work described here is a case–control association study using the Illumina Caprine SNP50 BeadChip to unravel the genes involved in susceptibility of goats to JD. Goats in herds with a high occurrence of Johne's disease were classified as healthy or infected based on the level of serum antibodies against MAP, and 331 animals were selected for the association study. Goats belonged to the Jonica (157) and Siriana breeds (174). Whole-genome association analysis identified one region suggestive of significance associated with an antibody response to MAP on chromosome 7 (p-value = 1.23 × 10−5). These results provide evidence for genetic loci involved in the antibody response to MAP in goats. 相似文献
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Francesco P. Nicoletti Matthew K. Thompson Stefan Franzen Giulietta Smulevich 《Journal of biological inorganic chemistry》2011,16(4):611-619
Dehaloperoxidase-hemoglobin (DHP) is a unique multifunctional enzyme with a globin fold. The enzyme serves as the respiratory
hemoglobin for the marine worm Amphitrite ornata and has been shown to catalyze the conversion of highly toxic trihalophenols to dihaloquinones as a detoxification function
for the organism. Given the simplicity of the structure of A. ornata, it is entirely possible that DHP may play an even more general role in detoxification of the organism from sulfide commonly
found in the coastal estuaries where A. ornata thrives. Comparison of DHP with other sulfide-binding hemoglobins shows that DHP possesses several distal cavity structural
properties, such as an aromatic cage and a hydrogen-bond-donor amino acid (His55), that facilitate sulfide binding. Furthermore,
a complete reduction of the ferric heme occurs after sulfide exposure under aerobic or anaerobic conditions to yield either
the oxy or the deoxy ferrous states of DHP, respectively. Oxidation of sulfide by the heme leads to sulfur products that are
less toxic to A. ornata. This proposed new function for DHP relies on the highly flexible distal His55 for deprotonation of the bound hydrogen sulfide,
similar to H2O2 activation of the peroxidase function, and provides further support for the importance of the flexibility of the distal His55
in this novel globin. 相似文献
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Simone Passolunghi Luca Riboldi Laura Dato Danilo Porro Paola Branduardi 《Microbial cell factories》2010,9(1):7