Open Access. Powered by Scholars. Published by Universities.®
- Discipline
-
- Animal Sciences (1)
- Ecology and Evolutionary Biology (1)
- Environmental Sciences (1)
- Life Sciences (1)
- Natural Resources Management and Policy (1)
-
- Natural Resources and Conservation (1)
- Other Environmental Sciences (1)
- Other Veterinary Medicine (1)
- Physical Sciences and Mathematics (1)
- Population Biology (1)
- Terrestrial and Aquatic Ecology (1)
- Veterinary Infectious Diseases (1)
- Veterinary Medicine (1)
- Veterinary Microbiology and Immunobiology (1)
- Veterinary Preventive Medicine, Epidemiology, and Public Health (1)
- Zoology (1)
Articles 1 - 5 of 5
Full-Text Articles in Medicine and Health Sciences
Detection Of Two Dissimilar Chronic Wasting Disease Isolates In Two Captive Rocky Mountain Elk (Cervus Canadensis) Herds: Two Distinctive Chronic Wasting Disease Isolates Identified In Captive Elk, Tracy A. Nichols, Eric M. Nicholson, Yihui Liu, Wanyin Tao, Terry R. Spraker, Michael Lavelle, Justin W. Fischer, Qingzhong Kong, Kurt C. Vercauteren
Detection Of Two Dissimilar Chronic Wasting Disease Isolates In Two Captive Rocky Mountain Elk (Cervus Canadensis) Herds: Two Distinctive Chronic Wasting Disease Isolates Identified In Captive Elk, Tracy A. Nichols, Eric M. Nicholson, Yihui Liu, Wanyin Tao, Terry R. Spraker, Michael Lavelle, Justin W. Fischer, Qingzhong Kong, Kurt C. Vercauteren
USDA Wildlife Services: Staff Publications
Chronic wasting disease (CWD) continues to spread in both wild and captive cervid herds in North America and has now been identified in wild reindeer and moose in Norway, Finland and Sweden. There is limited knowledge about the variety and characteristics of isolates or strains of CWD that exist in the landscape and their implications on wild and captive cervid herds. In this study, we evaluated brain samples from two captive elk herds that had differing prevalence, history and timelines of CWD incidence. Site 1 had a 16-year history of CWD with a consistently low prevalence between 5% and 10%. …
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: Iii. Peculiarities Of The Wild Type Bobp Unfolding In Crowded Milieu, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: Iii. Peculiarities Of The Wild Type Bobp Unfolding In Crowded Milieu, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Molecular Medicine Faculty Publications
Contrary to the majority of the members of the lipocalin family, which are stable monomers with the specific OBP fold (a β-barrel consisting of a 8-stranded anti-parallel β-sheet followed by a short α-helical segment, a ninth β-strand, and a disordered C-terminal tail) and a conserved disulfide bond, bovine odorant-binding protein (bOBP) does not have such a disulfide bond and forms a domain-swapped dimer that involves crossing the α-helical region from each monomer over the β-barrel of the other monomer. Furthermore, although natural bOBP isolated from bovine tissues exists as a stable domain-swapped dimer, recombinant bOBP has decreased dimerization potential and …
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: Ii. Unfolding Of The Monomeric Forms, Olga V. Stepanenko, Denis O. Roginski, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: Ii. Unfolding Of The Monomeric Forms, Olga V. Stepanenko, Denis O. Roginski, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Molecular Medicine Faculty Publications
In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the Trp64Cys/His155Cys double mutation to restore the canonical disulfide bond. We also analyzed the effect of the natural ligand binding on the conformational stabilities of these bOBP …
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: Ii. Unfolding Of The Monomeric Forms, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: Ii. Unfolding Of The Monomeric Forms, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Molecular Medicine Faculty Publications
In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the Trp64Cys/His155Cys double mutation to restore the canonical disulfide bond. We also analyzed the effect of the natural ligand binding on the conformational stabilities of these bOBP …
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: Ii. Unfolding Of The Monomeric Forms, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Structure And Stability Of Recombinant Bovine Odorant-Binding Protein: Ii. Unfolding Of The Monomeric Forms, Olga V. Stepanenko, Denis O. Roginskii, Olesya V. Stepanenko, Irina M. Kuznetsova, Vladimir N. Uversky, Konstantin K. Turoverov
Molecular Medicine Faculty Publications
In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the Trp64Cys/His155Cys double mutation to restore the canonical disulfide bond. We also analyzed the effect of the natural ligand binding on the conformational stabilities of these bOBP …