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Winter horse care |
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1994 |
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Journal of Equine Veterinary Science |
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14 |
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2 |
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115-117 |
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Equine Behaviour @ team @ |
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4664 |
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Equine Behaviour @ team @ |
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6602 |
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Author |
A. Lanata; A. Guidi; G. Valenza; P. Baragli; E. P. Scilingo |
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Title |
Quantitative heartbeat coupling measures in human-horse interaction |
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Conference Article |
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2016 |
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2016 38th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC) |
Abbreviated Journal |
2016 38th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (E |
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2696-2699 |
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electrocardiography; medical signal processing; signal classification; time series; Dtw; Hrv; Mpc; Msc; complex biological systems; dynamic time warping; grooming; heart rate variability time series; heartbeat dynamics; human-horse dynamic interaction; magnitude squared coherence; magnitude-phase coupling; mean phase coherence; nearest mean classifier; quantitative heartbeat coupling; real human-animal interaction; time duration; visual-olfactory interaction; Coherence; Couplings; Electrocardiography; Heart rate variability; Horses; Protocols; Time series analysis |
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Abstract— We present a study focused on a quantitative estimation of a human-horse dynamic interaction. A set of measures based on magnitude and phase coupling between heartbeat dynamics of both humans and horses in three different conditions is reported: no interaction, visual/olfactory interaction and grooming. Specifically, Magnitude Squared Coherence (MSC), Mean Phase Coherence (MPC) and Dynamic Time Warping (DTW) have been used as estimators of the amount of coupling between human and horse through the analysis of their heart rate variability (HRV) time series in a group of eleven human subjects, and one horse. The rationale behind this study is that the interaction of two complex biological systems go towards a coupling process whose dynamical evolution is modulated by the kind and time duration of the interaction itself. We achieved a congruent and consistent
statistical significant difference for all of the three indices. Moreover, a Nearest Mean Classifier was able to recognize the three classes of interaction with an accuracy greater than 70%. Although preliminary, these encouraging results allow a discrimination of three distinct phases in a real human-animal interaction opening to the characterization of the empirically proven relationship between human and horse. |
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2016 38th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (E |
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1557-170x |
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Equine Behaviour @ team @ |
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6175 |
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Á. Miklósi |
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The Evolution of Cognition |
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1999 |
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Animal Cognition |
Abbreviated Journal |
Anim. Cogn. |
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2 |
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3 |
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179-180 |
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Heyes, C.; Huber, L. |
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Equine Behaviour @ team @ |
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3247 |
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Author |
A. Wiggins; K. Crowston |
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Title |
From Conservation to Crowdsourcing: A Typology of Citizen Science |
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2011 |
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2011 44th Hawaii International Conference on System Sciences |
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2011 44th Hawaii International Conference on System Sciences |
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1-10 |
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groupware; natural sciences computing; research and development; social sciences; crowdsourcing; citizen science typology; research collaboration; scientific research projects; virtual collaboration; Communities; Education; Monitoring; Collaboration; Organizations; Biological system modeling; Production |
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Citizen science is a form of research collaboration involving members of the public in scientific research projects to address real-world problems. Often organized as a virtual collaboration, these projects are a type of open movement, with collective goals addressed through open participation in research tasks. Existing typologies of citizen science projects focus primarily on the structure of participation, paying little attention to the organizational and macrostructural properties that are important to designing and managing effective projects and technologies. By examining a variety of project characteristics, we identified five types-Action, Conservation, Investigation, Virtual, and Education- that differ in primary project goals and the importance of physical environment to participation. |
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2011 44th Hawaii International Conference on System Sciences |
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1530-1605 |
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Equine Behaviour @ team @ |
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6430 |
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Author |
Abbruzzetti, S.; Crema, E.; Masino, L.; Vecli, A.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
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Title |
Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump |
Type |
Journal Article |
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Year |
2000 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
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78 |
Issue |
1 |
Pages |
405-415 |
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Animals; Apoproteins/*chemistry; Horses; *Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence |
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Ultrafast, laser-induced pH jump with time-resolved photoacoustic detection has been used to investigate the early protonation steps leading to the formation of the compact acid intermediate (I) of apomyoglobin (ApoMb). When ApoMb is in its native state (N) at pH 7.0, rapid acidification induced by a laser pulse leads to two parallel protonation processes. One reaction can be attributed to the binding of protons to the imidazole rings of His24 and His119. Reaction with imidazole leads to an unusually large contraction of -82 +/- 3 ml/mol, an enthalpy change of 8 +/- 1 kcal/mol, and an apparent bimolecular rate constant of (0.77 +/- 0.03) x 10(10) M(-1) s(-1). Our experiments evidence a rate-limiting step for this process at high ApoMb concentrations, characterized by a value of (0. 60 +/- 0.07) x 10(6) s(-1). The second protonation reaction at pH 7. 0 can be attributed to neutralization of carboxylate groups and is accompanied by an apparent expansion of 3.4 +/- 0.2 ml/mol, occurring with an apparent bimolecular rate constant of (1.25 +/- 0.02) x 10(11) M(-1) s(-1), and a reaction enthalpy of about 2 kcal/mol. The activation energy for the processes associated with the protonation of His24 and His119 is 16.2 +/- 0.9 kcal/mol, whereas that for the neutralization of carboxylates is 9.2 +/- 0.9 kcal/mol. At pH 4.5 ApoMb is in a partially unfolded state (I) and rapid acidification experiments evidence only the process assigned to carboxylate protonation. The unusually large contraction and the high energetic barrier observed at pH 7.0 for the protonation of the His residues suggests that the formation of the compact acid intermediate involves a rate-limiting step after protonation. |
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Dipartimento di Fisica, Universita di Parma, 43100 Parma, Italia |
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0006-3495 |
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PMID:10620304 |
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no |
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Equine Behaviour @ team @ |
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3792 |
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Author |
Abbruzzetti, S.; Viappiani, C.; Sinibaldi, F.; Santucci, R. |
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Title |
Kinetics of histidine dissociation from the heme Fe(III) in N-fragment (residues 1-56) of cytochrome c |
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Journal Article |
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Year |
2004 |
Publication |
The Protein Journal |
Abbreviated Journal |
Protein J |
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23 |
Issue |
8 |
Pages |
519-527 |
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Animals; Cytochromes c/*chemistry; Enzyme Activation; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Peptide Mapping; Photolysis; Spectrophotometry |
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We have here investigated the dissociation kinetics of the His side chains axially ligated to the heme-iron in the ferric (1-56 residues) N-fragment of horse cyt c. The ligand deligation induced by acidic pH-jump occurs as a biexponential process with different pre-exponential factors, consistent with a structural heterogeneity in solution and the presence of two differently coordinated species. In analogy with GuHCl-denatured cyt c, our data indicate the presence in solution of two ferric forms of the N-fragment characterized by bis-His coordination, as summarized in the following scheme: His18-Fe(III)-His26 <==> His18-Fe(III)-His33. We have found that the pre-exponential factors depend on the extent of the pH-jump. This may be correlated with the different pKa values shown by His26 and His33; due to steric factors, His26 binds to the heme-Fe(III) less strongly than His33, as recently shown by studies on denatured cyt c. Interestingly, the two lifetimes are affected by temperature but not by the extent of the pH-jump. The lower pKa for the deligation reaction required the use of an improved laser pH-jump setup, capable of inducing changes in H+ concentration as large as 1 mM after the end of the laser pulse. For the ferric N-fragment, close activation entropy values have been determined for the two histidines coordinated to the iron; this result significantly differs from that for GuHCl-denatured cyt c, where largely different values of activation entropy were calculated. This underlines the role played by the missing segment (residues 57-104) peptide chain in discriminating deligation of the “nonnative” His from the sixth coordination position of the metal. |
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Dipartimento di Fisica, Universita degli Studi di Parma, Parco Area delle Scienze 7/A 43100 Parma, Italy |
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1572-3887 |
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PMID:15648974 |
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Equine Behaviour @ team @ |
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3770 |
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Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
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Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique |
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Journal Article |
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Year |
2001 |
Publication |
Journal of the American Chemical Society |
Abbreviated Journal |
J Am Chem Soc |
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123 |
Issue |
27 |
Pages |
6649-6653 |
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Keywords |
Animals; *Bacterial Proteins; Cytochrome c Group/*chemistry; Guanidine/*chemistry; Heme/*chemistry; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; *Lasers; Ligands; Protein Folding |
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We have developed an instrumental setup that uses transient absorption to monitor protein folding/unfolding processes following a laser-induced, ultrafast release of protons from o-nitrobenzaldehyde. The resulting increase in [H(+)], which can be more than 100 microM, is complete within a few nanoseconds. The increase in [H(+)] lowers the pH of the solution from neutrality to approximately 4 at the highest laser pulse energy used. Protein structural rearrangements can be followed by transient absorption, with kinetic monitoring over a broad time range (approximately 10 ns to 500 ms). Using this pH-jump/transient absorption technique, we have examined the dissociation kinetics of non-native axial heme ligands (either histidine His26 or His33) in GuHCl-unfolded Fe(III) cytochrome c (cyt c). Deligation of the non-native ligands following the acidic pH-jump occurs as a biexponential process with different pre-exponential factors. The pre-exponential factors markedly depend on the extent of the pH-jump, as expected from differences in the pK(a) values of His26 and His33. The two lifetimes were found to depend on temperature but were not functions of either the magnitude of the pH-jump or the pre-pulse pH of the solution. The activation energies of the deligation processes support the suggestion that GuHCl-unfolded cyt c structures with non-native histidine axial ligands represent kinetic traps in unfolding. |
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Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 43100 Parma, Italy |
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0002-7863 |
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PMID:11439052 |
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Equine Behaviour @ team @ |
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3788 |
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Author |
Aberle, K. S. |
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Title |
Untersuchung der Verwandtschaftsverhältnisse, Inzucht und genetischen Distanzen bei den deutschen Kaltblutpferderassen |
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Manuscript |
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2003 |
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Ph.D. thesis |
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Hannover |
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German |
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Equine Behaviour @ team @ |
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5185 |
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Author |
Aberle, K.S.; Hamann, H.; Drögemüller, C.; Distl, O. |
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Title |
Genetic diversity in German draught horse breeds compared with a group of primitive, riding and wild horses by means of microsatellite DNA markers |
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Journal Article |
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Year |
2004 |
Publication |
Animal Genetics |
Abbreviated Journal |
Anim. Gen. |
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35 |
Issue |
4 |
Pages |
270-277 |
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diversity; endangered breeds; genetic variation; horse; microsatellite |
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Summary We compared the genetic diversity and distance among six German draught horse breeds to wild (Przewalski's Horse), primitive (Icelandic Horse, Sorraia Horse, Exmoor Pony) or riding horse breeds (Hanoverian Warmblood, Arabian) by means of genotypic information from 30 microsatellite loci. The draught horse breeds included the South German Coldblood, Rhenish German Draught Horse, Mecklenburg Coldblood, Saxon Thuringa Coldblood, Black Forest Horse and Schleswig Draught Horse. Despite large differences in population sizes, the average observed heterozygosity (Ho) differed little among the heavy horse breeds (0.64�0.71), but was considerably lower than in the Hanoverian Warmblood or Icelandic Horse population. The mean number of alleles (NA) decreased more markedly with declining population sizes of German draught horse breeds (5.2�6.3) but did not reach the values of Hanoverian Warmblood (NA = 6.7). The coefficient of differentiation among the heavy horse breeds showed 11.6% of the diversity between the heavy horse breeds, as opposed to 21.2% between the other horse populations. The differentiation test revealed highly significant genetic differences among all draught horse breeds except the Mecklenburg and Saxon Thuringa Coldbloods. The Schleswig Draught Horse was the most distinct draught horse breed. In conclusion, the study demonstrated a clear distinction among the German draught horse breeds and even among breeds with a very short history of divergence like Rhenish German Draught Horse and its East German subpopulations Mecklenburg and Saxon Thuringa Coldblood. |
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Blackwell Science Ltd |
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1365-2052 |
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Equine Behaviour @ team @ |
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5184 |
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