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Author de Wall, F.B.; Aureli, F. openurl 
  Title Conflict resolution and distress alleviation in monkeys and apes Type Journal Article
  Year 1997 Publication Annals of the New York Academy of Sciences Abbreviated Journal Ann N Y Acad Sci  
  Volume (down) 807 Issue Pages 317-328  
  Keywords *Adaptation, Psychological; Animals; Arousal; *Conflict (Psychology); Empathy; Haplorhini/*psychology; Hominidae/*psychology; Humans; Learning; Models, Psychological; *Social Behavior; Stress, Psychological  
  Abstract Research on nonhuman primates has produced compelling evidence for reconciliation and consolation, that is, postconflict contacts that serve to respectively repair social relationships and reassure distressed individuals, such as victims of attack. This has led to a view of conflict and conflict resolution as an integrated part of social relationships, hence determined by social factors and modifiable by the social environment. Implications of this new model of social conflict are discussed along with evidence for behavioral flexibility, the value of cooperation, and the possibility that distress alleviation rests on empathy, a capacity that may be present in chimpanzees and humans but not in most other animals.  
  Address Yerkes Regional Primate Research Center, Emory University, Atlanta, Georgia 30322, USA. dewaal@rmy.emory.edu  
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  ISSN 0077-8923 ISBN Medium  
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  Notes PMID:9071360 Approved no  
  Call Number refbase @ user @ Serial 2882  
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Author Grinder, M.I.; Krausman, P.R.; Hoffmann, R.S. url  doi
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  Title Equus asinus Type Journal Article
  Year 2006 Publication Mammalian Species Abbreviated Journal  
  Volume (down) 794 Issue 1 Pages 1-9  
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  Notes Approved no  
  Call Number Equine Behaviour @ team @ Serial 4633  
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Author Cho, K.C.; Chan, K.K. url  openurl
  Title Kinetics of cold-induced denaturation of metmyoglobin Type Journal Article
  Year 1984 Publication Biochimica et Biophysica Acta (BBA) – Protein Structure and Molecular Enzymology Abbreviated Journal  
  Volume (down) 786 Issue 1-2 Pages 103-108  
  Keywords Metmyoglobin denaturation; Temperature jump; Denaturation kinetics; Conformational transformation; (Horse heart)  
  Abstract Using a slow temperature-jump spectrophotometer, we have studied the kinetics of cold-induced denaturation of metmyoglobin between 0[degree sign]C and 20[degree sign]C at acidic pH. The time-scale of the transition is slow and is of the order of minutes. The results are consistent with the transition's involving a total of three states, native (N), transient intermediate (I) and denatured (D), which are converted from one to the other in that order.  
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  Notes Approved no  
  Call Number refbase @ user @ Serial 3978  
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Author Saigo, S. openurl 
  Title Kinetic and equilibrium studies of alkaline isomerization of vertebrate cytochromes c Type Journal Article
  Year 1981 Publication Biochimica et Biophysica Acta Abbreviated Journal Biochim Biophys Acta  
  Volume (down) 669 Issue 1 Pages 13-20  
  Keywords Amino Acid Sequence; Animals; Cytochrome c Group/*metabolism; Dogs; Hydrogen-Ion Concentration; Isomerism; Kinetics; Vertebrates/metabolism  
  Abstract Equilibria and kinetics of alkaline isomerization of seven ferricytochromes c from vertebrates were studied by pH-titration and pH-jump methods in the pH region of 7-12. In the equilibrium behavior, no significant difference was detected among the cytochromes c, whereas marked differences in the kinetic behavior were observed. According to the kinetic behavior of the isomerization, the cytochromes c examined fall into three classes: Group I (horse, sheep, dog and pigeon cytochromes c), Group II (tuna and bonito cytochromes c) and Group III (rhesus monkey cytochrome c). The kinetic results are interpreted in terms of the sequential scheme: Neutral form in equilibrium with fast Transient form in equilibrium with slow Alkaline form where the neutral and alkaline forms are the species stable at neutral and alkaline pH, respectively, and the transient form is a kinetic intermediate. From comparison of the primary sequences of the seven cytochromes c and the classification of these cytochromes c, it is concluded that the amino acid substitution Phe/Tyr at the 46-th position has a major influence on the kinetic behavior. In Group II and III cytochromes c, the ionization of Tyr-46 is suggested to bring about loosening of the heme crevice and thus facilitate the ligand replacement involved in the isomerization.  
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  ISSN 0006-3002 ISBN Medium  
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  Notes PMID:6271238 Approved no  
  Call Number refbase @ user @ Serial 3871  
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Author RUCKEBUSCH Y et al, openurl 
  Title Les états de sommeil chez le cheval Type Journal Article
  Year 1970 Publication Abbreviated Journal Soc.de Biologie de Toulouse  
  Volume (down) 658 Issue Pages 665  
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  Notes from Professor Hans Klingels Equine Reference List Approved no  
  Call Number Serial 1532  
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Author Kihara, H. url  openurl
  Title Comparison of the redox reactions of various types of cytochrome c with iron hexacyanides Type Journal Article
  Year 1981 Publication Biochimica et Biophysica Acta (BBA) – Bioenergetics Abbreviated Journal  
  Volume (down) 634 Issue Pages 93-104  
  Keywords Cytochrome c; Redox reaction; Iron hexacyanide; Temperature jump; Electron transfer  
  Abstract The dynamic behavior of various types of cytochromes c in the redox reaction with iron hexacyanides was studied using a temperature-jump method in order to elucidate the molecular mechanism of the redox reaction of cytochromes with their oxidoreductants. Transmittance after the temperature jump changed through a single exponential decay for all cytochromes investigated. Under a constant concentration of anion, the redox reaction of various types of cytochrome c with iron hexacyanides was analyzed according to the scheme: Ki=kt/k-i (i=1,2,3) where C(III) and C(II) are ferric and ferrous cytochromes, respectively, Fe(III) and Fe(II) are ferri- and ferrocyanides, respectively, C(III) [middle dot] Fe(II) is the ferricytochrome-ferrocyanide complex and C(II) [middle dot] Fe(III) is the ferrocytochrome-ferricyanide complex. When step B is slower than the other two steps A and C, τ-1 can be represented approximately as where the bar over the variables denotes the equilibrium value. In a large excess of ferrocyanide against cytochrome, we can estimate k2, k-2, K1 and K3 independently. In the case of horse cytochrome c at 18[degree sign]C in 0.1 M phosphate buffer at pH 7 with 0.3 M KNO3, the estimated parameters are k2 = 100 +/- 50 s-1, k-2 = (3.5 +/- 1.0) [middle dot] 103 s-1, K1 = 15 +/- 7 M-1 and K3 = (8.5 +/- 1.5) [middle dot] 10-4 M. From the same experiments for seven cytochromes (cytochrome c from horse, tuna, Candida krusei, Saccharomyces oviformis, Rhodospirillum rubrum cytochrome c2, Spirulina platensis cytochrome c-554 and Thermus thermophilus cytochrome c-552), the following results can be deduced. (1) Each parameter defined in the scheme above (k2, k-2, K1, K3) diverged beyond the error range. Above all, k2 values of cytochromes c-554 and c-552 are as large as 1 [middle dot] 104 s-1 and much larger than those for the other cytochromes (to 50 approx. 700 S-1). (2) The variance of k2K1 and k-2/K3 are relatively less than the variances of individual parameters (k2, k-2, K1 and K3), which suggests that the values of k2K1 and k-2/K3 have been conserved during the course of evolution.  
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  Notes Approved no  
  Call Number refbase @ user @ Serial 3980  
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Author Hasumi, H. openurl 
  Title Kinetic studies on isomerization of ferricytochrome c in alkaline and acid pH ranges by the circular dichroism stopped-flow method Type Journal Article
  Year 1980 Publication Biochimica et Biophysica Acta Abbreviated Journal Biochim Biophys Acta  
  Volume (down) 626 Issue 2 Pages 265-276  
  Keywords Circular Dichroism; *Cytochrome c Group; Hydrogen-Ion Concentration; Isomerism; Kinetics; Spectrophotometry  
  Abstract The isomerization of horse-heart ferricytochrome c caused by varying pH was kinetically studied by using circular dichroism (CD) and optical absorption stopped-flow techniques. In the pH range of 7--13, the existence of the three different forms of ferricytochrome c (pH less than 10, pH 10--12, and pH greater than 12) was indicated from the statistical difference CD spectra. On the basis of analyses of the stopped-flow traces in the near-ultraviolet and Soret wavelength regions, the isomerization of ferricytochrome c from neutral form to the above three alkaline forms was interpreted as follows (1) below pH 10, the replacement of the intrinsic ligand of methionine residue by lysine residue occurs; (2) between pH 10 and 12, the uncoupling of the polypeptide chain from close proximity of the heme group occurs first, followed by the interconversion of the intrinsic ligands; and (3) above pH 12, hydroxide form of ferricytochrome c is formed, though the replacement of the intrinsic ligand by extrinsic ligands may occur via different routes from those below pH 12. The CD changes at 288 nm and in the Soret region caused by the pH-jump (down) from pH 6.0 to 1.6 were compared with the appearance of the 620-nm absorption band ascribed to the formation of the high-spin form of ferricytochrome c. Both CD and absorption changes indicated that the isomerization at pH 1.6 consisted of two processes: one proceeded within the dead-time (about 2 ms) of the stopped-flow apparatus and the other proceeded at a determinable rate with the apparatus. On the basis of these results, the isomerization of ferricytochrome c at pH 1.6 was explained as follows: (1) the transition from the low-spin form to the high-spin forms occurs within about 2 ms, the dead-time of the stopped-flow apparatus; and (2) the polypeptide chain is unfolded after the formation of the high-spin form.  
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  ISSN 0006-3002 ISBN Medium  
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  Notes PMID:6260152 Approved no  
  Call Number refbase @ user @ Serial 3876  
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Author Anderson, W.D.; Summers, C.H. url  doi
openurl 
  Title Neuroendocrine Mechanisms, Stress Coping Strategies, and Social Dominance: Comparative Lessons about Leadership Potential Type Journal Article
  Year 2007 Publication The ANNALS of the American Academy of Political and Social Science Abbreviated Journal Ann Am Acad Polit Soc Sci  
  Volume (down) 614 Issue 1 Pages 102-130  
  Keywords social dominance – authoritarian – Five Factor Model – neurochemistry – neurotransmitters – leadership  
  Abstract The authors examine dominance and subordination in the social psychology, political science, and biology literatures. Using Summers and Winberg (2006) as a guide, the authors suggest that extreme dominance or subordination phenotypes--including social dominance orientation and right-wing authoritarianism--are determined by an organism's genetic predispositions, motivations, stress responses, and long-term hormone release and uptake states. The authors offer hypotheses about the likely neurochemical profiles for each of these extreme dominance and subordination phenotypes and suggest two designs that begin to test these hypotheses.  
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  Notes Approved no  
  Call Number Equine Behaviour @ team @ Serial 4699  
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Author Pocock Ri, openurl 
  Title On the agriotype of domestic asses Type Journal Article
  Year 0 Publication Abbreviated Journal  
  Volume (down) 523 Issue Pages 528  
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  Notes from Professor Hans Klingels Equine Reference List Approved no  
  Call Number Serial 1473  
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Author Moon, C.; Baldridge, M.T.; Wallace, M.A.; Burnham, C.-A.D.; Virgin, H.W.; Stappenbeck, T.S. url  doi
openurl 
  Title Vertically transmitted faecal IgA levels determine extra-chromosomal phenotypic variation Type Journal Article
  Year 2015 Publication Nature Abbreviated Journal Nature  
  Volume (down) 521 Issue 7550 Pages 90-93  
  Keywords Phenotype  
  Abstract The proliferation of genetically modified mouse models has exposed phenotypic variation between investigators and institutions that has been challenging to control1-5. In many cases, the microbiota is the presumed culprit of the variation. Current solutions to account for phenotypic variability include littermate and maternal controls or defined microbial consortia in gnotobiotic mice6,7. In conventionally raised mice, the microbiome is transmitted from the dam2,8,9. Here we show that microbially–driven dichotomous fecal IgA levels in WT mice within the same facility mimic the effects of chromosomal mutations. We observed in multiple facilities that vertically-transmissible bacteria in IgA-Low mice dominantly lowered fecal IgA levels in IgA-High mice after cohousing or fecal transplantation. In response to injury, IgA-Low mice showed increased damage that was transferable by fecal transplantation and driven by fecal IgA differences. We found that bacteria from IgA-Low mice degraded the secretory component (SC) of SIgA as well as IgA itself. These data indicate that phenotypic comparisons between mice must take into account the non-chromosomal hereditary variation between different breeders. We propose fecal IgA as one marker of microbial variability and conclude that cohousing and/or fecal transplantation enables analysis of progeny from different dams.  
  Address Department of Pathology and Immunology, Washington University School of Medicine, St Louis, Missouri 63110, USA.  
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  ISSN 0028-0836 ISBN Medium  
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  Notes Approved no  
  Call Number Equine Behaviour @ team @ Serial 6005  
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