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Author |
Pierce, M.M.; Nall, B.T. |
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Title |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
Type |
Journal Article |
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Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
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Volume |
298 |
Issue |
5 |
Pages |
955-969 |
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Keywords |
Amino Acid Sequence; Amino Acid Substitution/genetics; Binding Sites; Cytochrome c Group/*chemistry/genetics/*metabolism; *Cytochromes c; Enzyme Stability/drug effects; Fluorescence; Guanidine/pharmacology; Heme/*metabolism; Histidine/genetics/*metabolism; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation/genetics; Proline/*chemistry/metabolism; Protein Conformation/drug effects; Protein Denaturation/drug effects; *Protein Folding; Protein Renaturation; Saccharomyces cerevisiae/enzymology/genetics; Sequence Alignment; Thermodynamics |
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Abstract |
The effect of His-heme misligation on folding has been investigated for a triple mutant of yeast iso-2 cytochrome c (N26H,H33N,H39K iso-2). The variant contains a single misligating His residue at position 26, a location at which His residues are found in several cytochrome c homologues, including horse, tuna, and yeast iso-1. The amplitude for fast phase folding exhibits a strong initial pH dependence. For GdnHCl unfolded protein at an initial pH<5, the observed refolding at final pH 6 is dominated by a fast phase (tau(2f)=20 ms, alpha(2f)=90 %) that represents folding in the absence of misligation. For unfolded protein at initial pH 6, folding at final pH 6 occurs in a fast phase of reduced amplitude (alpha(2f) approximately 20 %) but the same rate (tau(2f)=20 ms), and in two slower phases (tau(m)=6-8 seconds, alpha(m) approximately 45 %; and tau(1b)=16-20 seconds, alpha(1b) approximately 35 %). Double jump experiments show that the initial pH dependence of the folding amplitudes results from a slow pH-dependent equilibrium between fast and slow folding species present in the unfolded protein. The slow equilibrium arises from coupling of the His protonation equilibrium to His-heme misligation and proline isomerization. Specifically, Pro25 is predominantly in trans in the unligated low-pH unfolded protein, but is constrained in a non-native cis isomerization state by His26-heme misligation near neutral pH. Refolding from the misligated unfolded form proceeds slowly due to the large energetic barrier required for proline isomerization and displacement of the misligated His26-heme ligand. |
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Center for Biomolecular Structure, Department of Biochemistry, University of Texas Health Science Center, 7703 Floyd Curl Drive, San Antonio, TX 78229-3900, USA |
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0022-2836 |
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PMID:10801361 |
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Call Number |
refbase @ user @ |
Serial |
3853 |
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Author |
Dyson, H.J.; Beattie, J.K. |
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Title |
Spin state and unfolding equilibria of ferricytochrome c in acidic solutions |
Type |
Journal Article |
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Year |
1982 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
257 |
Issue |
5 |
Pages |
2267-2273 |
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Keywords |
Animals; *Cytochrome c Group; Electron Spin Resonance Spectroscopy; Heme; Horses; Hydrogen-Ion Concentration; Kinetics; Ligands; Myocardium; Protein Binding; Protein Conformation; Spectrophotometry; Temperature |
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Abstract |
Equilibrium, stopped flow, and temperature-jump spectrophotometry have been used to identify processes in the unfolding of ferricytochrome c in acidic aqueous solutions. A relaxation occurring in approximately 100 microseconds involves perturbation of a spin-equilibrium between two folded conformers of the protein with methionine-80 coordinated or dissociated from the heme iron. The protein unfolds more slowly, in milliseconds, with dissociation and protonation of histidine-18. These two transitions appear cooperative in equilibrium measurements at low (0.01 M) ionic strength, but are separated at higher (0.10 M) ionic strength. They are resolved under both conditions in the dynamic measurements. The spin-equilibrium description permits a unified explanation of a number of properties of ferricytochrome c in acidic aqueous solutions. |
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0021-9258 |
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PMID:6277891 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3807 |
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Author |
Tsong, T.Y. |
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Title |
Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c |
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Journal Article |
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Year |
1977 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
252 |
Issue |
24 |
Pages |
8778-8780 |
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Keywords |
*Cytochrome c Group; Guanidines/*pharmacology; Protein Conformation/drug effects; Spectrometry, Fluorescence; Urea/*pharmacology |
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Abstract |
Several recent studies of protein the unfolded proteins. In urea- and guanidine HCl-unfolded ferricytochrome c (horse heart), an acid-induced spin state transformation of the heme group has been detected by the heme absorptions, Trp-59 fluorescence, and the intrinsic viscosity of protein. Kinetics of this second conformational transition, by the temperature jump and stopped flow methods, are complex. One rapid reaction (tau1), pH-independent, occurs in a 50-mus range; the second reaction (tau2), in a 1-ms range, depends linearly upon pH and is faster at the alkaline side; a third reaction (tau3), in a 1-s range, shows a sigmoidal transition at pH 5.1 and is faster at the acidic side. The results are consistent with a kinetic scheme which involves protein conformational changes in the transformation of the heme coordination state. The kinetics, along with previous equilibrium studies, indicate that ligand or charge interactions within a protein molecule are not completely prohibited even in strongly denaturing conditions, such as in high concentrations of urea and guanidine HCl. Thus, local structures of peptide chain associated with these interactions can exist in the unfolded protein. |
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0021-9258 |
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PMID:200618 |
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Call Number |
refbase @ user @ |
Serial |
3882 |
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Author |
Saigo, S. |
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Title |
A transient spin-state change during alkaline isomerization of ferricytochrome c |
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Journal Article |
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Year |
1981 |
Publication |
Journal of Biochemistry |
Abbreviated Journal |
J Biochem (Tokyo) |
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Volume |
89 |
Issue |
6 |
Pages |
1977-1980 |
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Keywords |
Animals; *Cytochrome c Group; Horses; Hydrogen-Ion Concentration; Isomerism; Kinetics; Myocardium/enzymology; Oxidation-Reduction; Spectrophotometry |
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Kinetic difference spectra during the alkaline isomerization of ferricytochrome c were obtained by the pH-jump method in the range of 540 to 655 nm. The spectrum of the transient intermediate, which appears during the course of the isomerization, was reproduced from the spectra. The intermediate showed an intense absorption band at 600 nm, indicating that it is a high spin or mixed spin species. This is in contrast to the stable neutral and alkaline forms which are low spin species. The transient spin-state change during the isomerization was also observed upon rapid oxidation of ferrocytochrome c at alkaline pH. |
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0021-924X |
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PMID:6270075 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3808 |
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Author |
Curtis, S.E.; Stricklin, W.R. |
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Title |
The importance of animal cognition in agricultural animal production systems: an overview |
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Journal Article |
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Year |
1991 |
Publication |
Journal of Animal Science |
Abbreviated Journal |
J. Anim Sci. |
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Volume |
69 |
Issue |
12 |
Pages |
5001-5007 |
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Keywords |
*Agriculture; Animal Population Groups/*psychology; *Animal Welfare; Animals; *Behavior, Animal; *Cognition; Heat; Helplessness, Learned; Housing, Animal/standards; Immobilization; Nesting Behavior; Pain/psychology/veterinary |
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To describe and then fulfill agricultural animals' needs, we must learn more about their fundamental psychological and behavioral processes. How does this animal feel? Is that animal suffering? Will we ever be able to know these things? Scientists specializing in animal cognition say that there are numerous problems but that they can be overcome. Recognition by scientists of the notion of animal awareness has been increasing in recent years, because of the work of Griffin and others. Feeling, thinking, remembering, and imagining are cognitive processes that are factors in the economic and humane production of agricultural animals. It has been observed that the animal welfare debate depends on two controversial questions: Do animals have subjective feelings? If they do, can we find indicators that reveal them? Here, indirect behavioral analysis approaches must be taken. Moreover, the linear additivity of several stressor effects on a variety of animal traits suggests that some single phenomenon is acting as a “clearinghouse” for many or all of the stresses acting on an animal at any given time, and this phenomenon might be psychological stress. Specific situations animals may encounter in agricultural production settings are discussed with respect to the animals' subjective feelings. |
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University of Illinois, Urbana 61801 |
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0021-8812 |
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PMID:1808193 |
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Equine Behaviour @ team @ |
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2754 |
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Author |
Nuñez, C.M.V.; Adelman, J.S.; Smith, J.; Gesquiere, L.R.; Rubenstein, D.I. |
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Title |
Linking social environment and stress physiology in feral mares (Equus caballus): Group transfers elevate fecal cortisol levels |
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Journal Article |
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Year |
2014 |
Publication |
General and Comparative Endocrinology |
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196 |
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26-33 |
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Equus caballus; Fecal cortisol; Feral mare; Group transfer; Stress; Social instability |
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Abstract Feral horses (Equus caballus) have a complex social structure, the stability of which is important to their overall health. Behavioral and demographic research has shown that decreases in group (or band) stability reduce female fitness, but the potential effects on the physiological stress response have not been demonstrated. To fully understand how band stability affects group-member fitness, we need to understand not only behavioral and demographic, but also physiological consequences of decreases to that stability. We studied group changes in feral mares (an activity that induces instability, including both male and female aggression) on Shackleford Banks, NC. We found that mares in the midst of changing groups exhibit increased fecal cortisol levels. In addition, mares making more group transfers show higher levels of cortisol two weeks post-behavior. These results offer insights into how social instability is integrated into an animal’s physiological phenotype. In addition, our results have important implications for feral horse management. On Shackleford Banks, mares contracepted with porcine zona pellucida (PZP) make approximately 10 times as many group changes as do untreated mares. Such animals may therefore be at higher risk of chronic stress. These results support the growing consensus that links between behavior and physiological stress must be taken into account when managing for healthy, functional populations. |
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0016-6480 |
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Equine Behaviour @ team @ |
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5743 |
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Author |
de Waal, F.B.; Luttrell, L.M. |
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Title |
The similarity principle underlying social bonding among female rhesus monkeys |
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Journal Article |
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Year |
1986 |
Publication |
Folia primatologica; international journal of primatology |
Abbreviated Journal |
Folia Primatol (Basel) |
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Volume |
46 |
Issue |
4 |
Pages |
215-234 |
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Aggression; Animals; Dominance-Subordination; Female; Grooming; *Group Processes; Macaca/*physiology; Macaca mulatta/*physiology; Male; *Object Attachment |
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Abstract |
Twenty adult female rhesus monkeys (Macaca mulatta) were observed over a three-year period. They lived in a mixed captive group with kinship relations known for three generations. The study's aim was to test Seyfarth's [J. theor. Biol. 65: 671-698, 1977] model of rank-related grooming and to investigate two other possible determinants of social bonding, i.e. relative age and the group's stratification into two social classes. Data on affiliation, coalitions, and social competition were collected by means of both focal observation and instantaneous time sampling. Whereas certain elements of the existing model were confirmed, its explanatory principles were not. Social competition did not result in more contact among close-ranking females (the opposite effect was found), and the relation between affiliative behavior and coalitions was more complex than predicted. Based on multivariate analyses and a comparison of theoretical models, we propose a simpler, more encompassing principle underlying interfemale attraction. According to this 'similarity principle', rhesus females establish bonds with females whom they most resemble. The similarity may concern genetical and social background, age, hierarchical position and social class. Effects of these four factors were independently demonstrated. The most successful model assumed that similarity factors influence female bonding in a cumulative fashion. |
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0015-5713 |
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PMID:3557225 |
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refbase @ user @ |
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211 |
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Cambefort, J.P. |
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A comparative study of culturally transmitted patterns of feeding habits in the chacma baboon Papio ursinus and the vervet monkey Cercopithecus aethiops |
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Journal Article |
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Year |
1981 |
Publication |
Folia Primatologica; International Journal of Primatology |
Abbreviated Journal |
Folia Primatol (Basel) |
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36 |
Issue |
3-4 |
Pages |
243-263 |
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Keywords |
Age Factors; Animals; *Cercopithecus; *Cercopithecus aethiops; Culture; *Feeding Behavior; Female; Group Structure; Learning; Male; *Papio; Social Class; Teaching |
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Japanese workers have studied social acquisition patterns of new feeding habits in Macaca fuscata which they have termed precultural. The present study investigates the same phenomenon in the chacma baboon and the vervet monkey in their natural habitat. The questions addressed are: (1) How a new feeding habit enters a troop and by which age and sex category, also how it is propagated? (2) When individuals are permitted with a choice between palatable and unpalatable food, can they learn by demonstration only or do they have to pass through a direct learning process? (3) Can the results from the above questions be explained by social parameters such as the social structure of the individual species? It was found that juvenile baboons discover new food and that after the discovery propagation is instantaneous. In vervets discovery is random among the age classes and propagation is slow and takes place through certain 'pivot' individuals. Both species fail to learn about palatability by demonstration but have to go through a direct learning process. This contrasts strongly with the forest baboon Mandrillus sphinx that have been shown to learn by demonstration. Socially, baboon juveniles stay closer to each other than the adults who force them to live at the periphery of the troop. Vervets again forage without precise sub-group formation. The link between social and cultural propagation and social structure is discussed on the basis of these findings. |
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0015-5713 |
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PMID:7319426 |
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2087 |
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Wilson, M.T.; Ranson, R.J.; Masiakowski, P.; Czarnecka, E.; Brunori, M. |
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Title |
A kinetic study of the pH-dependent properties of the ferric undecapeptide of cytochrome c (microperoxidase) |
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Journal Article |
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Year |
1977 |
Publication |
European Journal of Biochemistry / FEBS |
Abbreviated Journal |
Eur J Biochem |
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Volume |
77 |
Issue |
1 |
Pages |
193-199 |
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Animals; Cyanides; *Cytochrome c Group/metabolism; Ferric Compounds; Horses; Hydrogen-Ion Concentration; Imidazoles; Kinetics; Mathematics; Myocardium/enzymology; *Oligopeptides/metabolism; *Peptide Fragments/metabolism; Protein Binding; Spectrophotometry; Temperature |
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The ferric form of the haem undecapeptide, derived from horse cytochrome c by peptic digestion, undergoes at least three pH-induced transitions with pK values of 3.4, 5.8 and 7.6. Temperature-jump experiments suggest that the first of these is due to the binding of a deprotonated imidazole group to the feric iron while the second and third arise from the binding of the two available amino groups present (the alpha-NH2 of valine and the epsilon-NH2 of lysine). Molecular models indicate that steric retraints on the peptide dictate that these amino groups may only coordinate to iron atoms via intermolecular bonds, thus leading to the polymerization of the peptide. Cyanide binding studies are in agreement with these conclusions and also yield a value of 3.6 X 10(6) M-1 s-1 for the intrinsic combination constant of CN- anion with the haem. A model is proposed which describes the pH-dependent properties of the ferric undecapeptide. |
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0014-2956 |
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PMID:20304 |
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Equine Behaviour @ team @ |
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3814 |
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Author |
Morton, D.B. |
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Title |
Self-consciousness and animal suffering |
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Journal Article |
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Year |
2000 |
Publication |
Biologist (London, England) |
Abbreviated Journal |
Biologist (London) |
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47 |
Issue |
2 |
Pages |
77-80 |
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Keywords |
Animal Population Groups/*psychology; Animal Welfare/*standards; Animals; Behavior, Animal; *Consciousness; Dogs; *Ego; Horses/psychology; Pain/psychology/*veterinary; Pan troglodytes/psychology; Parrots; Pongo pygmaeus/psychology; Self Concept |
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Animals with relatively highly developed brains are likely to experience some degree of self-awareness and the ability to think. As well as being interesting in its own right, self-consciousness matters from an ethical point of view, since it can give rise to forms of suffering above and beyond the immediate physical sensations of pain or distress. This article surveys the evidence for animal self-consciousness and its implications for animal welfare. |
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Division of Primary Care, Public and Occupational Health, School of Medicine, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. d.b.morton@bham.ac.uk |
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0006-3347 |
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PMID:11190233 |
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Call Number |
refbase @ user @ |
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618 |
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