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Author |
Shuster, G.; Sherman, P.W. |
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Title |
Tool use by naked mole-rats |
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1998 |
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Animal Cognition |
Abbreviated Journal |
Anim. Cogn. |
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1 |
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1 |
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71-74 |
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Naked mole-rats (Heterocephalus glaber, Rodentia: Bathyergidae) excavate extensive subterranean burrows with their procumbent incisors. Captive individuals often place a wood shaving or tuber husk behind their incisor teeth and in front of their lips and molar teeth while gnawing on substrates that yield fine particulate debris. This oral barrier may prevent choking or aspiration of foreign material. Consistent use of tools has rarely been reported in rodents. |
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Equine Behaviour @ team @ |
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3367 |
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Author |
McNelis, N.L.; Boatright-Horowitz, S.L. |
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Title |
Social monitoring in a primate group: the relationship between visual attention and hierarchical ranks |
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Journal Article |
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Year |
1998 |
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Animal Cognition |
Abbreviated Journal |
Anim. Cogn. |
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1 |
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1 |
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65-69 |
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Social monitoring has been hypothesized to be an important component of primate social behavior. If the gaze direction of one animal can redirect the gaze of another, visual scanning of conspecifics can provide a more efficient means of locating food or predators than directly scanning the entire nonsocial environment. Social monitoring also allows distance regulation between members of a group, reducing the likelihood of agonistic encounters. Although assessment of gaze direction in freely moving primates is problematic, we were successful in assessing amounts of visual scanning among adult females of a captive, socially housed group of patas monkeys (Erythrocebus patas) using a focal sampling technique with on-the-dot recording (5-s sampling intervals). In study 1, relative amounts of scanning were assessed as subjects gazed at any other member of the group. Percentages of agreement between observers ranged from 80% to 92%, with corresponding s values ranging from 0.74 to 0.92. In study 2, relative amounts of visual scanning were assessed so that specific targets of gaze were identified. The resultant data supported a long-standing prediction about the role of social monitoring in primate group dynamics. Lower-ranking animals gazed toward higher-ranking animals more often than vice versa. Although the specific cues eliciting social monitoring remain to be determined, visual attention in this social primate group appeared to be systematically related to hierarchical ranks, assessed by displacements. Minimally, these results suggest that patas monkeys structure their visual attention based on previous encounters with other members of their social group. While simple discrimination learning could account for these results, the demonstration of a systematic relationship between visual attention and primate social dynamics is relevant to current discussions of a primate's understanding of conspecific gaze direction. |
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Equine Behaviour @ team @ |
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3377 |
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McLaren I.P.L. |
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Title |
Animal Learning and Cognition: A neural network approach |
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1998 |
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Trends in Cognitive Sciences |
Abbreviated Journal |
Trends. Cognit. Sci. |
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2 |
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236-236 |
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refbase @ user @ |
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3464 |
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Vallortigara G. |
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Title |
Minds of Their Own |
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1998 |
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Trends in Cognitive Sciences |
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Trends. Cognit. Sci. |
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2 |
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118-118 |
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refbase @ user @ |
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3466 |
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Mesulam, M.-M. |
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Review article. From sensation to cognition |
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1998 |
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Brain |
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121 |
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1013-1052 |
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refbase @ user @ |
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3467 |
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Gilmanshin, R.; Callender, R.H.; Dyer, R.B. |
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The core of apomyoglobin E-form folds at the diffusion limit |
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1998 |
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Nature Structural Biology |
Abbreviated Journal |
Nat Struct Biol |
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5 |
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5 |
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363-365 |
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Animals; Apoproteins/*chemistry; Diffusion; Horses; Myoglobin/*chemistry; *Protein Folding; Spectroscopy, Fourier Transform Infrared; Temperature |
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The E-form of apomyoglobin has been characterized using infrared and fluorescence spectroscopies, revealing a compact core with native like contacts, most probably consisting of 15-20 residues of the A, G and H helices of apomyoglobin. Fast temperature-jump, time-resolved infrared measurements reveal that the core is formed within 96 micros at 46 degrees C, close to the diffusion limit for loop formation. Remarkably, the folding pathway of the E-form is such that the formation of a limited number of native-like contacts is not rate limiting, or that the contacts form on the same time scale expected for diffusion controlled loop formation. |
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English |
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1072-8368 |
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PMID:9586997 |
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Equine Behaviour @ team @ |
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3795 |
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Mizuguchi, M.; Arai, M.; Ke, Y.; Nitta, K.; Kuwajima, K. |
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Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy |
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1998 |
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Journal of Molecular Biology |
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283 |
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1 |
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265-277 |
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equine lysozyme; protein folding; molten globule; stopped-flow; folding intermediate |
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The equilibrium unfolding and the kinetics of unfolding and refolding of equine lysozyme, a Ca2+-binding protein, were studied by means of circular dichroism spectra in the far and near-ultraviolet regions. The transition curves of the guanidine hydrochloride-induced unfolding measured at 230 nm and 292.5 nm, and for the apo and holo forms of the protein have shown that the unfolding is well represented by a three-state mechanism in which the molten globule state is populated as a stable intermediate. The molten globule state of this protein is more stable and more native-like than that of α-lactalbumin, a homologous protein of equine lysozyme. The kinetic unfolding and refolding of the protein were induced by concentration jumps of the denaturant and measured by stopped-flow circular dichroism. The observed unfolding and refolding curves both agreed well with a single-exponential function. However, in the kinetic refolding reactions below 3 M guanidine hydrochloride, a burst-phase change in the circular dichroism was present, and the burst-phase intermediate in the kinetic refolding is shown to be identical with the molten globule state observed in the equilibrium unfolding. Under a strongly native condition, virtually all the molecules of equine lysozyme transform the structure from the unfolded state into the molten globule, and the subsequent refolding takes place from the molten globule state. The transition state of folding, which may exist between the molten globule and the native states, was characterized by investigating the guanidine hydrochloride concentration-dependence of the rate constants of refolding and unfolding. More than 80% of the hydrophobic surface of the protein is buried in the transition state, so that it is much closer to the native state than to the molten globule in which only 36% of the surface is buried in the interior of the molecule. It is concluded that all the present results are best explained by a sequential model of protein folding, in which the molten globule state is an obligatory folding intermediate on the pathway of folding. |
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3990 |
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Kesel, L.; Neil, D.H. |
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Restraint and handling of animals |
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1998 |
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Clinical Textbook for Veterinary Technicians. 4th ed. |
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1-26 |
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Cited By (since 1996): 1; Export Date: 21 October 2008 |
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Equine Behaviour @ team @ |
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4523 |
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Luescher, U.A.; McKeown, D.B.; Dean, H. |
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A cross-sectional study on compulsive behaviour (stable vices) in horses |
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1998 |
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Equine veterinary journal. Supplement |
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27 |
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14-18 |
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Cited By (since 1996): 22; Export Date: 21 October 2008 |
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Equine Behaviour @ team @ |
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4527 |
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Zohary, D.; Tchernov, E.; Horwitz, L.K. |
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The role of unconscious selection in the domestication of sheep and goats |
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1998 |
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J Zool |
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245 |
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Equine Behaviour @ team @ Zohary1998 |
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6240 |
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