Records |
Author |
Dyer, F.C. |
Title |
Animal behaviour: when it pays to waggle |
Type |
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Year |
2002 |
Publication |
Nature |
Abbreviated Journal |
Nature |
Volume |
419 |
Issue |
6910 |
Pages |
885-886 |
Keywords |
*Animal Communication; Animals; Bees/*physiology; California; Dancing/physiology; Environment; Evolution; Female; Flowers/chemistry; *Food; Gravitation; Lighting; Motor Activity/*physiology; Odors; Seasons; Sunlight |
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0028-0836 |
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PMID:12410290 |
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no |
Call Number |
refbase @ user @ |
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769 |
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Author |
Selby, L.A.; Marienfeld, C.J.; Pierce, J.O. |
Title |
The effects of trace elements on human and animal health |
Type |
Journal Article |
Year |
1970 |
Publication |
Journal of the American Veterinary Medical Association |
Abbreviated Journal |
J Am Vet Med Assoc |
Volume |
157 |
Issue |
11 |
Pages |
1800-1808 |
Keywords |
Anemia, Hypochromic/veterinary; Animal Nutrition Physiology; Animals; Artiodactyla/*physiology; Chemistry; Cobalt/analysis/metabolism; Copper/analysis/metabolism; Deficiency Diseases/veterinary; Dogs/*physiology; Ecology; Horses/*physiology; Humans; Iodine/analysis/metabolism; Iron/analysis/metabolism; Manganese/analysis/metabolism; Nutritional Requirements; Selenium/metabolism; Trace Elements/*metabolism; Zinc/analysis/metabolism |
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0003-1488 |
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PMID:4922190 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
2733 |
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Author |
Gilmanshin, R.; Callender, R.H.; Dyer, R.B. |
Title |
The core of apomyoglobin E-form folds at the diffusion limit |
Type |
Journal Article |
Year |
1998 |
Publication |
Nature Structural Biology |
Abbreviated Journal |
Nat Struct Biol |
Volume |
5 |
Issue |
5 |
Pages |
363-365 |
Keywords |
Animals; Apoproteins/*chemistry; Diffusion; Horses; Myoglobin/*chemistry; *Protein Folding; Spectroscopy, Fourier Transform Infrared; Temperature |
Abstract |
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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1072-8368 |
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Notes |
PMID:9586997 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
3795 |
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Author |
Anderson, W.D.; Summers, C.H. |
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 |
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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no |
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Equine Behaviour @ team @ |
Serial |
4699 |
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Author |
Boucher, J.M.; Hanosset, R.; Augot, D.; Bart, J.M.; Morand, M.; Piarroux, R.; Pozet-Bouhier, F.; Losson, B.; Cliquet, F. |
Title |
Detection of Echinococcus multilocularis in wild boars in France using PCR techniques against larval form |
Type |
Journal Article |
Year |
2005 |
Publication |
Veterinary Parasitology |
Abbreviated Journal |
Vet Parasitol |
Volume |
129 |
Issue |
3-4 |
Pages |
259-266 |
Keywords |
Animals; Base Sequence; DNA, Helminth/chemistry/genetics; Echinococcosis/parasitology/pathology/*veterinary; Echinococcus multilocularis/*isolation & purification; Electron Transport Complex IV/chemistry/genetics; France; Histocytochemistry/veterinary; Liver/parasitology/pathology; Male; Molecular Sequence Data; Polymerase Chain Reaction/veterinary; Sequence Alignment; Sus scrofa/*parasitology; Swine Diseases/*parasitology/pathology |
Abstract |
Recently, new data have been collected on the distribution and ecology of Echinococcus multilocularis in European countries. Different ungulates species such as pig, goat, sheep, cattle and horse are known to host incomplete development of larval E. multilocularis. We report a case of E. multilocularis portage in two wild boars from a high endemic area in France (Department of Jura). Histological examination was performed and the DNA was isolated from hepatic lesions then amplified by using three PCR methods in two distinct institutes. Molecular characterisation of PCR products revealed 99% nucleotide sequence homology with the specific sequence of the U1 sn RNA gene of E. multilocularis, 99 and 99.9% nucleotide sequence homology with the specific sequence of the cytochrome oxydase gene of Echinococcus genus and 99.9% nucleotide sequence homology with a genomic DNA sequence of Echinococcus genus for the first and the second wild boar, respectively. |
Address |
AFSSA Nancy, Laboratoire d'Etudes et de Recherches sur la Rage et la Pathologie des Animaux Sauvages, Domaine de Pixerecourt-B.P. 9, Malzeville F 54220, France |
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English |
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Series Issue |
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Edition |
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ISSN |
0304-4017 |
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Notes |
PMID:15845281 |
Approved |
no |
Call Number |
Equine Behaviour @ team @ |
Serial |
2629 |
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Author |
Pierce, M.M.; Nall, B.T. |
Title |
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization |
Type |
Journal Article |
Year |
2000 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
Volume |
298 |
Issue |
5 |
Pages |
955-969 |
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 |
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. |
Address |
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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English |
Summary Language |
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Series Editor |
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Edition |
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ISSN |
0022-2836 |
ISBN |
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Area |
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Conference |
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Notes |
PMID:10801361 |
Approved |
no |
Call Number |
refbase @ user @ |
Serial |
3853 |
Permanent link to this record |
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Author |
Touma, C.; Sachser, N.; Mostl, E.; Palme, R. |
Title |
Effects of sex and time of day on metabolism and excretion of corticosterone in urine and feces of mice |
Type |
Journal Article |
Year |
2003 |
Publication |
General and Comparative Endocrinology |
Abbreviated Journal |
Gen Comp Endocrinol |
Volume |
130 |
Issue |
3 |
Pages |
267-278 |
Keywords |
Animals; Chromatography, High Pressure Liquid; Circadian Rhythm/*physiology; Corticosterone/*metabolism/urine; Feces/*chemistry; Female; Immunoenzyme Techniques; Kinetics; Male; Mice; Mice, Inbred C57BL; Reference Values; Sex Factors; Stress/metabolism; Time Factors; Tritium |
Abstract |
Non-invasive techniques to monitor stress hormones in small animals like mice offer several advantages and are highly demanded in laboratory as well as in field research. Since knowledge about the species-specific metabolism and excretion of glucocorticoids is essential to develop such a technique, we conducted radiometabolism studies in mice (Mus musculus f. domesticus, strain C57BL/6J). Each mouse was injected intraperitoneally with 740 kBq of 3H-labelled corticosterone and all voided urine and fecal samples were collected for five days. In a first experiment 16 animals (eight of each sex) received the injection at 9 a.m., while eight mice (four of each sex) were injected at 9 p.m. in a second experiment. In both experiments radioactive metabolites were recovered predominantly in the feces, although males excreted significantly higher proportions via the feces (about 73%) than females (about 53%). Peak radioactivity in the urine was detected within about 2h after injection, while in the feces peak concentrations were observed later (depending on the time of injection: about 10h postinjection in experiment 1 and about 4h postinjection in experiment 2, thus proving an effect of the time of day). The number and relative abundance of fecal [3H]corticosterone metabolites was determined by high performance liquid chromatography (HPLC). The HPLC separations revealed that corticosterone was extensively metabolized mainly to more polar substances. Regarding the types of metabolites formed, significant differences were found between males and females, but not between the experiments. Additionally, the immunoreactivity of these metabolites was assessed by screening the HPLC fractions with four enzyme immunoassays (EIA). However, only a newly established EIA for 5alpha-pregnane-3beta,11beta,21-triol-20-one (measuring corticosterone metabolites with a 5alpha-3beta,11beta-diol structure) detected several peaks of radioactive metabolites with high intensity in both sexes, while the other EIAs showed only minor immunoreactivity. Thus, our study for the first time provides substantial information about metabolism and excretion of corticosterone in urine and feces of mice and is the first demonstrating a significant impact of the animals' sex and the time of day. Based on these data it should be possible to monitor adrenocortical activity non-invasively in this species by measuring fecal corticosterone metabolites with the newly developed EIA. Since mice are extensively used in research world-wide, this could open new perspectives in various fields from ecology to behavioral endocrinology. |
Address |
Department of Behavioral Biology, Institute of Neuro and Behavioral Biology, University of Muenster, Badestrasse 9, D-48149 Muenster, Germany. touma@uni-muenster.de |
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English |
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0016-6480 |
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PMID:12606269 |
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no |
Call Number |
Equine Behaviour @ team @ |
Serial |
4086 |
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Author |
Touma, C.; Palme, R.; Sachser, N. |
Title |
Analyzing corticosterone metabolites in fecal samples of mice: a noninvasive technique to monitor stress hormones |
Type |
Journal Article |
Year |
2004 |
Publication |
Hormones and Behavior |
Abbreviated Journal |
Horm Behav |
Volume |
45 |
Issue |
1 |
Pages |
10-22 |
Keywords |
Adrenal Cortex/drug effects; Adrenal Cortex Function Tests; Adrenocorticotropic Hormone/pharmacology; Analysis of Variance; Animals; Circadian Rhythm; Corticosterone/*analysis/metabolism; Dexamethasone/pharmacology; Feces/*chemistry; Female; Immunoenzyme Techniques/*methods; Male; Mice; Mice, Inbred C57BL; Models, Animal; Reproducibility of Results; Stress, Psychological/*metabolism |
Abstract |
In small animals like mice, the monitoring of endocrine functions over time is constrained seriously by the adverse effects of blood sampling. Therefore, noninvasive techniques to monitor, for example, stress hormones in these animals are highly demanded in laboratory as well as in field research. The aim of our study was to evaluate the biological relevance of a recently developed technique to monitor stress hormone metabolites in fecal samples of laboratory mice. In total, six experiments were performed using six male and six female mice each. Two adrenocorticotropic hormone (ACTH) challenge tests, two dexamethasone (Dex) suppression tests and two control experiments [investigating effects of the injection procedure itself and the diurnal variation (DV) of glucocorticoids (GCs), respectively] were conducted. The experiments clearly demonstrated that pharmacological stimulation and suppression of adrenocortical activity was reflected accurately by means of corticosterone metabolite (CM) measurements in the feces of males and females. Furthermore, the technique proved sensitive enough to detect dosage-dependent effects of the ACTH/Dex treatment and facilitated to reveal profound effects of the injection procedure itself. Even the naturally occurring DV of GCs could be monitored reliably. Thus, our results confirm that measurement of fecal CM with the recently established 5alpha-pregnane-3beta,11beta,21-triol-20-one enzyme immunoassay is a very powerful tool to monitor adrenocortical activity in laboratory mice. Since mice represent the vast majority of all rodents used for research worldwide and the number of transgenic and knockout mice utilized as animal models is still increasing, this noninvasive technique can open new perspectives in biomedical and behavioral science. |
Address |
Department of Behavioural Biology, University of Muenster, D-48149 Muenster, Germany. touma@uni-muenster.de |
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English |
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0018-506X |
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PMID:14733887 |
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no |
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Equine Behaviour @ team @ |
Serial |
4084 |
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Author |
Franceschini, C.; Siutz, C.; Palme, R.; Millesi, E. |
Title |
Seasonal changes in cortisol and progesterone secretion in Common hamsters |
Type |
Journal Article |
Year |
2007 |
Publication |
General and Comparative Endocrinology |
Abbreviated Journal |
Gen Comp Endocrinol |
Volume |
152 |
Issue |
1 |
Pages |
14-21 |
Keywords |
Animals; Cortisone/*secretion; Cricetinae/*metabolism; Feces/chemistry; Female; Lactation/physiology; Male; Pregnancy; Progesterone/*secretion; Reproduction/physiology; *Seasons; Sexual Behavior, Animal/physiology |
Abstract |
In this study, we investigated endocrine factors and behaviour in free-living Common hamsters (Cricetus cricetus) during reproductive and non-reproductive periods of the annual cycle. We applied a non-invasive method to gain information on seasonal changes in adrenocortical activity in male and female hamsters by analysing faecal glucocorticoid metabolite concentrations (FCM). In addition, plasma progesterone concentrations were monitored in females throughout the non-hibernation season. The animals were live-trapped from spring emergence until the onset of hibernation in autumn. Reproductive status was determined at capture and blood and faecal samples were collected. During behavioural observations, agonistic and sexual interactions were recorded. FCM concentrations were significantly higher in males than in females during the reproductive period. In males, a pronounced increase in FCM during the reproductive period coincided with high frequencies of intrasexual aggression. In females, FCM levels remained relatively constant. Aggressive behaviour in females increased during the reproductive period, but was much less frequent than in males. Females, which successfully raised a second litter after a postpartum oestrus and concurrent lactation and gestation had lower FCM levels than individuals, which lost their second litter after parturition. As expected, plasma progesterone concentrations were low before and after the reproductive period. During gestation, levels peaked and remained elevated during lactation. The results of this field study provide insight in critical periods associated with reproduction in male and female Common hamsters. |
Address |
Department of Behavioural Biology, University of Vienna, Althanstrasse 14, A-1090 Vienna, Austria. claudia.franceschini@univie.ac.ct |
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0016-6480 |
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PMID:17408667 |
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no |
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Equine Behaviour @ team @ |
Serial |
4076 |
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Author |
Hoang, L.; Maity, H.; Krishna, M.M.G.; Lin, Y.; Englander, S.W. |
Title |
Folding units govern the cytochrome c alkaline transition |
Type |
Journal Article |
Year |
2003 |
Publication |
Journal of Molecular Biology |
Abbreviated Journal |
J Mol Biol |
Volume |
331 |
Issue |
1 |
Pages |
37-43 |
Keywords |
Animals; Cytochrome c Group/*chemistry; Horses; Hydrogen/chemistry; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; *Protein Folding; Protein Structure, Tertiary; Spectrum Analysis; Titrimetry |
Abstract |
The alkaline transition of cytochrome c is a model for protein structural switching in which the normal heme ligand is replaced by another group. Stopped flow data following a jump to high pH detect two slow kinetic phases, suggesting two rate-limiting structure changes. Results described here indicate that these events are controlled by the same structural unfolding reactions that account for the first two steps in the reversible unfolding pathway of cytochrome c. These and other results show that the cooperative folding-unfolding behavior of protein foldons can account for a variety of functional activities in addition to determining folding pathways. |
Address |
Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. lhoang@mail.upenn.edu |
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0022-2836 |
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PMID:12875834 |
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no |
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Equine Behaviour @ team @ |
Serial |
3781 |
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