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Territorial behavior in Taiwanese kukrisnakes (Oligodon formosanus) [Ecology] (2011)

Huang, W.-S., Greene, H. W., Chang, T.-J., Shine, R.

National Academy of Sciences

In: PNAS - Proceedings of the National Academy of Sciences

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Publikationsdatum: 2011-05-04

Beschreibung: The independent evolutionary origin of a complex trait, within a lineage otherwise lacking it, provides a powerful opportunity to test hypotheses on selective forces. Territorial defense of an area containing resources (such as food or shelter) is widespread in lizards but not snakes. Our studies on an insular population of Taiwanese kukrisnakes (Oligodon formosanus) show that females of this species actively defend sea turtle nests by repelling conspecifics for long periods (weeks) until the turtle eggs hatch or are consumed. A clutch of turtle eggs comprises a large, long-lasting food resource, unlike the prey types exploited by other types of snakes. Snakes of this species have formidable weaponry (massively enlarged teeth that are used for slitting eggshells), and when threatened, these snakes wave their tails toward the aggressor (an apparent case of head-tail mimicry). Bites to the tail during intraspecific combat bouts thus can have high fitness costs for males (because the hemipenes are housed in the tail). In combination, unusual features of the species (ability to inflict severe damage to male conspecifics) and the local environment (a persistent prey resource, large relative to the snakes consuming it) render resource defense both feasible and advantageous for female kukrisnakes. The (apparently unique) evolution of territorial behavior in this snake species thus provides strong support for the hypothesis that resource defensibility is critical to the evolution of territoriality.

Print ISSN: 0027-8424

Digitale ISSN: 1091-6490

Thema: Biologie , Medizin , Allgemeine Naturwissenschaft

Publiziert von National Academy of Sciences

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Serotonin-mushroom body circuit modulating the formation of anesthesia-resistant memory in Drosophila [Neuroscience] (2011)

Lee, P.-T., Lin, H.-W., Chang, Y.-H., Fu, T.-F., Dubnau, J., Hirsh, J., Lee, T., Chiang, A.-S.

National Academy of Sciences

In: PNAS - Proceedings of the National Academy of Sciences

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Publikationsdatum: 2011-08-18

Beschreibung: Pavlovian olfactory learning in Drosophila produces two genetically distinct forms of intermediate-term memories: anesthesia-sensitive memory, which requires the amnesiac gene, and anesthesia-resistant memory (ARM), which requires the radish gene. Here, we report that ARM is specifically enhanced or inhibited in flies with elevated or reduced serotonin (5HT) levels, respectively. The requirement for 5HT was additive with the memory defect of the amnesiac mutation but was occluded by the radish mutation. This result suggests that 5HT and Radish protein act on the same pathway for ARM formation. Three supporting lines of evidence indicate that ARM formation requires 5HT released from only two dorsal paired medial (DPM) neurons onto the mushroom bodies (MBs), the olfactory learning and memory center in Drosophila: (i) DPM neurons were 5HT-antibody immunopositive; (ii) temporal inhibition of 5HT synthesis or release from DPM neurons, but not from other serotonergic neurons, impaired ARM formation; (iii) knocking down the expression of d5HT1A serotonin receptors in α/β MB neurons, which are innervated by DPM neurons, inhibited ARM formation. Thus, in addition to the Amnesiac peptide required for anesthesia-sensitive memory formation, the two DPM neurons also release 5HT acting on MB neurons for ARM formation.

Print ISSN: 0027-8424

Digitale ISSN: 1091-6490

Thema: Biologie , Medizin , Allgemeine Naturwissenschaft

Publiziert von National Academy of Sciences

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Hard magnetic property enhancement of Co7Hf-based ribbons by boron doping (2014)

H. W. Chang, M. C. Liao, C. W. Shih, W. C. Chang, C. C. Yang, C. H. Hsiao and H. Ouyang

American Institute of Physics (AIP)

In: Applied Physics Letters

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Publikationsdatum: 2014-11-13

Beschreibung: Hard magnetic property enhancement of melt spun Co 88 Hf 12 ribbons by boron doping is demonstrated. B-doping could not only remarkably enhance the magnetic properties from energy product ((BH) max ) of 2.6 MGOe and intrinsic coercivity ( i H c ) of 1.5 kOe for B-free Co 88 Hf 12 ribbons to (BH) max = 7.7 MGOe and i H c = 3.1 kOe for Co 85 Hf 12 B 3 ribbons but also improve the Curie temperature (T C ) of 7:1 phase. The (BH) max value achieved in Co 85 Hf 12 B 3 ribbons is the highest in Co-Hf alloy ribbons ever reported, which is about 15% higher than that of Co 11 Hf 2 B ribbons spun at 16 m/s [M. A. McGuire, O. Rios, N. J. Ghimire, and M. Koehler, Appl. Phys. Lett. 101 , 202401 (2012)]. The structural analysis confirms that B enters the orthorhombic Co 7 Hf (7:1) crystal structure as interstitial atoms, forming Co 7 HfB x , in the as-spun state. Yet B may diffuse out from the 7:1 phase after post-annealing, leading to the reduction of Curie temperature and the magnetic properties. The uniformly refined microstructure with B-doping results in high remanence (B r ) and improves the squareness of demagnetization curve. The formation of interstitial-atom-modified Co 7 HfB x phase and the microstructure refinement are the main reasons to give rise to the enhancement of hard magnetic properties in the B-containing Co 7 Hf-based ribbons.

Print ISSN: 0003-6951

Digitale ISSN: 1077-3118

Thema: Physik

Publiziert von American Institute of Physics (AIP)

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Structure-based design of non-natural amino-acid inhibitors of amyloid fibril formation (2011)

S. A. Sievers ; J. Karanicolas ; H. W. Chang ; [weitere]

Nature Publishing Group (NPG)

In: Nature. 475(7354): 96-100. doi: 10.1038/nature10154.

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Publikationsdatum: 2011-06-17

Beschreibung: Many globular and natively disordered proteins can convert into amyloid fibrils. These fibrils are associated with numerous pathologies as well as with normal cellular functions, and frequently form during protein denaturation. Inhibitors of pathological amyloid fibril formation could be useful in the development of therapeutics, provided that the inhibitors were specific enough to avoid interfering with normal processes. Here we show that computer-aided, structure-based design can yield highly specific peptide inhibitors of amyloid formation. Using known atomic structures of segments of amyloid fibrils as templates, we have designed and characterized an all-D-amino-acid inhibitor of the fibril formation of the tau protein associated with Alzheimer's disease, and a non-natural L-amino-acid inhibitor of an amyloid fibril that enhances sexual transmission of human immunodeficiency virus. Our results indicate that peptides from structure-based designs can disrupt the fibril formation of full-length proteins, including those, such as tau protein, that lack fully ordered native structures. Because the inhibiting peptides have been designed on structures of dual-beta-sheet 'steric zippers', the successful inhibition of amyloid fibril formation strengthens the hypothesis that amyloid spines contain steric zippers.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4073670/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4073670/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sievers, Stuart A -- Karanicolas, John -- Chang, Howard W -- Zhao, Anni -- Jiang, Lin -- Zirafi, Onofrio -- Stevens, Jason T -- Munch, Jan -- Baker, David -- Eisenberg, David -- P50 AG016570/AG/NIA NIH HHS/ -- R01 AG029430/AG/NIA NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2011 Jun 15;475(7354):96-100. doi: 10.1038/nature10154.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Howard Hughes Medical Institute, UCLA, Box 951970, Los Angeles, California 90095-1570, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21677644" target="_blank"〉PubMed〈/a〉

Schlagwort(e): Amino Acid Sequence ; Amino Acids/*chemistry/*pharmacology ; Amyloid/*antagonists & inhibitors/*chemistry/metabolism ; Amyloid beta-Peptides/antagonists & inhibitors/chemistry/metabolism ; Computer-Aided Design ; *Drug Design ; HIV Infections/virology ; Hydrogen Bonding ; Kinetics ; Models, Molecular ; Peptides/*chemistry/*pharmacology ; Polylysine/pharmacology ; Protein Conformation ; tau Proteins/antagonists & inhibitors

Print ISSN: 0028-0836

Digitale ISSN: 1476-4687

Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik

Publiziert von Nature Publishing Group (NPG)

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Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys (2013)

D. H. Barouch ; J. B. Whitney ; B. Moldt ; [weitere]

Nature Publishing Group (NPG)

In: Nature. 503(7475): 224-8. doi: 10.1038/nature12744.

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Publikationsdatum: 2013-11-01

Beschreibung: Human immunodeficiency virus type 1 (HIV-1)-specific monoclonal antibodies with extraordinary potency and breadth have recently been described. In humanized mice, combinations of monoclonal antibodies have been shown to suppress viraemia, but the therapeutic potential of these monoclonal antibodies has not yet been evaluated in primates with an intact immune system. Here we show that administration of a cocktail of HIV-1-specific monoclonal antibodies, as well as the single glycan-dependent monoclonal antibody PGT121, resulted in a rapid and precipitous decline of plasma viraemia to undetectable levels in rhesus monkeys chronically infected with the pathogenic simian-human immunodeficiency virus SHIV-SF162P3. A single monoclonal antibody infusion afforded up to a 3.1 log decline of plasma viral RNA in 7 days and also reduced proviral DNA in peripheral blood, gastrointestinal mucosa and lymph nodes without the development of viral resistance. Moreover, after monoclonal antibody administration, host Gag-specific T-lymphocyte responses showed improved functionality. Virus rebounded in most animals after a median of 56 days when serum monoclonal antibody titres had declined to undetectable levels, although, notably, a subset of animals maintained long-term virological control in the absence of further monoclonal antibody infusions. These data demonstrate a profound therapeutic effect of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys as well as an impact on host immune responses. Our findings strongly encourage the investigation of monoclonal antibody therapy for HIV-1 in humans.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4017780/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4017780/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barouch, Dan H -- Whitney, James B -- Moldt, Brian -- Klein, Florian -- Oliveira, Thiago Y -- Liu, Jinyan -- Stephenson, Kathryn E -- Chang, Hui-Wen -- Shekhar, Karthik -- Gupta, Sanjana -- Nkolola, Joseph P -- Seaman, Michael S -- Smith, Kaitlin M -- Borducchi, Erica N -- Cabral, Crystal -- Smith, Jeffrey Y -- Blackmore, Stephen -- Sanisetty, Srisowmya -- Perry, James R -- Beck, Matthew -- Lewis, Mark G -- Rinaldi, William -- Chakraborty, Arup K -- Poignard, Pascal -- Nussenzweig, Michel C -- Burton, Dennis R -- AI055332/AI/NIAID NIH HHS/ -- AI060354/AI/NIAID NIH HHS/ -- AI078526/AI/NIAID NIH HHS/ -- AI084794/AI/NIAID NIH HHS/ -- AI095985/AI/NIAID NIH HHS/ -- AI096040/AI/NIAID NIH HHS/ -- AI100148/AI/NIAID NIH HHS/ -- AI10063/AI/NIAID NIH HHS/ -- AI100663/AI/NIAID NIH HHS/ -- P01 AI100148/AI/NIAID NIH HHS/ -- P40 OD012217/OD/NIH HHS/ -- P51 RR000168/RR/NCRR NIH HHS/ -- R01 AI084794/AI/NIAID NIH HHS/ -- R37 AI055332/AI/NIAID NIH HHS/ -- R56 AI091514/AI/NIAID NIH HHS/ -- T32 AI007387/AI/NIAID NIH HHS/ -- U19 AI066305/AI/NIAID NIH HHS/ -- U19 AI078526/AI/NIAID NIH HHS/ -- U19 AI095985/AI/NIAID NIH HHS/ -- U19 AI096040/AI/NIAID NIH HHS/ -- UM1 AI100663/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2013 Nov 14;503(7475):224-8. doi: 10.1038/nature12744. Epub 2013 Oct 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉1] Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts 02215, USA [2] Ragon Institute of MGH, MIT, and Harvard, Cambridge, Massachusetts 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24172905" target="_blank"〉PubMed〈/a〉

Schlagwort(e): Animals ; Antibodies, Monoclonal/*therapeutic use ; Antibodies, Neutralizing/*therapeutic use ; DNA, Viral/blood ; HIV Antibodies/immunology ; HIV-1/*immunology ; Macaca mulatta ; Simian Acquired Immunodeficiency Syndrome/*therapy ; Simian Immunodeficiency Virus/*physiology ; T-Lymphocytes/immunology ; Viremia/therapy

Print ISSN: 0028-0836

Digitale ISSN: 1476-4687

Thema: Biologie , Chemie und Pharmazie , Medizin , Allgemeine Naturwissenschaft , Physik

Publiziert von Nature Publishing Group (NPG)

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