Search Results - (Author, Cooperation:W. C. Tseng)

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  1. 1
    Staff View
    Publication Date:
    2013-04-23
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Animals ; Arrestins/*chemistry/immunology/*metabolism ; Crystallography, X-Ray ; Humans ; Immunoglobulin Fab Fragments/chemistry/immunology/metabolism ; Models, Molecular ; Phosphopeptides/*chemistry/*metabolism ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Stability ; Rats ; Receptors, Vasopressin/*chemistry ; Rotation
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Staff View
    Publication Date:
    2018-03-07
    Publisher:
    American Physical Society (APS)
    Print ISSN:
    1098-0121
    Electronic ISSN:
    1095-3795
    Topics:
    Physics
    Keywords:
    Structure, structural phase transitions, mechanical properties, defects
    Published by:
    http://www.aps.org/

    Latest Papers from Table of Contents or Articles in Press
  3. 3
    Lu, L.W. ; Chiang, G.H. ; Tseng, W.-C. ; Randerath, K.

    Amsterdam : Elsevier
    Staff View
    ISSN:
    0006-291X
    Source:
    Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics:
    Biology
    Chemistry and Pharmacology
    Physics
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1016/0006-291X(76)90233-3

    Articles: DFG German National Licenses
  4. 4
    Lin, T. -H. ; Huang, Y. -L. ; Tseng, W. -C.
    Springer
    Published 1995
    Staff View
    ISSN:
    1432-0800
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Energy, Environment Protection, Nuclear Power Engineering
    Medicine
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00192589

    Articles: DFG German National Licenses
  5. 5
    Lin, Shoei-Yn Shiau ; Tseng, W. C. ; Lee, C. Y.
    Springer
    Published 1975
    Staff View
    ISSN:
    1432-1912
    Keywords:
    Contracture ; Spontaneous Contractions ; Cations ; Procaine ; Tetrodotoxin
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Summary 1. Scorpion toxin II is potent in inducing contracture and spontaneous contractions of the chick biventer cervicis muscle. In addition, this toxin induces membrane depolarization and blockade of neuromuscular transmission in this muscle preparation. The purpose of the present study is to explore the possible mechanism of actions of toxin II. 2. The muscle contracture induced by toxin II is moderately accelerated by Ca2+-free Krebs solution, delayed by high Ca2+ (10 mM), high Mg2+ (10 mM) and low Na+ (60 mM) Krebs solution. Moreover, this action is inhibited slightly by d-tubocurarine and completely by either procaine or tetrodotoxin, but unaffected by β-bungarotoxin. All these findings suggest that toxin II induces contracture mainly by increasing the Na+ permeability of the muscle membrane. 3. Spontaneous contractions induced by toxin II are abolished by Ca2+-free Krebs solution, inhibited partially by either d-tubocurarine or β-bungarotoxin and completely by tetrodotoxin or procaine. These results suggest that toxin II induces spontaneous contractions partially by releasing acetylcholine from nerve endings and partially by increasing the Na+ permeability of the muscle membrane
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00508410

    Articles: DFG German National Licenses
  6. 6
    Staff View
    ISSN:
    1432-1912
    Keywords:
    Direct Hemolysis ; Contracture ; Local Irritation ; Anticholinesterase ; Mitochondria
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Medicine
    Notes:
    Summary The actions of cardiotoxin (CTX), melittin and prymnesin were compared on dog erythrocytes, chicken biventer, chicken biventer cervicis muscle, rabbit conjunctiva, acetylcholinesterase, succinate-cytochrome c reductase and turbidity of the rat liver mitochondrial suspension. 1. CTX and melittin were approximately equipotent in the various biological activities, while prymnesin was not. 2. The rate of direct hemolysis induced by CTX was slow, while that induced by either melittin or prymnesin was fast. 3. Phosphate ions, 10mM Ca++, as well as 1 mM reduced glutathione, considerably inhibited the CTX-induced hemolysis, but only slightly inhibited that induced by melittin or prymnesin. 4. CTX, melittin and prymnesin caused contracture of the chicken biventer cervicis muscle. Prymnesin was much less active in this preparation as compared with its hemolytic potency. The CTX contracture was completely inhibited by high Ca++ (10 mM) medium, while the melittin contracture was not. 5. The rate of CTX contracture to reach the peak tension was increased when the concentration of CTX was increased, while the rate of melittin contracture did not change very much as the concentrations varied. 6. All three toxins caused a local irritation of the conjunctival sac of the rabbit eye. 7. Both CTX and melittin inhibited acetylcholinesterase and succinate-cytochrome c reductase activities, and also increased the turbidity of the rat liver mitochondrial suspension, while prymnesin was totally inactive in these respects. It is concluded that the mechanism of actions of these toxins may be different at the molecular level. The role of the detergent properties of these toxins in their biological activities is discussed.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00500037

    Articles: DFG German National Licenses