ProQuest

Deep Indexing added to selected databases

The Melting World of Penguins

 
About CSA Products Support & Training News and Events Discovery Guides Contact Us
Quick Links
> Field Codes
> Serials Source List
> Thesaurus
 
 

CSA Neurosciences Abstracts

 
 
    This database enables neuroscientists to keep abreast of major advances within the field and their implications for other medical specialties. The database covers all aspects of vertebrate and invertebrate neuroscience, emphasizing basic research but also including such devastating neural diseases as Alzheimer's.
Subject Coverage
    Major areas of coverage include:
    • Motor Systems
    • Somatosensory Systems
    • Pain and Analgesia
    • Visual Systems
    • Auditory and Vestibular Systems
    • Taste, Smell, and Chemical Senses
    • Electrical and Magnetic Senses
    • Sonar, Lateral Line, and Other Senses
    • Neuroanatomy, Histology, and Cytology
    • Neural Growth and Development
    • Neurophysiology
    • Neurochemistry and Cell Biology
    • Molecular Neurobiology
    • Neuroendocrinology
    • Neuroimmunology
    • Neurogenetics
    • Neuropharmacology
    • Neurotoxicology, Drugs of Abuse
    • Aging, Neurodegeneration, and Repair
    • Memory, Learning, Neuropsychology, and Language
    • Alzheimer's Disease and Other Dementias
    • Experimental Neuropathology
    • Neural Correlates of Behavior
    • Neural Networks and Computation
    • Neuroimaging Techniques
    • Methods and Apparatus
Dates of Coverage
    1982 - currrent
Update Frequency
    Monthly, with approximately 1,200 new records added
Size
    Over 0 records as of May 2013
Print Equivalent
    CSA Neurosciences Abstracts (v.1-v.21, 1983-2003)
Supplier
    Proquest
    789 E. Eisenhower Parkway
    P.O. Box 1346
    Ann Arbor, MI 48106-1346
    Tel: +1-734-761-4700
Sample Record

    TI:

    Title
    Binding of alpha-Synuclein Affects the Lipid Packing in Bilayers of Small Vesicles

    AU:

    Author
    Kamp, Frits; Beyer, Klaus

    AF:

    Author Affiliation
    Laboratory of Alzheimer's and Parkinson's Disease Research, Department of Biochemistry, Ludwig Maximilian University, 80336 Munich, Germany

    SO:

    Source
    Journal of Biological Chemistry [J. Biol. Chem.]. Vol. 281, no. 14, pp. 9251-9259. 7 Apr 2006.

    IS:

    ISSN
    0021-9258

    EI:

    Electronic ISSN
    1083-351X

    DE:

    Descriptors
    Synuclein; Anisotropy; Temperature effects; Packing; fluorescence spectroscopy; Hydrophobicity; Neurodegenerative diseases; Movement disorders; Cooperativity; Phospholipids; sphingomyelin; Synaptic vesicles; Parkinson's disease; Cholesterol

    AB:

    Abstract
    The intracellular deposition of fibrillar aggregates of alpha-synuclein is a characteristic feature of Parkinson disease. Alternatively, as a result of its unusual conformational plasticity, alpha-synuclein may fold into an amphipathic helix upon contact with a lipid-water interface. Using spin label ESR and fluorescence spectroscopy, we show here that alpha-synuclein affects the lipid packing in small unilamellar vesicles. The ESR hyperfine splittings of spin-labeled phospholipid probes revealed that alpha-synuclein induces chain ordering at carbon 14 of the acyl chains below the chain melting phase transition temperature but not in the liquid crystalline state of electroneutral vesicle membranes. Binding of alpha-synuclein leads to an increase in the temperature and cooperativity of the phase transition according to the fluorescence anisotropy of the hydrophobic polyene 1,6-diphenylhexatriene and of the fluorescence emission maxima of the amphiphilic probe 6-dodecanoyl-2-dimethylaminonaphthalene. Binding parameters were obtained from the fluorescence anisotropy measurements in combination with our previous determinations by titration calorimetry (Nuscher, B., Kamp, F., Mehnert, T., Odoy, S., Haass, C., Kahle, P. J., and Beyer, K. (2004) J. Biol. Chem. 279, 21966-21975). We also show that alpha-synuclein interacts with vesicle membranes containing sphingomyelin and cholesterol. We propose that the protein is capable of annealing defects in curved vesicle membranes, which may prevent synaptic vesicles from premature fusion.

    LA:

    Language
    English

    SL:

    Summary Language
    English

    PY:

    Publication Year
    2006

    PT:

    Publication Type
    Journal Article

    PB:

    Publisher
    American Society for Biochemistry and Molecular Biology, 9650 Rockville Pike Bethesda MD 20814-3996 USA, asbmb@asbmb.faseb.org, http://www.jbc.org

    CL:

    Classification
    N3 11071 Membranes, receptors, and channels

    UD:

    Update
    200604

    SF:

    Subfile
    CSA Neurosciences Abstracts

    AN:

    Accession Number
    6747828

    PG:

    Journal Pages
    9251-9259

    JV:

    Journal Volume
    281

    JI:

    Journal Issue
    14

Field Codes
    The following field codes are found in the records of this database. Here they are listed in alphabetical order by two-letter code. See Field Codes and Search Examples for detailed descriptions and search examples.

    AB = Abstract LA = Language
    AF = Author Affiliation NT = Notes
    AN = Accession Number NU = Other Numbers
    AU = Authors OT = Original Title
    CA = Corporate Author PB = Publisher
    CF = Conference PT = Publication Type
    CL = Classification PY = Publication Year
    DE = Descriptors SF = Subfile
    ED = Editor SL = Summary Language
    ER = Environmental Regime SO = Source
    IB = ISBN TI = Title
    ID = Identifiers TR = ASFA Input Center Number
    IS = ISSN UD = Update