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  1. Book: Amyloid, prions, and other protein aggregates / C / Ed. by Indu Kheterpal ...

    Wetzel, Ronald

    (Methods in enzymology ; 413)

    2006  

    Author's details ed. by Ronald Wetzel
    Series title Methods in enzymology ; 413
    Amyloid, prions, and other protein aggregates
    Collection Amyloid, prions, and other protein aggregates
    Language English
    Size XXXVI, 375 S. : Ill., graph. Darst.
    Publisher Elsevier
    Publishing place Amsterdam u.a.
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT014894012
    ISBN 978-0-12-182818-9 ; 0-12-182818-2
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Se 222 -413- verfügbar in Königswinter Königswinter

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  2. Book: Amyloid, prions, and other protein aggregates / B

    Wetzel, Ronald

    (Methods in enzymology ; 412)

    2006  

    Author's details ed. by Ronald Wetzel
    Series title Methods in enzymology ; 412
    Amyloid, prions, and other protein aggregates
    Collection Amyloid, prions, and other protein aggregates
    Language English
    Size XL, 403 S. : Ill., graph. Darst.
    Publisher Elsevier
    Publishing place Amsterdam u.a.
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT014899954
    ISBN 978-0-12-182817-2 ; 0-12-182817-4
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Se 222 -412- verfügbar in Königswinter Königswinter

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  3. Article ; Online: Exploding the Repeat Length Paradigm while Exploring Amyloid Toxicity in Huntington's Disease.

    Wetzel, Ronald

    Accounts of chemical research

    2020  Volume 53, Issue 10, Page(s) 2347–2357

    Abstract: Huntington's disease (HD) is a progressive, familial neurodegenerative disease triggered by the expansion of a polyglutamine (polyQ) track in the protein huntingtin (htt). PolyQ sequences up to ... ...

    Abstract Huntington's disease (HD) is a progressive, familial neurodegenerative disease triggered by the expansion of a polyglutamine (polyQ) track in the protein huntingtin (htt). PolyQ sequences up to Q
    MeSH term(s) Amino Acid Sequence ; Amyloid/metabolism ; Animals ; Humans ; Huntingtin Protein/chemistry ; Huntingtin Protein/genetics ; Huntingtin Protein/metabolism ; Huntington Disease/metabolism ; Huntington Disease/pathology ; Kinetics ; Mutagenesis ; PC12 Cells ; Peptides/chemistry ; Peptides/metabolism ; Protein Aggregates ; Rats
    Chemical Substances Amyloid ; Huntingtin Protein ; Peptides ; Protein Aggregates ; polyglutamine (26700-71-0)
    Language English
    Publishing date 2020-09-25
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1483291-4
    ISSN 1520-4898 ; 0001-4842
    ISSN (online) 1520-4898
    ISSN 0001-4842
    DOI 10.1021/acs.accounts.0c00450
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Book ; Collection: Amyloid, prions, and other protein aggregates

    Wetzel, Ronald

    (Methods in enzymology ; ...)

    1999  

    Author's details ed. by Ronald Wetzel
    Series title Methods in enzymology
    ...
    Language English
    Dates of publication 1999-9999
    Publisher Elsevier
    Publishing place Amsterdam u.a.
    Publishing country Netherlands
    Document type Book ; Collection (display volumes)
    Note Hrsg. wechselt
    HBZ-ID HT014894008
    Database Catalogue ZB MED Medicine, Health

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  5. Book: Amyloid, prions, and other protein aggregates / [A]

    Wetzel, Ronald

    (Methods in enzymology ; 309)

    1999  

    Author's details ed. by Ronald Wetzel
    Series title Methods in enzymology ; 309
    Amyloid, prions, and other protein aggregates
    Collection Amyloid, prions, and other protein aggregates
    Keywords Amyloid ; Molekularbiologie ; Prion ; Biochemische Methode ; Enzymologie ; Methode ; Proteine ; Aggregat
    Subject Eiweiss ; Protein ; Molekulare Biologie ; Methodik ; Verfahren ; Technik ; Methoden ; Klinische Enzymologie ; Aggregiertes System
    Language English
    Size XXXIX, 820 S. : Ill., graph. Darst.
    Publisher Elsevier
    Publishing place Amsterdam u.a.
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT011091122
    ISBN 0-12-182210-9 ; 978-0-12-182210-1
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Se 222 -309- verfügbar in Königswinter Königswinter

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  6. Article ; Online: Physical chemistry of polyglutamine: intriguing tales of a monotonous sequence.

    Wetzel, Ronald

    Journal of molecular biology

    2012  Volume 421, Issue 4-5, Page(s) 466–490

    Abstract: Polyglutamine (polyQ) sequences of unknown normal function are present in a significant number of proteins, and their repeat expansion is associated with a number of genetic neurodegenerative diseases. PolyQ solution structure and properties are ... ...

    Abstract Polyglutamine (polyQ) sequences of unknown normal function are present in a significant number of proteins, and their repeat expansion is associated with a number of genetic neurodegenerative diseases. PolyQ solution structure and properties are important not only because of the normal and abnormal biology associated with these sequences but also because they represent an interesting case of a biologically relevant homopolymer. As the common thread in expanded polyQ repeat diseases, it is important to understand the structure and properties of simple polyQ sequences. At the same time, experience has shown that sequences attached to polyQ, whether in artificial constructs or in disease proteins, can influence structure and properties. The two major contenders for the molecular source of the neurotoxicity implicit in polyQ expansion within disease proteins are a populated toxic conformation in the monomer ensemble and a toxic aggregated species. This review summarizes experimental and computational studies on the solution structure and aggregation properties of both simple and complex polyQ sequences, and their repeat-length dependence. As a representative of complex polyQ proteins, the behavior of huntingtin N-terminal fragments, such as exon-1, receives special attention.
    MeSH term(s) Chemistry, Physical ; Computer Simulation ; Humans ; Models, Molecular ; Neurodegenerative Diseases/pathology ; Neurodegenerative Diseases/physiopathology ; Peptides/chemistry
    Chemical Substances Peptides ; polyglutamine (26700-71-0)
    Language English
    Publishing date 2012-01-27
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2012.01.030
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 867: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  7. Article: Amyloid fibrils--common threads in the natural history of proteins.

    Wetzel, Ronald

    Accounts of chemical research

    2006  Volume 39, Issue 9, Page(s) 567

    Language English
    Publishing date 2006-09
    Publishing country United States
    Document type Editorial
    ZDB-ID 1483291-4
    ISSN 1520-4898 ; 0001-4842
    ISSN (online) 1520-4898
    ISSN 0001-4842
    DOI 10.1021/ar0681934
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article: Physical Chemistry of Polyglutamine: Intriguing Tales of a Monotonous Sequence

    Wetzel, Ronald

    Journal of molecular biology. 2012 Aug. 24, v. 421, no. 4-5

    2012  

    Abstract: Polyglutamine (polyQ) sequences of unknown normal function are present in a significant number of proteins, and their repeat expansion is associated with a number of genetic neurodegenerative diseases. PolyQ solution structure and properties are ... ...

    Abstract Polyglutamine (polyQ) sequences of unknown normal function are present in a significant number of proteins, and their repeat expansion is associated with a number of genetic neurodegenerative diseases. PolyQ solution structure and properties are important not only because of the normal and abnormal biology associated with these sequences but also because they represent an interesting case of a biologically relevant homopolymer. As the common thread in expanded polyQ repeat diseases, it is important to understand the structure and properties of simple polyQ sequences. At the same time, experience has shown that sequences attached to polyQ, whether in artificial constructs or in disease proteins, can influence structure and properties. The two major contenders for the molecular source of the neurotoxicity implicit in polyQ expansion within disease proteins are a populated toxic conformation in the monomer ensemble and a toxic aggregated species. This review summarizes experimental and computational studies on the solution structure and aggregation properties of both simple and complex polyQ sequences, and their repeat-length dependence. As a representative of complex polyQ proteins, the behavior of huntingtin N-terminal fragments, such as exon-1, receives special attention.
    Keywords neurodegenerative diseases ; neurotoxicity ; physical chemistry ; proteins
    Language English
    Dates of publication 2012-0824
    Size p. 466-490.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2012.01.030
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 4' 63/108: Show issues

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  9. Article: [Besprechung von:] Buckland, William R. and Ronald A. Fox: Bibliography of basis texts and monographs on statistical methods 1945-1960. 2 ed. Edinburgh and London 1963

    Wetzel, Wolfgang / Buckland, William R

    Weltwirtschaftliches Archiv : Zeitschrift des Instituts für Weltwirtschaft an der Universität Kiel Vol. 98, No. 1 , p. 42-43

    1967  Volume 98, Issue 1, Page(s) 42–43

    Author's details Wolfgang Wetzel
    Publisher Mohr
    Publishing place Tübingen
    Document type Article
    ZDB-ID 518-6
    Database ECONomics Information System

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  10. Article: Kinetics and thermodynamics of amyloid fibril assembly.

    Wetzel, Ronald

    Accounts of chemical research

    2006  Volume 39, Issue 9, Page(s) 671–679

    Abstract: With some exceptions, amyloids appear to be accidental aggregated structures whose formation was not selected for in molecular evolution. Despite this, amyloid fibrils are in many respects surprisingly well-behaved molecules. For example, Huntington's ... ...

    Abstract With some exceptions, amyloids appear to be accidental aggregated structures whose formation was not selected for in molecular evolution. Despite this, amyloid fibrils are in many respects surprisingly well-behaved molecules. For example, Huntington's disease-related polyglutamine sequences aggregate via a relatively simple nucleated growth polymerization mechanism. In addition, the Alzheimer's plaque protein Abeta has been shown to undergo reversible amyloid fibril formation to a position of dynamic equilibrium such that reaction thermodynamics can be quantified. Studies of these well-behaved amyloid systems are allowing us to peer more deeply into the process and products of off-pathway misfolding and aggregation.
    MeSH term(s) Amyloid/chemistry ; Kinetics ; Thermodynamics
    Chemical Substances Amyloid
    Language English
    Publishing date 2006-09
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 1483291-4
    ISSN 1520-4898 ; 0001-4842
    ISSN (online) 1520-4898
    ISSN 0001-4842
    DOI 10.1021/ar050069h
    Database MEDical Literature Analysis and Retrieval System OnLINE

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