Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure.

Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

  • Abstract Text of This Paper
  • Journal Published
  • MeSH Keywords of This Abstract
  • Chemicals and Substances Used in this Paper
  • Grants and Granting Agency of this Research
  • Database Accession Numbers Used in this Paper
  • Related Papers
  • Related Research Tags
  • Rate this Research Paper
  • Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Abstract Text:

    jie zhengJie Zheng,buyong maBuyong Ma,ruth nussinovRuth Nussinov,

    Amyloid fibrils characterized as highly intractable thread-like species are associated with many neurodegenerative diseases. Although neither the mechanism of amyloid formation nor the origin of amyloid toxicity is currently completely understood, the detailed three-dimensional atomic structures of the yeast protein Sup35 and Abeta amyloid protein determined by recent experiments provide the first and important step towards the comprehension of the pathogenesis and aggregation mechanisms of amyloid diseases. By analyzing these two amyloid peptides which have available crystal structures and other amyloid sequences with proposed structures using computational simulations, we delineate three common features in amyloid organizations and amyloid structures. These could contribute to an improved understanding of the molecular mechanism of amyloid formation, the nature of the aggregation driving forces that stabilize these structures and the development of potential therapeutic agents against amyloid diseases.

    Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Publishing Authors By Initials

    j zhengJ Zheng,b maB Ma,r nussinovR Nussinov,

    For similar proteins: fungal proteins: saccharomyces cerevisiae proteins research abstracts see: proteins: fungal proteins: saccharomyces cerevisiae proteins research

    PUBMED ID PMID:

    MEDLINE DATE:

    Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Physical biology

    VOLUME: 3

    Page Numbers: P1-4

    Journal Abbreviation:

    ISSN: 1478-3975

    DAY: 3

    MONTH: 10

    YEAR: 2006

    Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 101197454

    Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Keywords Mesh Terms:

    KEYWORDS: Saccharomyces cerevisiae Proteins

    MESH TERMS: chemistry

    Chemical & Substance for Abstract: Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure. Information

    Substance Name: SUP35 protein, S cerevisiae

    Registry Number: 133737-87-8

    Grant and Affiliation Information for Consensus features in amyloid fibrils: sheet-sheet recognition via a (polar or nonpolar) zipper structure.

    AFFILIATION: Basic Research Program, SAIC-Frederick, Inc., Center for Cancer Research Nanobiology Program, NCI-Frederick, Frederick, MD 21702, USA.

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY: United States NCI

    GRANT: N01-CO-12400

    ACRONYM: CO

    MEDLINETA: Phys Biol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Consensus features in amyloid fibrils: sheet-sheet recognition via a polar or nonpolar zipper structure Related Publications

     

    Molecular Station USER Menu

    Welcome to Molecular Station!

    You have to register before you can post on our forums or use our advanced features. Register Now! Its Free and Fast!

    Already registered? Login now below.

    User Name:

    Password:

    Already registered and Forgot your password? Click below to recover it.

    Recover Lost Password

    Join now - it's fast and free!

    Molecular Station is THE largest network of researchers, scientists and science lovers anywhere!

    Research Terms of Usage and Disclaimer
    Home
    Features

    Protocols

    DNA Forum

    Science Forum

    DNA Forum
    Biology Forum

    Science News


    [CaRP] XML error: Invalid document end at line 2

    For more click here:Science News