Special Feature

User Panel

My Panel

My Panel

Bookmark Science Articles

Recent News
Bookmark / Share This Science Site

The RASSF1A tumor suppressor.

The RASSF1A tumor suppressor. 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
  • The RASSF1A tumor suppressor. Abstract Text:

    howard donningerHoward Donninger,michele d vosMichele D Vos,geoffrey j clarkGeoffrey J Clark,

    RASSF1A (Ras association domain family 1 isoform A) is a recently discovered tumor suppressor whose inactivation is implicated in the development of many human cancers. Although it can be inactivated by gene deletion or point mutations, the most common contributor to loss or reduction of RASSF1A function is transcriptional silencing of the gene by inappropriate promoter methylation. This epigenetic mechanism can inactivate numerous tumor suppressors and is now recognized as a major contributor to the development of cancer. RASSF1A lacks apparent enzymatic activity but contains a Ras association (RA) domain and is potentially an effector of the Ras oncoprotein. RASSF1A modulates multiple apoptotic and cell cycle checkpoint pathways. Current evidence supports the hypothesis that it serves as a scaffold for the assembly of multiple tumor suppressor complexes and may relay pro-apoptotic signaling by K-Ras.

    The RASSF1A tumor suppressor. Publishing Authors By Initials

    h donningerH Donninger,md vosMD Vos,gj clarkGJ Clark,

    For similar enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: ras proteins research abstracts see: enzymes and coenzymes: enzymes: hydrolases: acid anhydride hydrolases: gtp phosphohydrolases: gtp-binding proteins: monomeric gtp-binding proteins: ras proteins research

    PUBMED ID PMID:

    MEDLINE DATE:

    The RASSF1A tumor suppressor. Journal Published:

    PUBLICATION TYPE: Review

    Journal: Journal of cell science

    VOLUME: 120

    Page Numbers: 3163-72

    Journal Abbreviation: J. Cell. Sci.

    ISSN: 0021-9533

    DAY: 15

    MONTH: Sep

    YEAR: 2007

    The RASSF1A tumor suppressor. Information

    Number of References: 132

    LANGUAGE: eng

    NlmUniqueID: 52457

    The RASSF1A tumor suppressor. Keywords Mesh Terms:

    KEYWORDS: ras Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: The RASSF1A tumor suppressor. Information

    Substance Name: ras Proteins

    Registry Number: EC 3.6.5.2

    Grant and Affiliation Information for The RASSF1A tumor suppressor.

    AFFILIATION: Molecular Targets Group, Department of Medicine, J. G. Brown Cancer Center, University of Louisville, 119C Baxter Boulevard, 580 S. Preston Street, Louisville, KY 40202, USA.

    Country: England

    England Research PublicationEngland Research Publication

    AGENCY:

    GRANT:

    ACRONYM:

    MEDLINETA: J Cell Sci

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    The RASSF1A tumor suppressor 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