Massoulie_2008_Chem.Biol.Interact_175_30

Reference

Title : Old and new questions about cholinesterases - Massoulie_2008_Chem.Biol.Interact_175_30
Author(s) : Massoulie J , Perrier N , Noureddine H , Liang D , Bon S
Ref : Chemico-Biological Interactions , 175 :30 , 2008
Abstract : Cholinesterases have been intensively studied for a long time, but still offer many fascinating and fundamental questions regarding their evolution, activity, biosynthesis, folding, post-translational modifications, association with structural proteins (ColQ, PRiMA and maybe others), export or degradation. They constitute an excellent model to study these processes, particularly because of the sensitivity and specificity of enzymic assays. In addition, a number of provocative ideas concerning their proposed non-conventional, or non-catalytic functions deserve to be further documented.
ESTHER : Massoulie_2008_Chem.Biol.Interact_175_30
PubMedSearch : Massoulie_2008_Chem.Biol.Interact_175_30
PubMedID: 18541228

Related information

Family ACHEBCHECholinesterase

Citations formats

Massoulie J, Perrier N, Noureddine H, Liang D, Bon S (2008)
Old and new questions about cholinesterases
Chemico-Biological Interactions 175 :30

Massoulie J, Perrier N, Noureddine H, Liang D, Bon S (2008)
Chemico-Biological Interactions 175 :30

Array
(
    [id] => 198151
    [paper] => Massoulie_2008_Chem.Biol.Interact_175_30
    [author] => Massoulie J || Perrier N || Noureddine H || Liang D || Bon S
    [year] => 2008
    [title] => Old and new questions about cholinesterases
    [journal] => Chemico-Biological Interactions
    [volume] => 175
    [page] => 30
    [medline] => 18541228
    [abstract] => Massoulie_2008_Chem.Biol.Interact_175_30
    [kin_reference] => 
    [mutation] => 
    [kinetic_parameter] => 
    [inhibitor] => 
    [kin_value] => 
    [substrate] => 
    [gene_locus] => Array
        (
        )

    [family] => ACHE || BCHE || Cholinesterase
    [interact_gene_locus] => 
    [xenobiotic_sensitivity] => 
    [news] => 
    [likid_reference] => 
    [lip_reference] => 
    [gene_locus_frgt] => 
    [structure] => 
    [comment] => 
    [chemical] => 
    [arpigny_jaeger] => 
    [reactivator] => 
    [disease] => 
    [enzyme] => 
    [risk_factor] => 
    [tissue] => 
    [sub_tissue] => 
    [activity] => 
    [specific_activity] => 
    [disease_by_interaction] => 
    [abstract_text] => Array
        (
            [id] => 148159
            [longtext] => Massoulie_2008_Chem.Biol.Interact_175_30
            [content] => Cholinesterases have been intensively studied for a long time, but still offer many fascinating and fundamental questions regarding their evolution, activity, biosynthesis, folding, post-translational modifications, association with structural proteins (ColQ, PRiMA and maybe others), export or degradation. They constitute an excellent model to study these processes, particularly because of the sensitivity and specificity of enzymic assays. In addition, a number of provocative ideas concerning their proposed non-conventional, or non-catalytic functions deserve to be further documented.
        )

)