Conformational choreography of a molecular switch region in myelin basic protein--molecular dynamics shows induced folding and secondary structure type conversion upon threonyl phosphorylation in both aqueous and membrane-associated environments.
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Myelin management by the 18.5-kDa and 21.5-kDa classic myelin basic protein isoformsAtomic resolution view into the structure–function relationships of the human myelin peripheral membrane protein P2Docking and molecular dynamics simulations of the Fyn-SH3 domain with free and phospholipid bilayer-associated 18.5-kDa myelin basic protein (MBP)-Insights into a noncanonical and fuzzy interaction.The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro.Interaction of myelin basic protein with cytoskeletal and signaling proteins in cultured primary oligodendrocytes and N19 oligodendroglial cells.The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein.Classic 18.5- and 21.5-kDa myelin basic protein isoforms associate with cytoskeletal and SH3-domain proteins in the immortalized N19-oligodendroglial cell line stimulated by phorbol ester and IGF-1.Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5-kDa myelin basic protein decrease its affinity for the Fyn-SH3 domain and alter process development and protein localization in oligodendrocytesStructured functional domains of myelin basic protein: cross talk between actin polymerization and Ca(2+)-dependent calmodulin interactionMyelin architecture: zippering membranes tightly together.Molecular dynamics simulations and conductance studies of the interaction of VP1 N-terminus from Polio virus and gp41 fusion peptide from HIV-1 with lipid membranes.Computational comparison of two new fusion proteins for multiple sclerosis
P2860
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P2860
Conformational choreography of a molecular switch region in myelin basic protein--molecular dynamics shows induced folding and secondary structure type conversion upon threonyl phosphorylation in both aqueous and membrane-associated environments.
description
2010 nî lūn-bûn
@nan
2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Conformational choreography of ...... brane-associated environments.
@ast
Conformational choreography of ...... brane-associated environments.
@en
type
label
Conformational choreography of ...... brane-associated environments.
@ast
Conformational choreography of ...... brane-associated environments.
@en
prefLabel
Conformational choreography of ...... brane-associated environments.
@ast
Conformational choreography of ...... brane-associated environments.
@en
P921
P1476
Conformational choreography of ...... brane-associated environments.
@en
P2093
D Peter Tieleman
Eoin P Coll
P304
P356
10.1016/J.BBAMEM.2010.11.030
P407
P577
2010-12-03T00:00:00Z