Binding of the proline-rich segment of myelin basic protein to SH3 domains: spectroscopic, microarray, and modeling studies of ligand conformation and effects of posttranslational modifications.
about
Fuzziness: linking regulation to protein dynamicsPhosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosisMyelin management by the 18.5-kDa and 21.5-kDa classic myelin basic protein isoformsAssignment of PolyProline II conformation and analysis of sequence--structure relationshipHair for brain trade-off, a metabolic bypass for encephalizationDocking 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 oligodendrocytesInduced secondary structure and polymorphism in an intrinsically disordered structural linker of the CNS: solid-state NMR and FTIR spectroscopy of myelin basic protein bound to actin.Classic and Golli Myelin Basic Protein have distinct developmental trajectories in human visual cortex.Protein microarrays: novel developments and applications.Structured functional domains of myelin basic protein: cross talk between actin polymerization and Ca(2+)-dependent calmodulin interactionDissecting protein function and signaling using protein microarrays.The multiple roles of myelin protein genes during the development of the oligodendrocyte.Fuzzy complexes of myelin basic protein: NMR spectroscopic investigations of a polymorphic organizational linker of the central nervous system.Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site.Zinc induces disorder-to-order transitions in free and membrane-associated Thellungiella salsuginea dehydrins TsDHN-1 and TsDHN-2: a solution CD and solid-state ATR-FTIR study.Proton detection for signal enhancement in solid-state NMR experiments on mobile species in membrane proteins.Fuzziness enables context dependence of protein interactions.Phosphoproteome analysis of an early onset mouse model (TgCRND8) of Alzheimer's disease reveals temporal changes in neuronal and glia signaling pathways.
P2860
Q22061730-96CBED26-0742-4746-A996-0BFC915E333FQ24311954-4823BD52-AA6E-4F14-80B7-A8E06C9FEEB1Q26860265-B96F446A-2FF2-49F7-A7D6-F8D412454A29Q27348754-2B462255-FBCD-4EFB-8DE2-E7738C2D5525Q28654854-3D1D28AB-9393-4E22-AE88-F591FF400B99Q30008752-17D53F9F-E995-4011-9C44-3B460BDC6246Q30009295-451220EA-116B-4ADC-AAFA-C3C3B715C380Q30009395-ECD9569B-5FF1-494F-9D5C-1BA2F9302A6FQ30009603-54B5E141-EBB6-4CC9-82EB-4942A0035170Q30010178-0432EE76-7DB1-4D96-914F-813BEA4DBADCQ30010240-487FD62A-35A6-4F44-9086-68134F5A4434Q30157404-A76FCC75-873A-45BF-9792-917C032F634CQ30374606-6202369E-FFC7-4225-8DC2-3F0CDBE5E824Q35109872-F9A284E1-AB05-452E-9584-D5348BC94A72Q35187622-64EA1669-6F83-49D7-B51A-E57CDD6902CAQ37574617-D18770B7-BB16-4BA6-A189-4DA6DD3F1E08Q37657601-FC3ABC4A-6B69-4D43-B8F7-D87BBE8881EDQ37746944-9E6272EC-093A-4B85-890E-A851B4A8691CQ38630369-35F8E5F2-9C6F-48E7-A25E-DC36FBB170DCQ39378291-6AA4C48F-A23A-4F23-86CB-0D1AC06AA4CDQ46649963-0242BF7E-630C-499D-9F9A-DA8687463CEAQ48005558-53BB1244-A97E-4D42-B215-1AF457682AADQ48201617-AE1F0587-4524-4CC4-84E8-A9DE0AAD7D04
P2860
Binding of the proline-rich segment of myelin basic protein to SH3 domains: spectroscopic, microarray, and modeling studies of ligand conformation and effects of posttranslational modifications.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Binding of the proline-rich se ...... sttranslational modifications.
@en
type
label
Binding of the proline-rich se ...... sttranslational modifications.
@en
prefLabel
Binding of the proline-rich se ...... sttranslational modifications.
@en
P2093
P356
P1433
P1476
Binding of the proline-rich se ...... sttranslational modifications.
@en
P2093
David S Libich
Godha Rangaraj
Joan M Boggs
P304
P356
10.1021/BI701336N
P407
P577
2007-12-08T00:00:00Z