Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1471-2202
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Structure and regulation of MARK, a kinase involved in abnormal phosphorylation of Tau protein ; volume:9 ; number:2 ; day:3 ; month:12 ; year:2008 ; pages:1-6 ; date:12.2008
BMC neuroscience ; 9, Heft 2 (3.12.2008), 1-6, 12.2008
- Urheber
-
Timm, Thomas
- Beteiligte Personen und Organisationen
-
Marx, Alexander
Panneerselvam, Saravanan
Mandelkow, Eckhard
Mandelkow, Eva-Maria
SpringerLink (Online service)
- DOI
-
10.1186/1471-2202-9-S2-S9
- URN
-
urn:nbn:de:1111-2016032059753
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
- 14.08.2025, 10:55 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Timm, Thomas
- Marx, Alexander
- Panneerselvam, Saravanan
- Mandelkow, Eckhard
- Mandelkow, Eva-Maria
- SpringerLink (Online service)
Ähnliche Objekte (12)
Critical residues involved in tau binding to fyn: implications for tau phosphorylation in Alzheimer’s disease
Abnormal Localization and Accumulation of FLT3-ITD, a Mutant Receptor Tyrosine Kinase Involved in Leukemogenesis
A new TAO kinase inhibitor reduces tau phosphorylation at sites associated with neurodegeneration in human tauopathies
Abeta is prerequisite, but insufficient to cause tau phosphorylation in vivo: tau phosphorylation in APP mice by diabetes
Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin
Tau phosphorylation regulates the interaction between BIN1’s SH3 domain and Tau’s proline-rich domain
Reversible tau phosphorylation and neuronal plasticity in mammalian hibernation
Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C
Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
Abnormal hematopoietic phenotypes in Pim kinase triple knockout mice
Phosphorylation of nuclear Tau is modulated by distinct cellular pathways
Tau phosphorylation by GSK-3β promotes tangle-like filament morphology
Critical residues involved in tau binding to fyn: implications for tau phosphorylation in Alzheimer’s disease
Abnormal Localization and Accumulation of FLT3-ITD, a Mutant Receptor Tyrosine Kinase Involved in Leukemogenesis
A new TAO kinase inhibitor reduces tau phosphorylation at sites associated with neurodegeneration in human tauopathies
Abeta is prerequisite, but insufficient to cause tau phosphorylation in vivo: tau phosphorylation in APP mice by diabetes
Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin
Tau phosphorylation regulates the interaction between BIN1’s SH3 domain and Tau’s proline-rich domain
Reversible tau phosphorylation and neuronal plasticity in mammalian hibernation
Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C
Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
Abnormal hematopoietic phenotypes in Pim kinase triple knockout mice
Phosphorylation of nuclear Tau is modulated by distinct cellular pathways
Tau phosphorylation by GSK-3β promotes tangle-like filament morphology
Critical residues involved in tau binding to fyn: implications for tau phosphorylation in Alzheimer’s disease
Abnormal Localization and Accumulation of FLT3-ITD, a Mutant Receptor Tyrosine Kinase Involved in Leukemogenesis
A new TAO kinase inhibitor reduces tau phosphorylation at sites associated with neurodegeneration in human tauopathies
Abeta is prerequisite, but insufficient to cause tau phosphorylation in vivo: tau phosphorylation in APP mice by diabetes
Phosphorylation regulates tau’s phase separation behavior and interactions with chromatin
Tau phosphorylation regulates the interaction between BIN1’s SH3 domain and Tau’s proline-rich domain
Reversible tau phosphorylation and neuronal plasticity in mammalian hibernation
Myomegalin is a novel A-kinase anchoring protein involved in the phosphorylation of cardiac myosin binding protein C
Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation
Abnormal hematopoietic phenotypes in Pim kinase triple knockout mice
Phosphorylation of nuclear Tau is modulated by distinct cellular pathways