Amanote Research
Register
Sign In
Discover open access scientific publications
Search, annotate, share and cite publications
Publications by Jin-Hua Tian
Ca2+-Dependent Phosphorylation of Syntaxin-1a by the Death-Associated Protein (DAP) Kinase Regulates Its Interaction With Munc18
Journal of Biological Chemistry
Biochemistry
Cell Biology
Molecular Biology
Related publications
DAP-kinase Is a Ca2+/Calmodulin-Dependent, Cytoskeletal-Associated Protein Kinase, With Cell Death-Inducing Functions That Depend on Its Catalytic Activity
EMBO Journal
Immunology
Molecular Biology
Biochemistry
Microbiology
Neuroscience
Medicine
Genetics
Ca2+/Calmodulin-Dependent Protein Kinase II Regulates Tiam1 by Reversible Protein Phosphorylation
Journal of Biological Chemistry
Biochemistry
Cell Biology
Molecular Biology
Phosphorylation of APOBEC3G by Protein Kinase a Regulates Its Interaction With HIV-1 Vif
Nature Structural and Molecular Biology
Structural Biology
Molecular Biology
Regulation of Exocytosis by Cyclin-Dependent Kinase 5 via Phosphorylation of Munc18
Journal of Biological Chemistry
Biochemistry
Cell Biology
Molecular Biology
Phosphorylation-Dependent Reversible Association of Ca2+/Calmodulin-Dependent Protein Kinase II With the Postsynaptic Densities
Journal of Biological Chemistry
Biochemistry
Cell Biology
Molecular Biology
Phosphorylation of the IQ Domain Regulates the Interaction Between Ca2+-Vector Protein and Its Target in Amphioxus
Journal of Biological Chemistry
Biochemistry
Cell Biology
Molecular Biology
Phosphorylation of the Guanine-Nucleotide-Exchange Factor CalDAG-GEFI by Protein Kinase a Regulates Ca2+-Dependent Activation of Platelet Rap1b GTPase
Biochemical Journal
Biochemistry
Cell Biology
Molecular Biology
Ca2+/Calmodulin-Dependent Protein Kinase Kinase Phosphorylation of Sirtuin 1 in Endothelium Is Atheroprotective
Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
Inhibition of Ca2+/Calmodulin-Dependent Protein Kinase II by Arachidonic Acid and Its Metabolites.
Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary