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The Journal of Biological Chemistry|August 30, 1996
Site-specific phosphorylation of synapsin I by mitogen-activated protein kinase and Cdk5 and its effects on physiological functionsM Matsubara, M Kusubata, K Ishiguro, et al.Acta Neuropathologica|September 1, 1996
Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3 beta and cyclin-dependent kinase 5, a component of TPK IIH Yamaguchi, K Ishiguro, T Uchida, et al.Neuroscience Letters|December 14, 1992
Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filamentsK Ishiguro, A Omori, M Takamatsu, et al.Journal of Neurochemistry|February 1, 1993
Tau protein kinase II is involved in the regulation of the normal phosphorylation state of tau proteinM Arioka, M Tsukamoto, K Ishiguro, et al.FEBS Letters|December 6, 1993
A cdc2-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline-directed protein kinase associated with microtubuleS Kobayashi, K Ishiguro, A Omori, et al.The Journal of Biological Chemistry|May 25, 1992
Tau protein kinase I converts normal tau protein into A68-like component of paired helical filamentsK Ishiguro, M Takamatsu, K Tomizawa, et al.FEBS Letters|July 5, 1993
Glycogen synthase kinase 3 beta is identical to tau protein kinase I generating several epitopes of paired helical filamentsK Ishiguro, A Shiratsuchi, S Sato, et al.FEBS Letters|April 4, 1994
Identification of the 23 kDa subunit of tau protein kinase II as a putative activator of cdk5 in bovine brainK Ishiguro, S Kobayashi, A Omori, et al.Journal of Biochemistry|October 2, 1998
Microtubule-stimulated phosphorylation of tau at Ser202 and Thr205 by cdk5 decreases its microtubule nucleation activityY Wada, K Ishiguro, T J Itoh, et al.Journal of Biochemistry|April 1, 1995
Evidence for cdk5 as a major activity phosphorylating tau protein in porcine brain extractT Hosoi, M Uchiyama, E Okumura, et al.Pageof 146