τ is phosphorylated by GSK‐3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A‐kinase

[1]  Khadija Iqbal,et al.  Abnormal phosphorylation of tau and the mechanism of Alzheimer neurofibrillary degeneration: sequestration of microtubule-associated proteins 1 and 2 and the disassembly of microtubules by the abnormal tau. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[2]  I. Grundke‐Iqbal,et al.  Glycosylation of microtubule–associated protein tau: An abnormal posttranslational modification in Alzheimer's disease , 1996, Nature Medicine.

[3]  Alejandra del C. Alonso,et al.  Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules , 1996, Nature Medicine.

[4]  Khadija Iqbal,et al.  Calcium/calmodulin‐dependent protein kinase II phosphorylates tau at Ser‐262 but only partially inhibits its binding to microtubules , 1996, FEBS letters.

[5]  I. Grundke‐Iqbal,et al.  Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1. , 1996, Brain research. Molecular brain research.

[6]  I. Grundke‐Iqbal,et al.  Alzheimer abnormally phosphorylated tau is more hyperphosphorylated than the fetal tau and causes the disruption of microtubules , 1995, Neurobiology of Aging.

[7]  E. Mandelkow,et al.  Microtubule-associated Protein/Microtubule Affinity-regulating Kinase (p110mark) , 1995, The Journal of Biological Chemistry.

[8]  I. Grundke‐Iqbal,et al.  Dephosphorylation of Alzheimer Paired Helical Filaments by Protein Phosphatase-2A and −2B (*) , 1995, The Journal of Biological Chemistry.

[9]  Khadija Iqbal,et al.  Modulation of GSK‐3‐catalyzed phosphorylation of microtubule‐associated protein tau by non‐proline‐dependent protein kinases , 1995, FEBS letters.

[10]  K. Titani,et al.  Proline-directed and Non-proline-directed Phosphorylation of PHF-tau (*) , 1995, The Journal of Biological Chemistry.

[11]  I. Grundke‐Iqbal,et al.  Alzheimer paired helical filaments Restoration of the biological activity by dephosphorylation , 1994, FEBS letters.

[12]  Khadija Iqbal,et al.  Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[13]  C. W. Scott,et al.  Casein kinase II preferentially phosphorylates human tau isoforms containing an amino-terminal insert. Identification of threonine 39 as the primary phosphate acceptor. , 1994, The Journal of biological chemistry.

[14]  E. Mandelkow,et al.  Abnormal Alzheimer‐like phosphorylation of tau‐protein by cyclin‐dependent kinases cdk2 and cdk5 , 1993, FEBS letters.

[15]  Jen‐Shin Song,et al.  Protein Kinase FA/GSK‐3 Phosphorylates on Ser235‐Pro and Ser404‐Pro that Are Abnormally Phosphorylated in Alzheimer's Disease Brain , 1993, Journal of neurochemistry.

[16]  K. Imahori,et al.  Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments , 1993 .

[17]  E. Mandelkow,et al.  Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding , 1993, Neuron.

[18]  J. Trojanowski,et al.  The abnormal phosphorylation of tau protein at Ser-202 in Alzheimer disease recapitulates phosphorylation during development. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[19]  C. W. Scott,et al.  Phosphorylation of tau by proline-directed protein kinase (p34cdc2/p58cyclin A) decreases tau-induced microtubule assembly and antibody SMI33 reactivity , 1993, Brain Research.

[20]  W. T. Moore,et al.  Application of synthetic phospho‐ and unphospho‐ peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease , 1993, Journal of neuroscience research.

[21]  G. Drewes,et al.  Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau , 1992, FEBS letters.

[22]  R. Braun,et al.  Proline-directed phosphorylation of human Tau protein. , 1992, The Journal of biological chemistry.

[23]  P. Cohen,et al.  p42 map kinase phosphorylation sites in microtubule‐associated protein tau are dephosphorylated by protein phosphatase 2A1 Implications for Alzheimer's disease , 1992, FEBS letters.

[24]  Jen‐Shin Song,et al.  Identification of the ATP·Mg-dependent protein phosphatase activator (Fa) as a synapsin I kinase that inhibits cross-linking of synapsin I with brain microtubules , 1992, Journal of protein chemistry.

[25]  V. Lee,et al.  Immunological and conformational characterization of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's disease , 1992 .

[26]  K. Titani,et al.  Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain. , 1992, The Journal of biological chemistry.

[27]  J. Ávila,et al.  Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain. , 1992, The Journal of biological chemistry.

[28]  G. Drewes,et al.  Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state. , 1992, The EMBO journal.

[29]  K. Imahori,et al.  Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments. , 1992, The Journal of biological chemistry.

[30]  E. Mandelkow,et al.  The switch of tau protein to an Alzheimer‐like state includes the phosphorylation of two serine‐proline motifs upstream of the microtubule binding region. , 1992, The EMBO journal.

[31]  G. Johnson,et al.  Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain. , 1992, The Journal of biological chemistry.

[32]  J. Trojanowski,et al.  A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. , 1991, Science.

[33]  Khadija Iqbal,et al.  Identification and localization of a tau peptide to paired helical filaments of Alzheimer disease. , 1989, Proceedings of the National Academy of Sciences of the United States of America.

[34]  H. Tung,et al.  Purification and characterization of protein phosphatase 1I activating kinase from bovine brain cytosolic and particulate fractions. , 1989, The Journal of biological chemistry.

[35]  T. Singh.  Polyamines stimulate the activity of glycogen synthase (casein) kinase-1 from bovine kidney and different rat tissues. , 1988, Archives of biochemistry and biophysics.

[36]  H. Wiśniewski,et al.  Microtubule-associated polypeptides tau are altered in Alzheimer paired helical filaments. , 1988, Brain research.

[37]  J. Baudier,et al.  Phosphorylation of tau proteins to a state like that in Alzheimer's brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids. , 1987, The Journal of biological chemistry.

[38]  J. Baudier,et al.  Separation of the different microtubule-associated tau protein species from bovine brain and their mode II phosphorylation by Ca2+/phospholipid-dependent protein kinase C. , 1987, The Journal of biological chemistry.

[39]  M. Kirschner,et al.  Tau protein function in living cells , 1986, The Journal of cell biology.

[40]  H. Wiśniewski,et al.  Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[41]  H. Wiśniewski,et al.  Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. , 1986, The Journal of biological chemistry.

[42]  J. Porath,et al.  Isolation of phosphoproteins by immobilized metal (Fe3+) affinity chromatography. , 1986, Analytical biochemistry.

[43]  H. Wiśniewski,et al.  Ultrastructure of Paired Helical Filaments of Alzheimer's Neurofibrillary Tangle , 1984, Journal of neuropathology and experimental neurology.

[44]  G. Lindwall,et al.  Phosphorylation affects the ability of tau protein to promote microtubule assembly. , 1984, The Journal of biological chemistry.

[45]  R. Sloboda,et al.  Decoration and stabilization of intact, smooth-walled microtubules with microtubule-associated proteins. , 1979, Biochemistry.

[46]  M. Kirschner,et al.  Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly. , 1977, Journal of molecular biology.

[47]  M. Kirschner,et al.  A protein factor essential for microtubule assembly. , 1975, Proceedings of the National Academy of Sciences of the United States of America.

[48]  C. Cantor,et al.  Microtubule assembly in the absence of added nucleotides. , 1973, Proceedings of the National Academy of Sciences of the United States of America.

[49]  D. Glick.  Methods of Biochemical Analysis , 1968 .

[50]  A. Bensadoun,et al.  Assay of proteins in the presence of interfering materials. , 1976, Analytical biochemistry.