Comparison of the phosphorylation of microtubule-associated protein tau by non-proline dependent protein kinases. (Q48172695)

9 February 2018

title

Comparison of the phosphorylation of microtubule-associated protein tau by non-proline dependent protein kinases. (English)

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9 February 2018

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T J Singh

1

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9 February 2018

I Grundke-Iqbal

series ordinal

2

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9 February 2018

B McDonald

series ordinal

3

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9 February 2018

K Iqbal

series ordinal

4

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9 February 2018

publication date

1 February 1994

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9 February 2018

Molecular and Cellular Biochemistry

published in

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9 February 2018

volume

131

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9 February 2018

issue

2

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9 February 2018

page(s)

181-189

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9 February 2018

https://scigraph.springernature.com/pub.10.1007/bf00925955

exact match

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cites work

Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain.

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Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis

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Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

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Phosphorylation of microtubule-associated protein tau: identification of the site for Ca2(+)-calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles.

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A protein kinase associated with paired helical filaments in Alzheimer disease

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Inhibition of glycogen synthase (casein) kinase-1 by heparin

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Multisite phosphorylation of tau proteins from rat brain.

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12 December 2020

Glycogen synthase kinase-3 and the Alzheimer-like state of microtubule-associated protein tau.

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Proline-directed phosphorylation of human Tau protein.

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Two novel kinases phosphorylate tau and the KSP site of heavy neurofilament subunits in high stoichiometric ratios

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Tau in Alzheimer neurofibrillary tangles. N- and C-terminal regions are differentially associated with paired helical filaments and the location of a putative abnormal phosphorylation site

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Phosphate analysis and dephosphorylation of modified tau associated with paired helical filaments

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Protein sequence and mass spectrometric analyses of tau in the Alzheimer's disease brain

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Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology

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Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer-like state

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Separation of the different microtubule-associated tau protein species from bovine brain and their mode II phosphorylation by Ca2+/phospholipid-dependent protein kinase C.

1 reference

12 December 2020

The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region

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12 December 2020

The Alzheimer-like phosphorylation of tau protein reduces microtubule binding and involves Ser-Pro and Thr-Pro motifs

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Identification and localization of a tau peptide to paired helical filaments of Alzheimer disease

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The distribution of tau in the mammalian central nervous system

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Phosphorylation-dependent epitopes of neurofilament antibodies on tau protein and relationship with Alzheimer tau

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Autophosphorylation of rat brain Ca2+-activated and phospholipid-dependent protein kinase.

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The subunit structure of rabbit-skeletal-muscle phosphorylase kinase, and the molecular basis of its activation reactions

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Phosphorylation of recombinant tau by cAMP-dependent protein kinase. Identification of phosphorylation sites and effect on microtubule assembly.

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A68: a major subunit of paired helical filaments and derivatized forms of normal Tau.

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Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments

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Ca2+/calmodulin-dependent protein kinase enriched in cerebellar granule cells. Identification of a novel neuronal calmodulin-dependent protein kinase

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Glycogen synthase (casein) kinase-1: tissue distribution and subcellular localization.

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Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain

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12 December 2020

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.

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Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

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A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis

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Structure of the bovine tau gene: alternatively spliced transcripts generate a protein family

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Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments

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Brain protein kinase PK40erk converts TAU into a PHF-like form as found in Alzheimer's disease.

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Polyamines stimulate the activity of glycogen synthase (casein) kinase-1 from bovine kidney and different rat tissues.

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Tau protein kinase II is involved in the regulation of the normal phosphorylation state of tau protein.

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12 December 2020

Identifiers

DOI

10.1007/BF00925955

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9 February 2018

PubMed ID

8035784

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9 February 2018