(Q50513992)

14 March 2018

title

Multiple forms of phosphatase from human brain: isolation and partial characterization of affi-gel blue binding phosphatases. (English)

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14 March 2018

author name string

L Y Cheng

1

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14 March 2018

J Z Wang

2

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14 March 2018

C X Gong

3

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14 March 2018

J J Pei

4

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14 March 2018

T Zaidi

5

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14 March 2018

I Grundke-Iqbal

6

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14 March 2018

K Iqbal

7

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14 March 2018

publication date

1 January 2000

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14 March 2018

published in

Neurochemical Research

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14 March 2018

volume

25

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14 March 2018

page(s)

107-120

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14 March 2018

issue

1

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14 March 2018

https://scigraph.springernature.com/pub.10.1023/a:1007547701518

exact match

0 references

cites work

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.

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Dephosphorylation of Alzheimer's disease abnormally phosphorylated tau by protein phosphatase-2A.

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

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Microtubule Assembly in the Absence of Added Nucleotides

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The structure and regulation of protein phosphatases

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Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle

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Activation of brain calcineurin phosphatase towards nonprotein phosphoesters by Ca2+, calmodulin, and Mg2+

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Okadaic acid induces hyperphosphorylated forms of tau protein in human brain slices.

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The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases.

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Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B.

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

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Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules.

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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

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Dephosphorylation of tau protein and Alzheimer paired helical filaments by calcmeurin and phosphatase-2A

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12 December 2020

Subcellular distribution of protein phosphatases and abnormally phosphorylated tau in the temporal cortex from Alzheimer's disease and control brains.

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12 December 2020

20 Use of calmodulin affinity chromatography for purification of specific calmodulin-dependent enzymes

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12 December 2020

Protein serine/threonine phosphatases--new avenues for cell regulation

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Expression of protein phosphatases (PP-1, PP-2A, PP-2B and PTP-1B) and protein kinases (MAP kinase and P34cdc2) in the hippocampus of patients with Alzheimer disease and normal aged individuals.

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Monoclonal antibody PHF-1 recognizes tau protein phosphorylated at serine residues 396 and 404.

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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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Phosphoprotein phosphatase activities in Alzheimer disease brain

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Discovery of a Ca2+- and calmodulin-dependent protein phosphatase: probable identity with calcineurin (CaM-BP80)

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Alzheimer's disease abnormally phosphorylated tau is dephosphorylated by protein phosphatase-2B (calcineurin).

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Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

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Restoration of biological activity of Alzheimer abnormally phosphorylated tau by dephosphorylation with protein phosphatase-2A, -2B and -1.

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

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Protein phosphatases: recent progress

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Protein tyrosine phosphatases: mechanism of catalysis and substrate specificity

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Decoration and stabilization of intact, smooth-walled microtubules with microtubule-associated proteins

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Dephosphorylation of microtubule-associated protein tau by protein phosphatase-1 and -2C and its implication in Alzheimer disease.

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Calcineurin: a calcium- and calmodulin-binding protein of the nervous system

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Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Electron microscopic studies of free and proteinase-bound duck ovostatins (ovomacroglobulins). Model of ovostatin structure and its transformation upon proteolysis

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

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Reduction of calcineurin enzymatic activity in Alzheimer's disease: correlation with neuropathologic changes.

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12 December 2020

Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau

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12 December 2020

Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding.

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12 December 2020

Alzheimer paired helical filaments. Restoration of the biological activity by dephosphorylation.

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12 December 2020

Identifiers

DOI

10.1023/A:1007547701518

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14 March 2018

Dimensions Publication ID

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14 March 2018