Oxidized and phosphorylated synthetic peptides corresponding to the second and third tubulin‐binding repeats of the τ protein reveal structural features of paired helical filament assembly (Q48647557)

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scientific article published on August 1, 1997

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English	Oxidized and phosphorylated synthetic peptides corresponding to the second and third tubulin‐binding repeats of the τ protein reveal structural features of paired helical filament assembly	scientific article published on August 1, 1997

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5 November 2019

Oxidized and phosphorylated synthetic peptides corresponding to the second and third tubulin-binding repeats of the tau protein reveal structural features of paired helical filament assembly (English)

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5 November 2019

Oxidized and phosphorylated synthetic peptides corresponding to the second and third tubulin‐binding repeats of the τ protein reveal structural features of paired helical filament assembly (English)

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10.1111/J.1399-3011.1997.TB01178.X

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phosphorylation

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R. Hoffmann

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N. F. Dawson

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J. D. Wade

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L. Otvös

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publication date

1 August 1997

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5 November 2019

August 1997

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10.1111/J.1399-3011.1997.TB01178.X

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https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3011.1997.tb01178.x

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10.1111/J.1399-3011.1997.TB01178.X

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Chemical Biology and Drug Design

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5 November 2019

Alzheimer's disease: a cell biological perspective

1

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The disordered neuronal cytoskeleton in Alzheimer's disease

2

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Physiological production of the beta-amyloid protein and the mechanism of Alzheimer's disease

3

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Tau protein and the neurofibrillary pathology of Alzheimer's disease

4

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Clinical neuroscience (New York, N.Y.)

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1

184

author name string

Trojanowski J.Q.

publication date

1994

1 reference

10.1111/J.1399-3011.1997.TB01178.X

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Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau

6

1 reference

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Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: distinction between PHF-like immunoreactivity and microtubule binding.

7

1 reference

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The microtubule binding domain of tau protein.

9

1 reference

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Tau protein induces bundling of microtubules in vitro: comparison of different tau isoforms and a tau protein fragment

10

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Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau.

11

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Tau protein binds to microtubules through a flexible array of distributed weak sites

12

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Common and distinct tubulin binding sites for microtubule-associated proteins

13

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Detection of Phosphorylated Ser262 in Fetal Tau, Adult Tau, and Paired Helical Filament Tau

15

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Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloid-like fibrils in vitro

16

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Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly

17

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Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro

18

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Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau

20

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Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments

21

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Tau self-association: stabilization with a chemical cross-linker and modulation by phosphorylation and oxidation state

22

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Proline-directed and non-proline-directed phosphorylation of PHF-tau.

24

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Chemical phosphorylation of the peptides GGXA (X = S, T, Y): an evaluation of different chemical approaches

26

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A mild method for the preparation of disulfide-linked hybrids of immunoglobulin light chains

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Peptide stability in drug development. II. Effect of single amino acid substitution and glycosylation on peptide reactivity in human serum

29

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Aspartate-bond isomerization affects the major conformations of synthetic peptides

30

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Conformations of (X-L-Pro-Y)2 cyclic hexapeptides. Preferred .beta.-turn conformers and implications for .beta. turns in proteins

31

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Phosphorylation loops in synthetic peptides of the human neurofilament protein middle-sized subunit

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Glycosylation of synthetic peptides breaks helices. Phosphorylation results in distorted structure

33

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The effects of aspartic acid-bond isomerization on in vitro properties of the amyloid beta-peptide as modeled with N-terminal decapeptide fragments

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Analysis of the conserved glycosylation site in the nicotinic acetylcholine receptor: potential roles in complex assembly

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Recognition of the minimal epitope of monoclonal antibody Tau‐1 depends upon the presence of a phosphate group but not its location

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Immunological and conformation characterization of a phosphorylated immunodominant epitope on the paired helical filaments found in Alzheimer's disease

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Reversible β-pleated sheet formation of a phosphorylated synthetic τ peptide

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In vitro polymerization of oxidized tau into filaments

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A discrete repeated sequence defines a tubulin binding domain on microtubule-associated protein tau.

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The effects of post-translational side-chain modifications on the stimulatory activity, serum stability and conformation of synthetic peptides carrying T helper cell epitopes

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Calpain‐Induced Proteolysis of Normal Human Tau and Tau Associated with Paired Helical Filaments

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Specific processing of native and phosphorylated tau protein by proteases

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Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease

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Identifiers

10.1111/J.1399-3011.1997.TB01178.X

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9273897%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9273897%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

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