The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
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In the citing paper
“In solution, however, Tau is intrinsically disordered, highly soluble, and binds to microtubules.”
From Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau (2017) · cites this paper as [17]
In the citing paper
“In agreement with the intrinsically disordered nature of Tau17, CD spectra of K18, recorded at 5 °C, were characteristic for random coil behavior (Fig. 4a).”
From Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau (2017) · cites this paper as [17]
Citations
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“…from microtubule protein by a combination of phosphocellulose chromatography, ammonium sulfate precipitation, and hydroxyapatite chromatography (Cleveland et al., 1977b), is seen by SDS/polyacrylamide gel electrophoresis to consist of four closely spaced bands of apparent molecular weights…”
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Cited by
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Self-citationPhosphorylation affects the ability of tau protein to promote microtubule assembly.
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“Since the discovery of phosphorylation and the first description of isoforms of Tau (Cleveland et al., 1977), the roles of Tau proteoforms (different chemical versions of a polypeptide) have been explored functionally (Adams et al.”
BackgroundStructural Polymorphism of 441-Residue Tau at Single Residue Resolution
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Tau stabilizes microtubules by binding at the interface between tubulin heterodimers
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The role of tau in Alzheimer's disease
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Tau can switch microtubule network organizations: from random networks to dynamic and stable bundles
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“Tau is a major neuronal MAP involved in the regulation of microtubule bundling and dynamics (Weingarten et al., 1975; Cleveland et al., 1977a,b; Binder et al., 1985; Chen et al., 1992; Drechsel et al., 1992; Brandt and Lee, 1993b; Trinczek et al., 1995).”
BackgroundTranscriptional and conformational changes of the tau molecule in Alzheimer's disease
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Folding of the Repeat Domain of Tau Upon Binding to Lipid Surfaces
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Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63
“In 1975, neuropathologists Kirschner MW et al. discovered a new protein in the brain tissue of patients with neurodegenerative diseases such as Alzheimer’s disease (AD) and Pick’s disease [1,2].”
BackgroundDevelopments in Tau PET Imaging
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Mechanisms of trafficking in axons and dendrites: implications for development and neurodegeneration
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Neuronal and Glial Distribution of Tau Protein in the Adult Rat and Monkey
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Pawlowski, M., Meuth, S., & Duning, T. (2017) · Diagnostics · doi:10.3390/diagnostics7030042 · Cited by 25
Analysis of Human Tau in Cerebrospinal Fluid
Hanisch, K., Soininen, H., Alafuzoff, I., & Hoffmann, R. (2010) · Journal of Proteome Research · doi:10.1021/pr901002t · Cited by 17
Yesiltepe, M., Yin, T., Tambini, M., Bao, H., Pan, M., d’Abramo, C., Giliberto, L., Han, X., & D’Adamio, L. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01832-2 · Cited by 10
“Tau’s function and stability are modulated by phosphorylation at multiple sites [60, 61].”
Background
Metadata
- Authors
- Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1977-10
- Volume
- 116
- Issue
- 2
- Pages
- 227-247
- ISSN
- 0022-2836
- Cited by
- 730
- References
- 2
- Language
- en
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