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Amyloid accelerator polyphosphate fits as the mystery density in α-synuclein fibrils.
- Published in:
- PLoS Biology, 2024, v. 22, n. 10, p. 1, doi. 10.1371/journal.pbio.3002650
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- Article
A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis.
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- eLife, 2015, p. 1, doi. 10.7554/eLife.07304
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- Article
Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase.
- Published in:
- Nature Communications, 2019, v. 10, n. 1, p. N.PAG, doi. 10.1038/s41467-019-10150-y
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- Article
Chaperone activation and client binding of a 2-cysteine peroxiredoxin.
- Published in:
- Nature Communications, 2019, v. 10, n. 1, p. 1, doi. 10.1038/s41467-019-08565-8
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- Article
Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau.
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- Nature Communications, 2018, v. 9, n. 1, p. 1, doi. 10.1038/s41467-018-07012-4
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- Article
Cryo-EM structures reveal tau filaments from Down syndrome adopt Alzheimer's disease fold.
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- Acta Neuropathologica Communications, 2024, v. 12, n. 1, p. 1, doi. 10.1186/s40478-024-01806-y
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- Article
Aggregation of Mod5 is affected by tRNA binding with implications for tRNA gene-mediated silencing.
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- FEBS Letters, 2017, v. 591, n. 11, p. 1601, doi. 10.1002/1873-3468.12627
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- Article
Single-particle cryo-electron microscopy of macromolecular complexes.
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- Microscopy, 2016, v. 65, n. 1, p. 9, doi. 10.1093/jmicro/dfv366
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- Article
Phosphorylation of tau at a single residue inhibits binding to the E3 ubiquitin ligase, CHIP.
- Published in:
- Nature Communications, 2024, v. 15, n. 1, p. 1, doi. 10.1038/s41467-024-52075-1
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- Article
The conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis.
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- Protein Science: A Publication of the Protein Society, 2012, v. 21, n. 8, p. 1162, doi. 10.1002/pro.2103
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- Article
Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide.
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- Protein Science: A Publication of the Protein Society, 2009, v. 18, n. 9, p. 1815, doi. 10.1002/pro.191
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- Article