Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.

The Journal of neuroscience : the official journal of the Society for Neuroscience - 13 Jan 2010

Jinwal Umesh K, Koren John, Borysov Sergiy I, Schmid Andreas B, Abisambra Jose F, Blair Laura J, Johnson Amelia G, Jones Jeffrey R, Shults Cody L, O'Leary John C, Jin Ying, Buchner Johannes, Cox Marc B, Dickey Chad A

Abstract excerpt

Imbalanced protein load within cells is a critical aspect for most diseases of aging. In particular, the accumulation of proteins into neurotoxic aggregates is a common thread for a host of neurodegenerative diseases. Our previous work demonstrated that age-related changes to the cellular chaperone repertoire contributes to abnormal buildup of the microtubule-associated protein tau that accumulates in a group of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Benzoquinones
Share to Chymotrypsin

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to HSP90 Heat-Shock Proteins

Share to Lactams, Macrocyclic

Share to Microtubules

Share to Peptidylprolyl Isomerase

Share to Tacrolimus Binding Proteins

Share to Xenopus

Source

Open in PubMed Open full text

Identifiers

PMID: 20071522
DOI: 10.1523/JNEUROSCI.4815-09.2010
PMCID: PMC2830818

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules.PMID 20071522Read ↗

Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90.Semantic proximity Read ↗

The Crystal Structure of the Hsp90-LA1011 Complex and the Mechanism by which LA1011 may Improve the Prognosis of Alzheimer’s DiseaseSemantic proximity Read ↗

Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies.Semantic proximity Read ↗

Saccharomyces cerevisiae Fpr1 functions as a chaperone to inhibit protein aggregation.Semantic proximity Read ↗

Peptidyl-prolyl isomerase activity of FK506 binding protein 12 prevents tau peptide from aggregating.Semantic proximity Read ↗

FKBP51-Hsp90 Interaction-Deficient Mice Exhibit Altered Endocrine Stress Response and Sex Differences Under High-Fat DietSemantic proximity Read ↗

The 90-kDa heat-shock protein (Hsp90)-binding immunophilin FKBP51 is a mitochondrial protein that translocates to the nucleus to protect cells against oxidative stress.Semantic proximity Read ↗

Bidirectional interplay of HSF1 degradation and UPR activation promotes tau hyperphosphorylationSemantic proximity Read ↗

MOLECULAR BASIS FOR PINK1 MATURATIONSemantic proximity Read ↗

UBA52 is crucial in HSP90 ubiquitylation and neurodegenerative signaling during early phase of Parkinson’s diseaseSemantic proximity Read ↗

Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic InterventionSemantic proximity Read ↗

Control of Alzheimer's amyloid beta toxicity by the high molecular weight immunophilin FKBP52 and copper homeostasis in Drosophila.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.