Search Results - "Rauch, Jennifer N"
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Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro
Published in The Journal of biological chemistry (17-01-2014)“…Proteins with Bcl2-associated anthanogene (BAG) domains act as nucleotide exchange factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70)…”
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The proline-rich domain promotes Tau liquid-liquid phase separation in cells
Published in The Journal of cell biology (02-11-2020)“…Tau protein in vitro can undergo liquid-liquid phase separation (LLPS); however, observations of this phase transition in living cells are limited. To…”
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Tau Internalization is Regulated by 6-O Sulfation on Heparan Sulfate Proteoglycans (HSPGs)
Published in Scientific reports (23-04-2018)“…The misfolding and accumulation of tau protein into intracellular aggregates known as neurofibrillary tangles is a pathological hallmark of neurodegenerative…”
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Narrow equilibrium window for complex coacervation of tau and RNA under cellular conditions
Published in eLife (05-04-2019)“…The mechanism that leads to liquid-liquid phase separation (LLPS) of the tau protein, whose pathological aggregation is implicated in neurodegenerative…”
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Cofactors are essential constituents of stable and seeding-active tau fibrils
Published in Proceedings of the National Academy of Sciences - PNAS (26-12-2018)“…Amyloid fibrils are cross-β–rich aggregates that are exceptionally stable forms of protein assembly. Accumulation of tau amyloid fibrils is involved in many…”
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Stress routes clients to the proteasome via a BAG2 ubiquitin-independent degradation condensate
Published in Nature communications (02-06-2022)“…The formation of membraneless organelles can be a proteotoxic stress control mechanism that locally condenses a set of components capable of mediating protein…”
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Hsp70 protein complexes as drug targets
Published in Current pharmaceutical design (2013)“…Heat shock protein 70 (Hsp70) plays critical roles in proteostasis and is an emerging target for multiple diseases. However, competitive inhibition of the…”
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Validation of the Hsp70-Bag3 protein-protein interaction as a potential therapeutic target in cancer
Published in Molecular cancer therapeutics (01-03-2015)“…Hsp70 is a stress-inducible molecular chaperone that is required for cancer development at several steps. Targeting the active site of Hsp70 has proven…”
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Hsp70-Bag3 Interactions Regulate Cancer-Related Signaling Networks
Published in Cancer research (Chicago, Ill.) (01-09-2014)“…Bag3, a nucleotide exchange factor of the heat shock protein Hsp70, has been implicated in cell signaling. Here, we report that Bag3 interacts with the SH3…”
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Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor
Published in Nature communications (08-08-2019)“…Molecular chaperones such as Hsp40 and Hsp70 hold the androgen receptor (AR) in an inactive conformation. They are released in the presence of androgens,…”
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Myopathy associated BAG3 mutations lead to protein aggregation by stalling Hsp70 networks
Published in Nature communications (17-12-2018)“…BAG3 is a multi-domain hub that connects two classes of chaperones, small heat shock proteins (sHSPs) via two isoleucine-proline-valine (IPV) motifs and Hsp70…”
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Stabilizing the Hsp70-Tau Complex Promotes Turnover in Models of Tauopathy
Published in Cell chemical biology (18-08-2016)“…Heat shock protein 70 (Hsp70) is a chaperone that normally scans the proteome and initiates the turnover of some proteins (termed clients) by linking them to…”
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13
RNA stores tau reversibly in complex coacervates
Published in PLoS biology (06-07-2017)“…Nonmembrane-bound organelles that behave like liquid droplets are widespread among eukaryotic cells. Their dysregulation appears to be a critical step in…”
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High-throughput screen for inhibitors of protein–protein interactions in a reconstituted heat shock protein 70 (Hsp70) complex
Published in The Journal of biological chemistry (16-03-2018)“…Protein–protein interactions (PPIs) are an important category of putative drug targets. Improvements in high-throughput screening (HTS) have significantly…”
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Development of a Capillary Electrophoresis Platform for Identifying Inhibitors of Protein–Protein Interactions
Published in Analytical chemistry (Washington) (15-10-2013)“…Methods for identifying chemical inhibitors of protein–protein interactions (PPIs) are often prone to discovery of false positives, particularly those caused…”
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Author Correction: Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor
Published in Nature communications (07-10-2019)“…An amendment to this paper has been published and can be accessed via a link at the top of the paper…”
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A Scalable, Easy-to-Deploy Protocol for Cas13-Based Detection of SARS-CoV-2 Genetic Material
Published in Journal of clinical microbiology (19-03-2021)“…The COVID-19 pandemic has created massive demand for widespread, distributed tools for detecting SARS-CoV-2 genetic material. The hurdles to scalable testing…”
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BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins
Published in Journal of molecular biology (06-01-2017)“…Small heat shock proteins (sHsps) are a family of ATP-independent molecular chaperones that are important for binding and stabilizing unfolded proteins. In…”
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Mapping interactions with the chaperone network reveals factors that protect against tau aggregation
Published in Nature structural & molecular biology (01-05-2018)“…A network of molecular chaperones is known to bind proteins (‘clients’) and balance their folding, function and turnover. However, it is often unclear which…”
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Non-canonical Interactions between Heat Shock Cognate Protein 70 (Hsc70) and Bcl2-associated Anthanogene (BAG) Co-Chaperones Are Important for Client Release
Published in The Journal of biological chemistry (16-09-2016)“…Heat shock cognate protein 70 (Hsc70) regulates protein homeostasis through its reversible interactions with client proteins. Hsc70 has two major domains: a…”
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