User profiles for Jennifer N. Rauch
Jennifer RauchAssistant Professor, University of Massachusetts Amherst Verified email at umass.edu Cited by 3117 |
LRP1 is a master regulator of tau uptake and spread
The spread of protein aggregates during disease progression is a common theme underlying
many neurodegenerative diseases. The microtubule-associated protein tau has a central …
many neurodegenerative diseases. The microtubule-associated protein tau has a central …
[HTML][HTML] RNA stores tau reversibly in complex coacervates
Nonmembrane-bound organelles that behave like liquid droplets are widespread among
eukaryotic cells. Their dysregulation appears to be a critical step in several neurodegenerative …
eukaryotic cells. Their dysregulation appears to be a critical step in several neurodegenerative …
[PDF][PDF] Defining Hsp70 subnetworks in dengue virus replication reveals key vulnerability in flavivirus infection
Viral protein homeostasis depends entirely on the machinery of the infected cell. Accordingly,
viruses can illuminate the interplay between cellular proteostasis components and their …
viruses can illuminate the interplay between cellular proteostasis components and their …
A scalable, easy-to-deploy protocol for Cas13-based detection of SARS-CoV-2 genetic material
The COVID-19 pandemic has created massive demand for widespread, distributed tools for
detecting SARS-CoV-2 genetic material. The hurdles to scalable testing include reagent and …
detecting SARS-CoV-2 genetic material. The hurdles to scalable testing include reagent and …
[HTML][HTML] Tau internalization is regulated by 6-O sulfation on heparan sulfate proteoglycans (HSPGs)
The misfolding and accumulation of tau protein into intracellular aggregates known as
neurofibrillary tangles is a pathological hallmark of neurodegenerative diseases such as …
neurofibrillary tangles is a pathological hallmark of neurodegenerative diseases such as …
[HTML][HTML] Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro
JN Rauch, JE Gestwicki - Journal of Biological Chemistry, 2014 - ASBMB
Proteins with Bcl2-associated anthanogene (BAG) domains act as nucleotide exchange
factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70). There are six BAG …
factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70). There are six BAG …
Hsp70–Bag3 interactions regulate cancer-related signaling networks
…, M Garcia-Marcos, X Li, ZT Young, JN Rauch… - Cancer research, 2014 - AACR
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 domain of Src, thereby …
cell signaling. Here, we report that Bag3 interacts with the SH3 domain of Src, thereby …
BAG3 is a modular, scaffolding protein that physically links heat shock protein 70 (Hsp70) to the small heat shock proteins
Small heat shock proteins (sHsps) are a family of ATP-independent molecular chaperones
that are important for binding and stabilizing unfolded proteins. In this task, the sHsps have …
that are important for binding and stabilizing unfolded proteins. In this task, the sHsps have …
Mapping interactions with the chaperone network reveals factors that protect against tau aggregation
A network of molecular chaperones is known to bind proteins (‘clients’) and balance their
folding, function and turnover. However, it is often unclear which chaperones are critical for …
folding, function and turnover. However, it is often unclear which chaperones are critical for …
Narrow equilibrium window for complex coacervation of tau and RNA under cellular conditions
10.7554/eLife.42571.001 The mechanism that leads to liquid-liquid phase separation (LLPS)
of the tau protein, whose pathological aggregation is implicated in neurodegenerative …
of the tau protein, whose pathological aggregation is implicated in neurodegenerative …