Jennifer N. Rauch
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View article: Protocol for the removal of bound endotoxin from tau protein produced in Escherichia coli
Protocol for the removal of bound endotoxin from tau protein produced in Escherichia coli Open
View article: Extracellular tau clearance is governed by its aggregation state and independent of microglial activation by LPS and IFN-γ
Extracellular tau clearance is governed by its aggregation state and independent of microglial activation by LPS and IFN-γ Open
View article: Extracellular tau clearance is governed by its aggregation state and independent of microglial activation by LPS and IFN-γ
Extracellular tau clearance is governed by its aggregation state and independent of microglial activation by LPS and IFN-γ Open
Microglia are the tissue resident macrophages of the brain and their contribution to tau pathology progression remains to be fully understood. In this study, we developed a quantitative platform to elucidate the processing of extracellular…
View article: Uncovering Molecular Features that Contribute to Tau Spread and Aggregation
Uncovering Molecular Features that Contribute to Tau Spread and Aggregation Open
Background Tauopathies are a class of neurodegenerative diseases marked by tau protein spread and aggregation. Recently, our group described the cellular receptor Low‐density lipoprotein Receptor‐related Protein 1 (LRP1) as a regulator of …
View article: TTC17 is an endoplasmic reticulum resident TPR-containing adaptor protein
TTC17 is an endoplasmic reticulum resident TPR-containing adaptor protein Open
Protein folding, quality control, maturation, and trafficking are essential processes for proper cellular homeostasis. Around one-third of the human proteome is targeted to the endoplasmic reticulum (ER), the organelle that serves as entra…
View article: Data from Validation of the Hsp70–Bag3 Protein–Protein Interaction as a Potential Therapeutic Target in Cancer
Data from Validation of the Hsp70–Bag3 Protein–Protein Interaction as a Potential Therapeutic Target in Cancer Open
Hsp70 is a stress-inducible molecular chaperone that is required for cancer development at several steps. Targeting the active site of Hsp70 has proven relatively challenging, driving interest in alternative approaches. Hsp70 collaborates …
View article: Data from Validation of the Hsp70–Bag3 Protein–Protein Interaction as a Potential Therapeutic Target in Cancer
Data from Validation of the Hsp70–Bag3 Protein–Protein Interaction as a Potential Therapeutic Target in Cancer Open
Hsp70 is a stress-inducible molecular chaperone that is required for cancer development at several steps. Targeting the active site of Hsp70 has proven relatively challenging, driving interest in alternative approaches. Hsp70 collaborates …
View article: Supplemental Figures 1-4 from Validation of the Hsp70–Bag3 Protein–Protein Interaction as a Potential Therapeutic Target in Cancer
Supplemental Figures 1-4 from Validation of the Hsp70–Bag3 Protein–Protein Interaction as a Potential Therapeutic Target in Cancer Open
Supplemental Figures 1-4. Supplemental Figure 1. Chemical structures of the compounds used in this study and characterization of JG98-biotin by NMR and MS/MS; Supplemental Figure 2. JG-98 disrupts the Hsp70-Bag interaction in HeLa cells; S…
View article: Supplemental Figures 1-4 from Validation of the Hsp70–Bag3 Protein–Protein Interaction as a Potential Therapeutic Target in Cancer
Supplemental Figures 1-4 from Validation of the Hsp70–Bag3 Protein–Protein Interaction as a Potential Therapeutic Target in Cancer Open
Supplemental Figures 1-4. Supplemental Figure 1. Chemical structures of the compounds used in this study and characterization of JG98-biotin by NMR and MS/MS; Supplemental Figure 2. JG-98 disrupts the Hsp70-Bag interaction in HeLa cells; S…
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Description of additional methods and procedures used in the study.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Figure S2. Effect of Hsp70 or Bag3 depletion in HCT116 cells on signaling pathways.
View article: Data from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
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 mediating the effects of Hsp70 on Src signaling. Using sever…
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Legend for Supplemental Figures S1-S4.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Figure S3. Dose dependent effect of YM-1 signaling pathways.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Description of additional methods and procedures used in the study.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Table S1. Microarray data on effetcs of Hsp70 depletion in MCF7 cells.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Figure S3. Dose dependent effect of YM-1 signaling pathways.
View article: Data from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
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 mediating the effects of Hsp70 on Src signaling. Using sever…
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Table S1. Microarray data on effetcs of Hsp70 depletion in MCF7 cells.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Legend for Supplemental Figures S1-S4.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Figure S4. Treatment with YM-1 affects p21 and surviving in tumor xenografts.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Figure S1. Hsp70 depletion affects multiple pathways.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Figure S1. Hsp70 depletion affects multiple pathways.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Figure S2. Effect of Hsp70 or Bag3 depletion in HCT116 cells on signaling pathways.
View article: Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks
Data Supplement from Hsp70–Bag3 Interactions Regulate Cancer-Related Signaling Networks Open
Supplemental Figure S4. Treatment with YM-1 affects p21 and surviving in tumor xenografts.
View article: Mapping Phase Diagram of Tau-RNA LLPS Under Live Cell Coculturing Conditions
Mapping Phase Diagram of Tau-RNA LLPS Under Live Cell Coculturing Conditions Open
View article: Human tau mutations in cerebral organoids induce a progressive dyshomeostasis of cholesterol
Human tau mutations in cerebral organoids induce a progressive dyshomeostasis of cholesterol Open
View article: Stress routes clients to the proteasome via a BAG2 ubiquitin-independent degradation condensate
Stress routes clients to the proteasome via a BAG2 ubiquitin-independent degradation condensate Open
The formation of membraneless organelles can be a proteotoxic stress control mechanism that locally condenses a set of components capable of mediating protein degradation decisions. The breadth of mechanisms by which cells respond to stres…
View article: Comparison of Severe Acute Respiratory Syndrome Coronavirus 2 Screening Using Reverse Transcriptase–Quantitative Polymerase Chain Reaction or CRISPR-Based Assays in Asymptomatic College Students
Comparison of Severe Acute Respiratory Syndrome Coronavirus 2 Screening Using Reverse Transcriptase–Quantitative Polymerase Chain Reaction or CRISPR-Based Assays in Asymptomatic College Students Open
These findings reveal a shift in SARS-CoV-2 prevalence in a young and asymptomatic population and uncover the leading edge of a local outbreak that coincided with rising case counts in the surrounding county and the state of California. Th…
View article: Chemical validation of a druggable site on Hsp27/HSPB1 using in silico solvent mapping and biophysical methods
Chemical validation of a druggable site on Hsp27/HSPB1 using in silico solvent mapping and biophysical methods Open