Taylor Arhar
A5054708268- Heat shock proteins research
- Endoplasmic Reticulum Stress and Disease
- Protein Structure and Dynamics
- Protein Degradation and Inhibitors
- Fungal and yeast genetics research
- Parkinson's Disease Mechanisms and Treatments
- Toxin Mechanisms and Immunotoxins
- Ubiquitin and proteasome pathways
- Bioinformatics and Genomic Networks
- Neuroinflammation and Neurodegeneration Mechanisms
- Alzheimer's disease research and treatments
- Prion Diseases and Protein Misfolding
- Advanced Proteomics Techniques and Applications
- Nerve injury and regeneration
- vaccines and immunoinformatics approaches
- Trace Elements in Health
- Enzyme Structure and Function
- Neuroscience and Neuropharmacology Research
University of California, San Francisco
2018-2022
Beloit College
2021-2022
Institute for Neurodegenerative Disorders
2021-2022
Chaperones of the heat shock protein 70 (Hsp70) family engage in protein-protein interactions with many cochaperones. One "hotspot" for cochaperone binding is EEVD motif, found at extreme C terminus cytoplasmic Hsp70s. This motif known to bind tetratricopeptide repeat domain cochaperones, such as E3 ubiquitin ligase CHIP. In addition, also interacts a structurally distinct that present class B J-domain proteins, DnaJB4. These observations suggest CHIP and DnaJB4 might compete Hsp70's motif;...
ABSTRACT Although the primary protein sequence of ubiquitin (Ub) is extremely stable over evolutionary time, it highly tolerant to mutation during selection experiments performed in laboratory. We have proposed that this discrepancy results from difference between fitness under laboratory culture conditions and selective pressures changing environments timescales. Building on our previous work (Mavor et al., 2016), we used deep mutational scanning determine how twelve new chemicals...
Protein conformations are shaped by cellular environments, but how environmental changes alter the conformational landscapes of specific proteins in vivo remains largely uncharacterized, part due to challenge probing protein structures living cells. Here, we use deep mutational scanning investigate a toxic conformation α-synuclein, dynamic linked Parkinson's disease, responds perturbations proteostasis. In context course for graduate students UCSF Integrative Program Quantitative Biology,...
Abstract Chaperones of the heat shock protein 70 (Hsp70) family engage in protein-protein interactions (PPIs) with many co-chaperones. One hotspot for co-chaperone binding is EEVD motif that found at extreme C-terminus cytoplasmic Hsp70s. This known to bind tetratricopeptide repeat (TPR) domain co-chaperones, such as E3 ubiquitin ligase CHIP, and Class B J-domain proteins (JDPs), DnaJB4. Although complexes between Hsp70-CHIP Hsp70-DnaJB4 are both important chaperone functions, molecular...
Abstract Although the primary protein sequence of ubiquitin (Ub) is extremely stable over evolutionary time, it highly tolerant to mutation during selection experiments performed in laboratory. We have proposed that this discrepancy results from difference between fitness under laboratory culture conditions and selective pressures changing environments time scales. Building on our previous work (Mavor et al 2016), we used deep mutational scanning determine how twelve new chemicals...
ABSTRACT Protein conformations are shaped by cellular environments, but how environmental changes alter the conformational landscapes of specific proteins in vivo remains largely uncharacterized, part due to challenge probing protein structures living cells. Here, we use deep mutational scanning investigate a toxic conformation α-synuclein, dynamic linked Parkinson’s disease, responds perturbations proteostasis. In context course for graduate students UCSF Integrative Program Quantitative...