Search Results - "Murray, Amber N."

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  1. 1

    Impaired Thermosensation in Mice Lacking TRPV3, a Heat and Camphor Sensor in the Skin by Moqrich, Aziz, Hwang, Sun Wook, Earley, Taryn J., Petrus, Matt J., Murray, Amber N., Kathryn S. R. Spencer, Andahazy, Mary, Story, Gina M., Patapoutian, Ardem

    “…Environmental temperature is thought to be directly sensed by neurons through their projections in the skin. A subset of the mammalian transient receptor…”
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    Journal Article
  2. 2

    Hsp104 Gives Clients the Individual Attention They Need by Murray, Amber N., Kelly, Jeffery W.

    Published in Cell (09-11-2012)
    “…Yeast heat shock protein 104 (Hsp104), the only known eukaryotic disaggregase, remodels both disordered protein aggregates and cross-β sheet amyloids. To…”
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    Journal Article
  3. 3

    TRPM8 Is Required for Cold Sensation in Mice by Dhaka, Ajay, Murray, Amber N., Mathur, Jayanti, Earley, Taryn J., Petrus, Matt J., Patapoutian, Ardem

    Published in Neuron (Cambridge, Mass.) (03-05-2007)
    “…ThermoTRPs, a subset of the Transient Receptor Potential (TRP) family of cation channels, have been implicated in sensing temperature. TRPM8 and TRPA1 are both…”
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    Journal Article
  4. 4

    Surface adsorption considerations when working with amyloid fibrils in multiwell plates and Eppendorf tubes by Murray, Amber N., Palhano, Fernando L., Bieschke, Jan, Kelly, Jeffery W.

    Published in Protein science (01-11-2013)
    “…The accumulation of cross‐β‐sheet amyloid fibrils is the hallmark of amyloid diseases. Recently, we reported the discovery of amyloid disaggregase activities…”
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    Journal Article
  5. 5

    A Kinetic Aggregation Assay Allowing Selective and Sensitive Amyloid-β Quantification in Cells and Tissues by Du, Deguo, Murray, Amber N, Cohen, Ehud, Kim, Hyun-Eui, Simkovsky, Ryan, Dillin, Andrew, Kelly, Jeffery W

    Published in Biochemistry (Easton) (15-03-2011)
    “…The process of amyloid-β (Aβ) fibril formation is genetically and pathologically linked to Alzheimer’s disease (AD). Thus, a selective and sensitive method for…”
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    Journal Article
  6. 6

    N-glycosylation of enhanced aromatic sequons to increase glycoprotein stability by Price, Joshua L., Culyba, Elizabeth K., Chen, Wentao, Murray, Amber N., Hanson, Sarah R., Wong, Chi-Huey, Powers, Evan T., Kelly, Jeffery W.

    Published in Biopolymers (2012)
    “…N‐glycosylation can increase the rate of protein folding, enhance thermodynamic stability, and slow protein unfolding; however, the molecular basis for these…”
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    Journal Article
  7. 7

    Enhanced Aromatic Sequons Increase Oligosaccharyltransferase Glycosylation Efficiency and Glycan Homogeneity by Murray, Amber N., Chen, Wentao, Antonopoulos, Aristotelis, Hanson, Sarah R., Wiseman, R. Luke, Dell, Anne, Haslam, Stuart M., Powers, David L., Powers, Evan T., Kelly, Jeffery W.

    Published in Chemistry & biology (20-08-2015)
    “…N-Glycosylation plays an important role in protein folding and function. Previous studies demonstrate that a phenylalanine residue introduced at the n-2…”
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    Journal Article
  8. 8

    Discovery and characterization of a mammalian amyloid disaggregation activity by Murray, Amber N., Solomon, James P., Wang, Ya‐Juan, Balch, William E., Kelly, Jeffery W.

    Published in Protein science (01-04-2010)
    “…The formation of amyloid, a cross‐β‐sheet fibrillar aggregate, is associated with a variety of aging‐associated degenerative diseases. Herein, we report the…”
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    Journal Article
  9. 9

    The 8 and 5 kDa Fragments of Plasma Gelsolin Form Amyloid Fibrils by a Nucleated Polymerization Mechanism, while the 68 kDa Fragment Is Not Amyloidogenic by Solomon, James P, Yonemoto, Isaac T, Murray, Amber N, Price, Joshua L, Powers, Evan T, Balch, William E, Kelly, Jeffery W

    Published in Biochemistry (Easton) (08-12-2009)
    “…Familial amyloidosis of Finnish type (FAF), or gelsolin amyloidosis, is a systemic amyloid disease caused by a mutation (D187N/Y) in domain 2 of human plasma…”
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    Journal Article
  10. 10

    Abstract 3110: In depth comparison of cell free DNA blood collection tubes by Desharnais, Joel, Vasquez, Jacob M., Reshatoff, Katya J., Bui, Quyen, Chen, Han-Mei, Tsvetanova, Billyana, Lu, Jerry, Murray, Amber N., Costa, Gina L.

    Published in Cancer research (Chicago, Ill.) (15-08-2020)
    “…Abstract Liquid biopsy continues to gain traction as a minimally invasive method to monitor biomarkers associated with malignancy and metastasis such as…”
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    Journal Article
  11. 11

    Abstract 4598: A comprehensive assessment of the impact of preanalytical variables on cell free DNA and circulating tumor cells in blood by Pottekat, Anita, Allawi, Hatim T., Boragine, Genna T., Kaiser, Michael W., Sander, Tamara, Krueger, Chateen, Bruinsma, Janelle J., Murray, Amber N.

    Published in Cancer research (Chicago, Ill.) (01-07-2018)
    “…Abstract Liquid biopsy continues to gain traction as a minimally invasive method to monitor biomarkers associated with malignancy and metastasis. A simple…”
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    Journal Article
  12. 12

    A Kinetic Aggregation Assay Enabling Selective and Sensitive Aβ Amyloid Quantification in Cells and Tissues by Du, Deguo, Murray, Amber N., Cohen, Ehud, Kim, Hyun-Eui, Simkovsky, Ryan, Dillin, Andrew, Kelly, Jeffery W.

    Published in Biochemistry (Easton) (26-01-2011)
    “…The process of amyloid-β (Aβ) fibril formation is genetically and pathologically linked to Alzheimer's disease (AD). Thus, a selective and sensitive method for…”
    Get full text
    Journal Article
  13. 13

    Promoting Protein Folding with N-glycosylation and Amyloid Disaggregation by Murray, Amber N

    Published 01-01-2012
    “…Proteins must fold into complex three-dimensional structures to function. Considerable cellular resources are spent to facilitate protein folding. Enzymes…”
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    Dissertation
  14. 14

    Promoting Protein Folding with N-glycosylation and Amyloid Disaggregation by Murray, Amber N

    “…Proteins must fold into complex three-dimensional structures to function. Considerable cellular resources are spent to facilitate protein folding. Enzymes…”
    Get full text
    Dissertation