Search Results - "Freed, Jack H."

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  1. 1

    A New Wavelet Denoising Method for Selecting Decomposition Levels and Noise Thresholds by Srivastava, Madhur, Anderson, C. Lindsay, Freed, Jack H.

    Published in IEEE access (2016)
    “…A new method is presented to denoise 1-D experimental signals using wavelet transforms. Although the state-of-the-art wavelet denoising methods perform better…”
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  2. 2

    Cofactors are essential constituents of stable and seeding-active tau fibrils by Fichou, Yann, Lin, Yanxian, Rauch, Jennifer N., Vigers, Michael, Zeng, Zhikai, Srivastava, Madhur, Keller, Timothy J., Freed, Jack H., Kosik, Kenneth S., Han, Songi

    “…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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  3. 3

    Structural basis for membrane anchoring and fusion regulation of the herpes simplex virus fusogen gB by Cooper, Rebecca S., Georgieva, Elka R., Borbat, Peter P., Freed, Jack H., Heldwein, Ekaterina E.

    Published in Nature structural & molecular biology (01-05-2018)
    “…Viral fusogens merge viral and cell membranes during cell penetration. Their ectodomains drive fusion by undergoing large-scale refolding, but little is known…”
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  4. 4

    Tau Binds to Lipid Membrane Surfaces via Short Amphipathic Helices Located in Its Microtubule-Binding Repeats by Georgieva, Elka R., Xiao, Shifeng, Borbat, Peter P., Freed, Jack H., Eliezer, David

    Published in Biophysical journal (16-09-2014)
    “…Tau is a microtubule-associated protein that is genetically linked to dementia and linked to Alzheimer’s disease via its presence in intraneuronal…”
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  5. 5

    HIV gp41 Fusion Peptide Increases Membrane Ordering in a Cholesterol-Dependent Fashion by Lai, Alex L., Freed, Jack H.

    Published in Biophysical journal (07-01-2014)
    “…Fusion between viral envelopes and host cell membranes, which is mediated by special glycoproteins anchored on the viral membrane, is required for HIV viral…”
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  6. 6

    The Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane Structure by Lai, Alex L., Freed, Jack H.

    Published in Biophysical journal (15-12-2015)
    “…Viral glycoproteins, such as influenza hemagglutinin (HA) and human immunodeficiency virus gp41, are anchored by a single helical segment transmembrane domain…”
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  7. 7

    Conformational ensemble of the sodium-coupled aspartate transporter by Georgieva, Elka R, Borbat, Peter P, Ginter, Christopher, Freed, Jack H, Boudker, Olga

    Published in Nature structural & molecular biology (01-02-2013)
    “…The sodium and aspartate symporter Glt Ph mediates transport by alternating between outward-facing and inward-facing states. These conformational changes are…”
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  8. 8

    Transport domain unlocking sets the uptake rate of an aspartate transporter by Akyuz, Nurunisa, Georgieva, Elka R., Zhou, Zhou, Stolzenberg, Sebastian, Cuendet, Michel A., Khelashvili, George, Altman, Roger B., Terry, Daniel S., Freed, Jack H., Weinstein, Harel, Boudker, Olga, Blanchard, Scott C.

    Published in Nature (London) (05-02-2015)
    “…Glutamate transporters terminate neurotransmission by clearing synaptically released glutamate from the extracellular space, allowing repeated rounds of…”
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  9. 9

    Optimal Wavelet Selection for Signal Denoising by Sahoo, Gyana Ranjan, Freed, Jack H., Srivastava, Madhur

    Published in IEEE access (2024)
    “…Wavelet denoising plays a key role in removing noise from signals and is widely used in many applications. In denoising, selection of the mother wavelet is…”
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  10. 10

    Structural insights into perilipin 3 membrane association in response to diacylglycerol accumulation by Choi, Yong Mi, Ajjaji, Dalila, Fleming, Kaelin D., Borbat, Peter P., Jenkins, Meredith L., Moeller, Brandon E., Fernando, Shaveen, Bhatia, Surita R., Freed, Jack H., Burke, John E., Thiam, Abdou Rachid, Airola, Michael V.

    Published in Nature communications (02-06-2023)
    “…Lipid droplets (LDs) are dynamic organelles that contain an oil core mainly composed of triglycerides (TAG) that is surrounded by a phospholipid monolayer and…”
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  11. 11

    Signal transduction in light–oxygen–voltage receptors lacking the adduct-forming cysteine residue by Yee, Estella F., Diensthuber, Ralph P., Vaidya, Anand T., Borbat, Peter P., Engelhard, Christopher, Freed, Jack H., Bittl, Robert, Möglich, Andreas, Crane, Brian R.

    Published in Nature communications (09-12-2015)
    “…Light–oxygen–voltage (LOV) receptors sense blue light through the photochemical generation of a covalent adduct between a flavin-nucleotide chromophore and a…”
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  12. 12

    Signature of an aggregation-prone conformation of tau by Eschmann, Neil A., Georgieva, Elka R., Ganguly, Pritam, Borbat, Peter P., Rappaport, Maxime D., Akdogan, Yasar, Freed, Jack H., Shea, Joan-Emma, Han, Songi

    Published in Scientific reports (17-03-2017)
    “…The self-assembly of the microtubule associated tau protein into fibrillar cell inclusions is linked to a number of devastating neurodegenerative disorders…”
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  13. 13

    Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance by Lai, Alex L., Clerico, Eugenia M., Blackburn, Mandy E., Patel, Nisha A., Robinson, Carol V., Borbat, Peter P., Freed, Jack H., Gierasch, Lila M.

    Published in The Journal of biological chemistry (26-05-2017)
    “…Proteins are dynamic entities that populate conformational ensembles, and most functions of proteins depend on their dynamic character. Allostery, in…”
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  14. 14

    Mechanism of influenza A M2 transmembrane domain assembly in lipid membranes by Georgieva, Elka R., Borbat, Peter P., Norman, Haley D., Freed, Jack H.

    Published in Scientific reports (20-07-2015)
    “…M2 from influenza A virus functions as an oligomeric proton channel essential for the viral cycle, hence it is a high-priority pharmacological target whose…”
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    Organometallic and radical intermediates reveal mechanism of diphthamide biosynthesis by Dong, Min, Kathiresan, Venkatesan, Fenwick, Michael K, Torelli, Andrew T, Zhang, Yang, Caranto, Jonathan D, Dzikovski, Boris, Sharma, Ajay, Lancaster, Kyle M, Freed, Jack H, Ealick, Steven E, Hoffman, Brian M, Lin, Hening

    “…Diphthamide biosynthesis involves a carbon-carbon bond-forming reaction catalyzed by a radical S-adenosylmethionine (SAM) enzyme that cleaves a carbon-sulfur…”
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  17. 17

    Structural basis for activation, assembly and membrane binding of ESCRT-III Snf7 filaments by Tang, Shaogeng, Henne, W Mike, Borbat, Peter P, Buchkovich, Nicholas J, Freed, Jack H, Mao, Yuxin, Fromme, J Christopher, Emr, Scott D

    Published in eLife (15-12-2015)
    “…The endosomal sorting complexes required for transport (ESCRTs) constitute hetero-oligomeric machines that catalyze multiple topologically similar…”
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  18. 18

    Bacterial chemoreceptor dynamics correlate with activity state and are coupled over long distances by Samanta, Dipanjan, Borbat, Peter P., Dzikovski, Boris, Freed, Jack H., Crane, Brian R.

    “…Significance Bacterial chemoreceptors are a key system for understanding how conformational signals propagate over large distances in transmembrane signaling…”
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  19. 19

    Bacterial Energy Sensor Aer Modulates the Activity of the Chemotaxis Kinase CheA Based on the Redox State of the Flavin Cofactor by Samanta, Dipanjan, Widom, Joanne, Borbat, Peter P., Freed, Jack H., Crane, Brian R.

    Published in The Journal of biological chemistry (09-12-2016)
    “…Flagellated bacteria modulate their swimming behavior in response to environmental cues through the CheA/CheY signaling pathway. In addition to responding to…”
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  20. 20

    Copper-Based Pulsed Dipolar ESR Spectroscopy as a Probe of Protein Conformation Linked to Disease States by Merz, Gregory E., Borbat, Peter P., Pratt, Ashley J., Getzoff, Elizabeth D., Freed, Jack H., Crane, Brian R.

    Published in Biophysical journal (07-10-2014)
    “…We demonstrate the ability of pulsed dipolar electron spin resonance (ESR) spectroscopy (PDS) to report on the conformation of Cu-Zn superoxide dismutase…”
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