Search Results - "Gidalevitz, Tali"

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  1. 1

    Orchestration of secretory protein folding by ER chaperones by Gidalevitz, Tali, Stevens, Fred, Argon, Yair

    Published in Biochimica et biophysica acta (01-11-2013)
    “…The endoplasmic reticulum is a major compartment of protein biogenesis in the cell, dedicated to production of secretory, membrane and organelle proteins. The…”
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    HSP-4/BiP expression in secretory cells is regulated by a developmental program and not by the unfolded protein response by Zha, Ji, Ying, Mingjie, Alexander-Floyd, Jasmine, Gidalevitz, Tali

    Published in PLoS biology (25-03-2019)
    “…Differentiation of secretory cells leads to sharp increases in protein synthesis, challenging endoplasmic reticulum (ER) proteostasis. Anticipatory activation…”
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    A Bystander Mechanism Explains the Specific Phenotype of a Broadly Expressed Misfolded Protein by Klabonski, Lauren, Zha, Ji, Senthilkumar, Lakshana, Gidalevitz, Tali

    Published in PLoS genetics (01-12-2016)
    “…Misfolded proteins in transgenic models of conformational diseases interfere with proteostasis machinery and compromise the function of many structurally and…”
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    Destabilizing protein polymorphisms in the genetic background direct phenotypic expression of mutant SOD1 toxicity by Gidalevitz, Tali, Krupinski, Thomas, Garcia, Susana, Morimoto, Richard I

    Published in PLoS genetics (01-03-2009)
    “…Genetic background exerts a strong modulatory effect on the toxicity of aggregation-prone proteins in conformational diseases. In addition to influencing the…”
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    Progressive Disruption of Cellular Protein Folding in Models of Polyglutamine Diseases by Gidalevitz, Tali, Ben-Zvi, Anat, Ho, Kim H, Brignull, Heather R, Morimoto, Richard I

    “…Numerous human diseases are associated with the chronic expression of misfolded and aggregation-prone proteins. The expansion of polyglutamine residues in…”
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    A cellular perspective on conformational disease: the role of genetic background and proteostasis networks by Gidalevitz, Tali, Kikis, Elise A, Morimoto, Richard I

    Published in Current opinion in structural biology (01-02-2010)
    “…The inherently error-prone nature of protein biosynthesis and turnover leads to a constant flux of destabilized proteins. Genetic mutations in conformational…”
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    Multiple Molecular Mechanisms Rescue mtDNA Disease in C. elegans by Haroon, Suraiya, Li, Annie, Weinert, Jaye L., Fritsch, Clark, Ericson, Nolan G., Alexander-Floyd, Jasmine, Braeckman, Bart P., Haynes, Cole M., Bielas, Jason H., Gidalevitz, Tali, Vermulst, Marc

    Published in Cell reports (Cambridge) (20-03-2018)
    “…Genetic instability of the mitochondrial genome (mtDNA) plays an important role in human aging and disease. Thus far, it has proven difficult to develop…”
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    Identification of the N-terminal Peptide Binding Site of Glucose-regulated Protein 94 by Gidalevitz, Tali, Biswas, Chhanda, Ding, Hua, Schneidman-Duhovny, Dina, Wolfson, Haim J., Stevens, Fred, Radford, Sheena, Argon, Yair

    Published in The Journal of biological chemistry (16-04-2004)
    “…Because the stress protein GRP94 can augment presentation of peptides to T cells, it is important to define how it, as well as all other HSP90 family members,…”
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    Protein Disulfide Isomerase A6 Controls the Decay of IRE1α Signaling via Disulfide-Dependent Association by Eletto, Davide, Eletto, Daniela, Dersh, Devin, Gidalevitz, Tali, Argon, Yair

    Published in Molecular cell (20-02-2014)
    “…The response to endoplasmic reticulum (ER) stress relies on activation of unfolded protein response (UPR) sensors, and the outcome of the UPR depends on the…”
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    The special unfolded protein response in plasma cells by Ricci, Daniela, Gidalevitz, Tali, Argon, Yair

    Published in Immunological reviews (01-09-2021)
    “…The high rate of antibody production places considerable metabolic and folding stress on plasma cells (PC). Not surprisingly, they rely on the unfolded protein…”
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    Radicicol-sensitive Peptide Binding to the N-terminal Portion of GRP94 by Vogen, Shawn, Gidalevitz, Tali, Biswas, Chhanda, Simen, Birgitte B, Stein, Eytan, Gulmen, Funda, Argon, Yair

    Published in The Journal of biological chemistry (25-10-2002)
    “…GRP94 is a molecular chaperone that carries immunologically relevant peptides from cell to cell, transferring them to major histocompatibility proteins for…”
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  13. 13

    Candidate genes that affect aging through protein homeostasis by Argon, Yair, Gidalevitz, Tali

    “…Because aging is a multifactorial, pleiotropic process where many interacting mechanisms contribute to the organismal decline, the candidate gene approach…”
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    The Sensor IRE1 Couples Stress Detection to Protein Synthesis by Ricci, Daniela, Saunders, Jillian, Tutton, Stephen, Gidalevitz, Tali, Argon, Yair

    Published in The FASEB journal (01-05-2021)
    “…Endoplasmic reticulum (ER) stress results in accumulation of misfolded proteins and profoundly regulates cellular protein synthesis. The regulation includes…”
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    The stress of protein misfolding: from single cells to multicellular organisms by Gidalevitz, Tali, Prahlad, Veena, Morimoto, Richard I

    Published in Cold Spring Harbor perspectives in biology (01-06-2011)
    “…Organisms survive changes in the environment by altering their rates of metabolism, growth, and reproduction. At the same time, the system must ensure the…”
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    Increased activity of IRE1 improves the clinical presentation of EAE by Bracchi‐Ricard, Valerie, Nguyen, Kayla, Ricci, Daniela, Gaudette, Brian, Henao‐Mejia, Jorge, Brambilla, Roberta, Martynyuk, Tetyana, Gidalevitz, Tali, Allman, David, Bethea, John R., Argon, Yair

    Published in The FASEB journal (01-12-2023)
    “…Activation of the endoplasmic reticulum (ER) stress sensor inositol‐requiring enzyme‐1α (IRE1α) contributes to neuronal development and is known to induce…”
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    Protein homeostasis in models of aging and age-related conformational disease by Kikis, Elise A, Gidalevitz, Tali, Morimoto, Richard I

    “…The stability of the proteome is crucial to the health of the cell, and contributes significantly to the lifespan of the organism. Aging and many age-related…”
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