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Nature Structural & Molecular Biology|August 2, 2016
Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocationAdam L Yokom, Stephanie N Gates, Meredith E Jackrel, et al.Biochemistry|April 6, 2017
Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 StructuresClarissa L Weaver, Elizabeth C Duran, Korrie L Mack, et al.Molecular Cell|January 27, 2015
The Hsp104 N-terminal domain enables disaggregase plasticity and potentiationElizabeth A Sweeny, Meredith E Jackrel, Michelle S Go, et al.FEMS Yeast Research|May 23, 2018
Potentiating Hsp104 activity via phosphomimetic mutations in the middle domainAmber Tariq, JiaBei Lin, Megan M Noll, et al.Molecular Cell|August 10, 2019
Quality Control in the ER: Misfolded Prohormones Get a CheckupMacy L Sprunger, Meredith E JackrelSTAR Protocols|August 5, 2022
Monitoring condensate dynamics in S. cerevisiae using fluorescence recovery after photobleachingMacy L Sprunger, Meredith E JackrelBiochemical Society Transactions|May 30, 2024
The role of Matrin-3 in physiology and its dysregulation in diseaseMacy L Sprunger, Meredith E JackrelBiomolecules|August 6, 2021
Prion-Like Proteins in Phase Separation and Their Link to DiseaseMacy L Sprunger, Meredith E JackrelCell|January 21, 2014
Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding eventsMeredith E Jackrel, Morgan E DeSantis, Bryan A Martinez, et al.Protein Science : a Publication of the Protein Society|March 25, 2009
Redesign of a protein-peptide interaction: characterization and applicationsMeredith E Jackrel, Roberto Valverde, Lynne ReganPageof 21