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Biochemistry|June 22, 2005
Kinetic stabilization of an oligomeric protein under physiological conditions demonstrated by a lack of subunit exchange: implications for transthyretin amyloidosisR Luke Wiseman, Nora S Green, Jeffery W KellyTrends in Molecular Medicine|May 13, 2019
Proteostasis and Beyond: ATF6 in Ischemic DiseaseChristopher C Glembotski, Jessica D Rosarda, R Luke WisemanThe Journal of Cell Biology|February 22, 2022
Stress-responsive regulation of extracellular proteostasisJaleh S Mesgarzadeh, Joel N Buxbaum, R Luke WisemanTrends in Endocrinology and Metabolism: TEM|July 23, 2014
Stress-responsive regulation of mitochondria through the ER unfolded protein responseT Kelly Rainbolt, Jaclyn M Saunders, R Luke WisemanEMBO Reports|November 30, 2014
YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stressT Kelly Rainbolt, Jaclyn M Saunders, R Luke WisemanIUBMB Life|May 29, 2015
Endoplasmic reticulum quality control and systemic amyloid disease: Impacting protein stability from the inside outJohn J Chen, Joseph C Genereux, R Luke WisemanMolecular Cell|April 22, 2022
Reshaping endoplasmic reticulum quality control through the unfolded protein responseR Luke Wiseman, Jaleh S Mesgarzadeh, Linda M HendershotBiochemistry|December 14, 2005
Partitioning conformational intermediates between competing refolding and aggregation pathways: insights into transthyretin amyloid diseaseR Luke Wiseman, Evan T Powers, Jeffery W KellyBiochemistry|November 23, 2005
The pathway by which the tetrameric protein transthyretin dissociatesTed R Foss, R Luke Wiseman, Jeffery W KellyNature Chemical Biology|July 22, 2020
Pharmacologic IRE1/XBP1s activation confers targeted ER proteostasis reprogrammingJulia M D Grandjean, Aparajita Madhavan, Lauren Cech, et al.Pageof 20