New Greenberg lab collaborative publication on tropomyosin mutations in myopathies and birth defects

In collaboration with the Gurnett and Johnson labs, we looked at pathogenic mutations in tropomyosin that cause various forms of skeletal myopathies and birth defects. McAdow J, Yang S, Ou T, Huang G, Dobbs MB, Gurnett CA, Greenberg MJ, Johnson AN. A pathogenic mechanism associated with myopathies and structural birth defects involves TPM2 directed myogenesis. JCI Insight. 2022 May 17:e152466. doi: 10.1172/jci.insight.152466. Epub ahead of print. PMID: 35579956.
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Greenberg lab and friends present at BPS 2022

The Greenberg lab had 4 presentations at BPS 2022: Platform (Samantha Barrick - Postdoc): STRUCTURAL DIFFERENCES IN VINCULIN AND METAVINCULIN ACTIN-BINDING DOMAINS EXPLORED BY MOLECULAR DYNAMICS SIMULATIONS Poster (Jeff Lotthammer – Student Bowman lab): EXPLORING THE MYOSIN ACTIVE/AUTO-INHIBITED STATE EQUILIBRIUM BY MARKOV STATE MODELING Poster (Artur Meller – Student Bowman lab): SIGNATURES OF ALLOSTERIC MODULATOR SPECIFICITY ARE ENCODED IN MYOSIN MOTOR DOMAIN EQUILIBRIUM FLUCTUATIONS Poster (Michael Greenberg - PI): HARNESSING MULTISCALE MODELS OF A DILATED CARDIOMYOPATHY MUTATION FOR PRECISION MEDICINE
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Greenberg lab presents at ASCB 2021

The Greenberg lab had 2 posters as ASCB 2021: Dr. Samantha Barrick presented a poster: A Troponin T Variant Linked with Pediatric Dilated Cardiomyopathy Decreases Cardiac Contractility by Reducing the Coupling of Thin Filament Activation to Myosin and Calcium Binding And Michael Greenberg presented: Utilizing Multiscale Models of a Dilated Cardiomyopathy Mutation for Precision Medicine, which included collaborative work from the Lavine lab.
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New Greenberg lab publication on pediatric dilated cardiomyopathy from Dr. Barrick

New publication from the Greenberg lab is now online at the Molecular Biology of the Cell (here).  This work, led by first author Dr. Samantha Barrick, examines a variant in troponin T associated with pediatric onset dilated cardiomyopathy. We show that this variant causes molecular and cellular alterations consistent with those seen in known pathogenic variants. We show that the molecular mechanism driving the early disease pathogenesis is reduced coupling between calcium binding to troponin C and thin filament activation. This in turn leads to changes in cellular contractility and sarcomeric organization.
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