Scholars@Duke
Amber Leigh Bowman

Amber Leigh Bowman

Assistant Professor of Medicine
Medicine, General Internal Medicine
amber.bowman@duke.edu
Dept of Medicine, BOX_31325, Durham, NC 27710

Selected Publications

Current Use, Training, and Barriers of Point-of-Care Ultrasound in Anesthesiology: A National Survey of Veterans Affairs Hospitals.

Journal Article J Cardiothorac Vasc Anesth · August 2023 OBJECTIVES: The purpose of this study was to determine current use, training needs, and barriers to point-of-care ultrasound (POCUS) use among anesthesiologists in practice. DESIGN: Multicenter, prospective, observational study. SETTING: Anesthesiology dep ... Full text Link to item Cite

Phosphorylation of Src by phosphoinositide 3-kinase regulates beta-adrenergic receptor-mediated EGFR transactivation.

Journal Article Cell Signal · October 2016 β2-Adrenergic receptors (β2AR) transactivate epidermal growth factor receptors (EGFR) through formation of a β2AR-EGFR complex that requires activation of Src to mediate signaling. Here, we show that both lipid and protein kinase activities of the bifuncti ... Full text Link to item Cite

Muscle giants: molecular scaffolds in sarcomerogenesis.

Journal Article Physiol Rev · October 2009 Myofibrillogenesis in striated muscles is a highly complex process that depends on the coordinated assembly and integration of a large number of contractile, cytoskeletal, and signaling proteins into regular arrays, the sarcomeres. It is also associated wi ... Full text Link to item Cite

The rho-guanine nucleotide exchange factor domain of obscurin activates rhoA signaling in skeletal muscle.

Journal Article Mol Biol Cell · September 2009 Obscurin is a large ( approximately 800-kDa), modular protein of striated muscle that concentrates around the M-bands and Z-disks of each sarcomere, where it is well positioned to sense contractile activity. Obscurin contains several signaling domains, inc ... Full text Link to item Cite

Obscurin interacts with a novel isoform of MyBP-C slow at the periphery of the sarcomeric M-band and regulates thick filament assembly.

Journal Article Mol Biol Cell · June 2009 Obscurin is a multidomain protein composed of adhesion and signaling domains that plays key roles in the organization of contractile and membrane structures in striated muscles. Overexpression of the second immunoglobulin domain of obscurin (Ig2) in develo ... Full text Link to item Cite

The rho-guanine nucleotide exchange factor domain of obscurin regulates assembly of titin at the Z-disk through interactions with Ran binding protein 9.

Journal Article Mol Biol Cell · September 2008 Obscurin is an approximately 800-kDa protein composed of structural and signaling domains that organizes contractile structures in striated muscle. We have studied the Rho-GEF domain of obscurin to understand its roles in morphogenesis and signaling. We us ... Full text Link to item Cite

Different obscurin isoforms localize to distinct sites at sarcomeres.

Journal Article FEBS Lett · April 17, 2007 We used four antibodies to regions of obscurin isoforms A and B, encoded by the obscurin gene, to investigate the location of these proteins in skeletal myofibers at resting and stretched lengths. Obscurin A ( approximately 800 kDa) which was recognized by ... Full text Link to item Cite

Cloning and characterization of cytokeratins 8 and 19 in adult rat striated muscle. Interaction with the dystrophin glycoprotein complex.

Journal Article J Biol Chem · October 1, 2004 We used degenerate primers for the amino- and carboxyl-terminal ends of the rod domains of intermediate filament proteins in reverse transcriptase-PCR experiments to identify and clone cytokeratins 8 and 19 (K8 and K19) from cardiac muscle of the adult rat ... Full text Link to item Cite