Nicholas G. Bedrin

ORCID: 0000-0003-3731-0400
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About
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Research Areas
  • Muscle Physiology and Disorders
  • Muscle activation and electromyography studies
  • Cardiomyopathy and Myosin Studies
  • Muscle metabolism and nutrition
  • Innovations in Medical Education
  • Exercise and Physiological Responses
  • Surgical Simulation and Training
  • Adipose Tissue and Metabolism
  • Sports Performance and Training
  • Simulation-Based Education in Healthcare

University of Vermont Medical Center
2021

University of Vermont
2011-2015

We hypothesize that age-related skeletal muscle dysfunction and physical disability may be partially explained by alterations in the function of myosin molecule. To test this hypothesis, at whole muscle, single fiber, molecular levels was measured young (21–35 yr) older (65–75 male female volunteers with similar activity levels. After adjusting for size, adults had knee extensor isometric torque values compared young, but lower isokinetic power, most notably women. At single-fiber levels,...

10.1152/japplphysiol.00563.2013 article EN Journal of Applied Physiology 2013-07-25

Age-related loss of skeletal muscle mass and function is implicated in the development disease physical disability. However, little known about how age affects structure at cellular ultrastructural levels or such alterations impact function. Thus we examined tissue, cellular, myofibrillar young (21–35 yr) older (65–75 male female volunteers, matched for habitual activity level. Older adults had smaller whole tissue cross-sectional areas (CSAs) mass. At level, reduced CSAs myosin heavy chain...

10.1152/japplphysiol.01362.2013 article EN Journal of Applied Physiology 2014-05-02

Skeletal muscle contractile performance is governed by the properties of its constituent fibers, which are, in turn, determined molecular interactions myofilament proteins. To define determinants function humans, we measured mechanics during maximal Ca 2+ -activated and passive isometric conditions single fibers with homogenous (I IIA) mixed (I/IIA IIA/X) myosin heavy chain (MHC) isoforms from healthy, young adult male ( n = 5) female 7) volunteers. Fibers containing only MHC II (IIA...

10.1152/ajpcell.00158.2014 article EN AJP Cell Physiology 2015-01-08

Reduced skeletal muscle function in heart failure (HF) patients may be partially explained by altered myofilament protein content and function. Resistance training increases function, although whether these improvements are achieved correction of deficits is not known. To address this question, we examined 10 HF 14 controls prior to following an 18 week high-intensity resistance programme. Evaluations whole size strength, single fibre size, ultrastructure tension myosin-actin cross-bridge...

10.1113/jphysiol.2011.219659 article EN The Journal of Physiology 2011-12-24
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