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John Wright

Researcher at University of Texas at Austin

Publications -  45
Citations -  2572

John Wright is an academic researcher from University of Texas at Austin. The author has contributed to research in topics: Sarcomere & Upper and lower bounds. The author has an hindex of 24, co-authored 45 publications receiving 2330 citations. Previous affiliations of John Wright include Massachusetts Institute of Technology & Carnegie Mellon University.

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Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of the segmental extension model of resting tension.

TL;DR: Immunoelectron microscopic studies of an epitope in the extensible segment of titin revealed a transition in the elastic behavior of the titin filaments near the yield point sarcomere length of these muscles, providing direct evidence of tit in's involvement in the genesis of resting tension.
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Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line.

TL;DR: Immunoblot analysis indicates that although polypeptides of similar size are present in cardiac and smooth muscles at low abundance, those proteins show no immunological cross-reactivity with skeletal muscle nebulin, and raises the possibility that nebulin and titin might act as organizing templates and length-determining factors for actin and myosin respectively.
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Viscoelasticity of the sarcomere matrix of skeletal muscles. The titin-myosin composite filament is a dual-stage molecular spring.

TL;DR: In this article, the authors investigated the structural role of the endosarcomeric lattices of a rabbit psoas muscle fiber with respect to the relative immunoelectron microscopy of the elastic titin filaments.
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Solution-based analysis of multiple analytes by a sensor array: toward the development of an electronic tongue

TL;DR: In this article, a micromachined sensor array was developed for the rapid characterization of multi-component mixtures in aqueous media, using an array composed of individually immobilized polystyrene-polyethylene glycol composite microspheres selectively arranged in micro-achined etch cavities localized o n silicon wafers.
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Nebulin as a length regulator of thin filaments of vertebrate skeletal muscles: correlation of thin filament length, nebulin size, and epitope profile.

TL;DR: It is proposed that nebulin acts as a length- regulating template that determines thin filament length by matching its large number of 40-nm repeating domains with an equal number of helical repeats of the actin filaments.