T
Thomas C. Irving
Researcher at Illinois Institute of Technology
Publications - 227
Citations - 9049
Thomas C. Irving is an academic researcher from Illinois Institute of Technology. The author has contributed to research in topics: Myosin & Myofilament. The author has an hindex of 47, co-authored 192 publications receiving 7835 citations. Previous affiliations of Thomas C. Irving include Brandeis University & Loyola University Chicago.
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Journal ArticleDOI
Microfibrillar structure of type I collagen in situ
TL;DR: The molecular packing structure of collagen shown here provides information concerning the potential modes of action of two prominent molecules involved in human health and disease: decorin and the Matrix Metallo-Proteinase (MMP) collagenase.
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Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filaments.
Henk Granzier,Thomas C. Irving +1 more
TL;DR: The passive tension-sarcomere length relation of rat cardiac muscle was investigated by studying passive (or not activated) single myocytes and trabeculae and the contribution of collagen, titin, microtubules, and intermediate filaments to tension and stiffness was investigated.
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X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle.
TL;DR: Observations of filament extensions totaling 2-3 nm per half-sarcomere may necessitate some significant revision of the interpretation of a number of mechanical experiments in muscle, in which it has usually been assumed that virtually all of the elasticity resides in the cross-bridges.
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The In Situ Supermolecular Structure of Type I Collagen
Joseph P. R. O. Orgel,Andrew Miller,Thomas C. Irving,Robert F. Fischetti,Andrew Hammersley,Tim J Wess +5 more
TL;DR: The electron density map reveals the three-dimensional molecular packing arrangement of type I collagen and conclusively proves that the molecules are arranged on a quasihexagonal lattice.
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Skeletal Muscle Performance Determined by Modulation of Number of Myosin Motors Rather Than Motor Force or Stroke Size
Gabriella Piazzesi,Massimo Reconditi,Marco Linari,Leonardo Lucii,Pasquale Bianco,Pasquale Bianco,E Brunello,E Brunello,Valérie Decostre,Alex Stewart,David Gore,Thomas C. Irving,Malcolm Irving,Vincenzo Lombardi,Vincenzo Lombardi +14 more
TL;DR: It is shown that, during muscle shortening at a wide range of velocities, individual myosin motors maintain a force of about 6 pN while pulling an actin filament through a 6 nm stroke, then quickly detach when the motor reaches a critical conformation.