Zobrazeno 1 - 10
of 94
pro vyhledávání: '"FORD, LINCOLN E."'
Publikováno v:
The Journal of Cell Biology, 1969 May 01. 41(2), 378-392.
Externí odkaz:
https://www.jstor.org/stable/1605636
Force and myosin light chain phosphorylation in dog airway smooth muscle activated in different ways
Publikováno v:
In Respiratory Physiology & Neurobiology 2003 137(2):141-149
Autor:
Ford, Lincoln E.1 leford@hsph.harvard.edu
Publikováno v:
Canadian Journal of Physiology & Pharmacology. Jan2010, Vol. 88 Issue 1, p9-13. 4p. 1 Diagram, 1 Graph.
Autor:
Ford, Lincoln E.1 lieford@iupui.edu, Gilbert, Susan H.1
Publikováno v:
Canadian Journal of Physiology & Pharmacology. Jul2007, Vol. 85 Issue 7, p747-753. 6p. 1 Chart, 3 Graphs.
Autor:
Ford, Lincoln E.1 lieford@iupui.edu
Publikováno v:
Canadian Journal of Physiology & Pharmacology. Oct2005, Vol. 83 Issue 10, p841-850. 10p. 7 Diagrams, 1 Chart.
Autor:
Ford, Lincoln E., Podolsky, Richard J.
Publikováno v:
Science, 1970 Jan 01. 167(3914), 58-59.
Externí odkaz:
https://www.jstor.org/stable/1728185
Muscle birefringence, caused mainly by parallel thick filaments, increases in smooth muscle during stimulation, signalling thick filament formation upon activation. The reverse occurs in skeletal muscle, where a decrease in birefringence has been cor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::262721a1950813073776f14c7b767e24
https://europepmc.org/articles/PMC2075147/
https://europepmc.org/articles/PMC2075147/
Birefringence and force produced by pig tracheal smooth muscles were recorded every 100 ms during electrically stimulated tetani at muscle lengths that varied 1.5-fold and at the peak of acetylcholine contractures at the same lengths. Isometric force
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::28d85d17cb2c2fc70881e55fe3a75a6a
https://europepmc.org/articles/PMC1665598/
https://europepmc.org/articles/PMC1665598/
1. Substituting uridine triphosphate (UTP) for ATP as a substrate for rabbit skeletal myosin and actin at 4 degrees C slowed the dissociation of myosin-S1 from actin by threefold, and hydrolysis of the nucleotide by sevenfold, without a decrease in t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::0a64d55770696a157f37ab1be1d70609
https://europepmc.org/articles/PMC2279008/
https://europepmc.org/articles/PMC2279008/
Publikováno v:
Journal of Applied Physiology; 2000, Vol. 89 Issue 3, p1061-1064, 4p