Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Kim S. Lau"'
Publikováno v:
Journal of Biological Chemistry. 282:20447-20454
Repetitive low frequency stimulation results in potentiation of twitch force development in fast-twitch skeletal muscle due to myosin regulatory light chain (RLC) phosphorylation by Ca(2+)/calmodulin (CaM)-dependent skeletal muscle myosin light chain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::628d72a9620179b6cb8a2e127199688f
https://doi.org/10.1074/jbc.m702927200
https://doi.org/10.1074/jbc.m702927200
Autor:
Annette Meeson, Kim S. Lau, Daniel J. Garry, Robert W. Grange, E. V A Chin, John M. Shelton, James T. Stull, R. Sanders Williams
Publikováno v:
American Journal of Physiology-Cell Physiology. 281:C1487-C1494
Myoglobin is a cytoplasmic hemoprotein that is restricted to cardiomyocytes and oxidative skeletal myofibers and facilitates oxygen delivery during periods of high metabolic demand. Myoglobin content in skeletal muscle increases in response to hypoxi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dc4bf44d850397c5db8e1145866cf17
https://doi.org/10.1152/ajpcell.2001.281.5.c1487
https://doi.org/10.1152/ajpcell.2001.281.5.c1487
Publikováno v:
Physiological Genomics. 5:35-44
During skeletal muscle contraction, NO derived from neuronal nitric oxide synthase (nNOS) in skeletal muscle fibers or from endothelial cells (eNOS) may relax vascular smooth muscle contributing to functional hyperemia. To examine the relative import
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8cb475b5ba2a914f109bf08fc2e75d8
https://doi.org/10.1152/physiolgenomics.2001.5.1.35
https://doi.org/10.1152/physiolgenomics.2001.5.1.35
Autor:
Paul L. Huang, Kim S. Lau, Kristine E. Kamm, Ingrid H. Sarelius, Robert W. Grange, James T. Stull, Eiji Isotani
Publikováno v:
Physiological Genomics. 2:21-27
Lau, Kim S., Robert W. Grange, Eiji Isotani, Ingrid H. Sarelius, Kristine E. Kamm, Paul L. Huang, and James T. Stull. nNOS and eNOS modulate cGMP formation and vascular response in contracting fast-twitch skeletal muscle. Physiol. Genomics 2: 21–27
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8da91f485c1d0b1a2fea753c0a522230
https://doi.org/10.1152/physiolgenomics.2000.2.1.21
https://doi.org/10.1152/physiolgenomics.2000.2.1.21
Autor:
Joshua R. Sanes, R. Mark Grady, James T. Stull, Mia C. Nichol, Robert W. Grange, Kim S. Lau, Margaret M. Maimone
Publikováno v:
Nature Cell Biology. 1:215-220
A dystrophin-containing glycoprotein complex (DGC) links the basal lamina surrounding each muscle fibre to the fibre's cytoskeleton, providing both structural support and a scaffold for signalling molecules. Mutations in genes encoding several DGC co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64df297818f14b4cf73c903b158d82bc
https://doi.org/10.1038/12034
https://doi.org/10.1038/12034
Autor:
Kim S. Lau, Ingrid H. Sarelius, James T. Stull, Robert W. Grange, Wen Jinn Chang, Kristine E. Kamm
Publikováno v:
FEBS Letters. 431:71-74
Nitric oxide generated by neuronal nitric oxide synthase in contracting skeletal muscle fibers may regulate vascular relaxation via a cGMP-mediated pathway. Neuronal nitric oxide synthase content is greatly reduced in skeletal muscles from mdx mice.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38f830fde822f605e39f33fb45e2a0ae
https://doi.org/10.1016/s0014-5793(98)00728-5
https://doi.org/10.1016/s0014-5793(98)00728-5
Autor:
Kim S. Lau, Kirk McMillan, Timothy J. McCabe, Wen Jinn Chang, James G. Tidball, Roanna C. Padre, Susan T. Iannaccone, James T. Stull, Melissa J. Spencer, Bettie Sue Siler Masters
Publikováno v:
Proceedings of the National Academy of Sciences. 93:9142-9147
Neuronal nitric oxide synthase (nNOS) in fast-twitch skeletal muscle fibers is primarily particulate in contrast to its greater solubility in brain. Immunohistochemistry shows nNOS localized to the sarcolemma, with enrichment at force transmitting si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::252166f13090f530bfa28d2d5447ee05
https://doi.org/10.1073/pnas.93.17.9142
https://doi.org/10.1073/pnas.93.17.9142
Autor:
Leeju C. Wu, Kim S. Lau, Amy J. North, Philip W. Shaul, Timothy S. Brannon, Zohre German, Lieselotte B. Wells
Publikováno v:
American Journal of Physiology-Lung Cellular and Molecular Physiology. 270:L643-L649
Nitric oxide (NO) is critically involved in oxygen-mediated pulmonary vasodilatation in the fetus and newborn. We determined the effects of prolonged alterations in oxygenation on endothelial NO synthase (eNOS) gene expression in early passage ovine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06bd8f124a32649325eff7cebf96159a
https://doi.org/10.1152/ajplung.1996.270.4.l643
https://doi.org/10.1152/ajplung.1996.270.4.l643
Autor:
Yi-Shuian Huang, Gordon Aalund, David T. Chuang, Kim S. Lau, Menghsiao Meng, R. Max Wynn, James R. Davie
Publikováno v:
Journal of Biological Chemistry. 270:19861-19867
The recombinant rat branched-chain alpha-ketoacid dehydrogenase kinase has been amplified from rat kidney cDNA, based on the previously reported rat cDNA sequence (Popov, K. M., Zhao, Y., Shimomura, Y., Kuntz, M. J., and Harris, R. A. (1992) J. Biol.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7094a8269f2ded6aa414ab5075626a32
https://doi.org/10.1074/jbc.270.34.19861
https://doi.org/10.1074/jbc.270.34.19861
Autor:
W J Herring, David T. Chuang, D J Danner, Kim S. Lau, Jacinta L. Chuang, Rody P. Cox, M McKean
Publikováno v:
Journal of Biological Chemistry. 267:24090-24096
We have determined the structural organization of the dihydrolipoyl transacylase (E2) gene of the human branched chain alpha-keto acid dehydrogenase complex. The single copy E2 gene spans approximately 68 kilobases of genomic DNA. The complete coding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5eeed71dfa695804aa95a181cba61999
https://doi.org/10.1016/s0021-9258(18)35950-7
https://doi.org/10.1016/s0021-9258(18)35950-7