Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Christine Brosseau"'
Publikováno v:
Journal of Biological Chemistry. 278:28533-28539
To better understand the molecular basis for some of the unique mechanical properties of tonic smooth muscle, we use a laser trap to assay the mechanochemistry of single smooth muscle heavy meromyosin molecules lacking a seven-amino acid insert in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bcc76d0b42f9cf5aa63fd8065b27127
https://doi.org/10.1074/jbc.m303583200
https://doi.org/10.1074/jbc.m303583200
Autor:
Jeffrey Robbins, Christine Brosseau, Norman R. Alpert, Hanna Osinska, John N. Lorenz, Andrea Federico, David M. Warshaw, Raisa Klevitsky, M. Benjamin Perryman, Maike Krenz, Florence Bouyer-Dalloz, Steve M. Helmke, James Gulick, Timothy E. Hewett, Atsushi Sanbe
Publikováno v:
Journal of Biological Chemistry. 278:17466-17474
Comparison of mammalian cardiac alpha- and beta-myosin heavy chain isoforms reveals 93% identity. To date, genetic methodologies have effected only minor switches in the mammalian cardiac myosin isoforms. Using cardiac-specific transgenesis, we have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::846e9ae13b1a02c0302e98fad04dca17
https://doi.org/10.1074/jbc.m210804200
https://doi.org/10.1074/jbc.m210804200
Publikováno v:
Biophysical Journal. 82(4):2134-2147
To better understand how skeletal muscle myosin molecules move actin filaments, we determine the motion-generating biochemistry of a single myosin molecule and study how it scales with the motion-generating biochemistry of an ensemble of myosin molec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8e0f28a8e1fc34e2767977e636df1f4a
Autor:
David M. Warshaw, Norman R. Alpert, Kelly Vaughn-Whitley, Saidi A Mohiddin, Dorothy Tripodi, Jacqueline Jacobson-Hatzell, Christine Brosseau, Lameh Fananapazir
Publikováno v:
American journal of physiology. Heart and circulatory physiology. 288(3)
Autosomal dominant familial hypertrophic cardiomyopathy (FHC) has variable penetrance and phenotype. Heterozygous mutations in MYH7 encoding β-myosin heavy chain are the most common causes of FHC, and we proposed that “enhanced” mutant actin-myo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5dea030fbc3729bbb3b6c0f44ce8020
https://pubmed.ncbi.nlm.nih.gov/15528230
https://pubmed.ncbi.nlm.nih.gov/15528230
Autor:
David M. Warshaw, Andrea Federico, Maike Krenz, Christine Brosseau, Jeffrey Robbins, Norman R. Alpert
Publikováno v:
American journal of physiology. Heart and circulatory physiology. 283(4)
Two myosin isoforms are expressed in myocardium, αα-homodimers (V1) and ββ-homodimers (V3). V1exhibits higher velocities and myofibrillar ATPase activities compared with V3. We also observed this for cardiac myosin from normal (V1) and propylthio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::21dfda267e1b41af7566cbf19510adf7
https://pubmed.ncbi.nlm.nih.gov/12234796
https://pubmed.ncbi.nlm.nih.gov/12234796