Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Nedjma B. Zitouni"'
Autor:
Lennart Hilbert, Genevieve Bates, Horia N Roman, Jenna L Blumenthal, Nedjma B Zitouni, Apolinary Sobieszek, Michael C Mackey, Anne-Marie Lauzon
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 10, p e1003273 (2013)
The proteins involved in smooth muscle's molecular contractile mechanism - the anti-parallel motion of actin and myosin filaments driven by myosin heads interacting with actin - are found as different isoforms. While their expression levels are alter
Externí odkaz:
https://doaj.org/article/494dcae7d24f47eea35101091263a3f4
Autor:
Genevieve Bates, Nedjma B. Zitouni, Jean-Pierre Lavoie, Gijs Ijpma, Linda Kachmar, Anne-Marie Lauzon, Oleg S. Matusovsky, Andrea Benedetti
Publikováno v:
American Journal of Respiratory Cell and Molecular Biology. 54:718-727
Heaves is a naturally occurring equine disease that shares many similarities with human asthma, including reversible antigen-induced bronchoconstriction, airway inflammation, and remodeling. The purpose of this study was to determine whether the trac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2064e8691f3d49582d1e35704510f723
https://doi.org/10.1165/rcmb.2015-0180oc
https://doi.org/10.1165/rcmb.2015-0180oc
Publikováno v:
Biophysical Journal. 108(3):622-631
Actin filaments propelled in vitro by groups of skeletal muscle myosin motors exhibit distinct phases of active sliding or arrest, whose occurrence depends on actin length (L) within a range of up to 1.0 μm. Smooth muscle myosin filaments are expone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fffe4a6b7fa1bf4f02368521d86b2eaf
Autor:
Oleg S. Matusovsky, Horia N. Roman, Nedjma B. Zitouni, Anne-Marie Lauzon, Andrea Benedetti, Apolinary Sobieszek, Lennart Hilbert, Linda Kachmar, Gijs Ijpma
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1830:4634-4641
Smooth muscle has the distinctive ability to maintain force for long periods of time and at low energy costs. While it is generally agreed that this property, called the latch-state, is due to the dephosphorylation of myosin while attached to actin,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3313b7d99097de806da6048bd63aad9e
https://doi.org/10.1016/j.bbagen.2013.05.042
https://doi.org/10.1016/j.bbagen.2013.05.042
Autor:
Linda Kachmar, Nedjma B. Zitouni, Albert Kalganov, Nabil Shalabi, Dilson E. Rassier, Anne-Marie Lauzon
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1830:2710-2719
Background There is evidence that the actin-activated ATP kinetics and the mechanical work produced by muscle myosin molecules are regulated by two surface loops, located near the ATP binding pocket (loop 1), and in a region that interfaces with acti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ceca94c0bf00a146d2a530bdc860a28a
https://doi.org/10.1016/j.bbagen.2012.11.022
https://doi.org/10.1016/j.bbagen.2012.11.022
Publikováno v:
American Journal of Physiology-Lung Cellular and Molecular Physiology. 291:L932-L940
Four smooth muscle myosin heavy chain (SMMHC) isoforms are generated by alternative mRNA splicing of a single gene. Two of these isoforms differ by the presence [(+)insert] or absence [(−)insert] of a 7-amino acid insert in the motor domain. The ra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85ba120e7c55c0537472734f42ca1590
https://doi.org/10.1152/ajplung.00339.2004
https://doi.org/10.1152/ajplung.00339.2004
Autor:
Horia N. Roman, Nedjma B. Zitouni, Apolinary Sobieszek, Andrea Benedetti, Anne-Marie Lauzon, Linda Kachmar
Smooth muscle has the unique property of maintaining tension with low ATP consumption. It is generally accepted that this property, called the latch-state, results from the dephosphorylation of myosin while attached to actin. However, detached dephos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04d508aa9a0da2eb25855d76db49f675
https://europepmc.org/articles/PMC4165515/
https://europepmc.org/articles/PMC4165515/
Autor:
Anne-Marie Lauzon, Jenna L. Blumenthal, Nedjma B. Zitouni, Apolinary Sobieszek, Genevieve Bates, Lennart Hilbert, Horia N. Roman, Michael C. Mackey
Publikováno v:
PLoS Computational Biology, Vol 9, Iss 10, p e1003273 (2013)
PLoS Computational Biology
PLoS Computational Biology
The proteins involved in smooth muscle's molecular contractile mechanism – the anti-parallel motion of actin and myosin filaments driven by myosin heads interacting with actin – are found as different isoforms. While their expression levels are a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c194ccfd452fc7dfb68793f88f80a493
http://europepmc.org/articles/PMC3812040?pdf=render
http://europepmc.org/articles/PMC3812040?pdf=render
Autor:
Nedjma B. Zitouni, Michael C. Mackey, Anne-Marie Lauzon, Lennart Hilbert, Shivaram Cumarasamy
Publikováno v:
Biophysical journal. 105(6)
Naturally occurring groups of muscle myosin behave differently from individual myosins or small groups commonly assayed in vitro. Here, we investigate the emergence of myosin group behavior with increasing myosin group size. Assuming the number of my
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71c5a616bab3032f8df711d1b8c33c83
https://pubmed.ncbi.nlm.nih.gov/24047998
https://pubmed.ncbi.nlm.nih.gov/24047998
Autor:
Dilson E. Rassier, Andrea Benedetti, Linda Kachmar, Basil J. Petrof, Genevieve Bates, Anne-Marie Lauzon, Sara Sigurdardottir, Nedjma B. Zitouni
Publikováno v:
American journal of physiology. Cell physiology. 304(9)
Duchenne muscular dystrophy (DMD) is a lethal disorder caused by defects in the dystrophin gene, which leads to respiratory or cardiac muscle failure. Lack of dystrophin predisposes the muscle cell sarcolemmal membrane to mechanical damage. However,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9a9c5b76182cee7a6d933d18f53763e
https://pubmed.ncbi.nlm.nih.gov/23426972
https://pubmed.ncbi.nlm.nih.gov/23426972