Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Younss Ait Mou"'
Autor:
Kamran Khowaja, Dena Al-Thani, Asma Osman Hassan, Yasmin Abdelaal, Younss Ait Mou, Mohamad Hassan Fadi Hijab
Publikováno v:
HCI in Games: Serious and Immersive Games ISBN: 9783030774134
HCI (29)
HCI (29)
This virtual classroom has created a lot of challenges for students with limited access to the technology (computer or smartphone) or the Internet and especially for the parents of children with developmental disabilities, including children with aut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8000e1b3f72d3c747dd7ccf3ebd6a3c7
https://doi.org/10.1007/978-3-030-77414-1_24
https://doi.org/10.1007/978-3-030-77414-1_24
Publikováno v:
Bioprinting. 23:e00148
3D printing (3DP) processes have evolved from simple prototyping for visual inspection purposes to functional product manufacturing that offers flexibility, customization, scalability, reliability, durability, and relatively high speed. These process
Autor:
Thomas C. Irving, Bijan Ghaleh, Olivier Cazorla, Younss Ait Mou, Valérie Scheuermann, Alain Lacampagne, Stéphane Blot, Pieter P. de Tombe
Publikováno v:
Journal of Molecular and Cellular Cardiology
Journal of Molecular and Cellular Cardiology, Elsevier, 2018, 114, pp.345-353. ⟨10.1016/j.yjmcc.2017.12.008⟩
Journal of Molecular and Cellular Cardiology, Elsevier, 2018, 114, pp.345-353. ⟨10.1016/j.yjmcc.2017.12.008⟩
AimsDuchenne Muscular Dystrophy (DMD) is a disease that mainly affects young mans. It is characterized by striated muscle disorder. DMD is associated with depressed heart pump function resulting from a down regulation of the left ventricular (LV) con
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24e6068173b15501867811eaa058c74a
https://hal.umontpellier.fr/hal-02376879/document
https://hal.umontpellier.fr/hal-02376879/document
Autor:
Namthip Witayavanitkul, Margaret V. Westfall, Sakthivel Sadayappan, Sudarsan Rajan, Ramzi J. Khairallah, David F. Wieczorek, Jason Sarkey, Ying Ge, Thomas C. Irving, Younss Ait Mou, Pieter P. de Tombe, Diederik W. D. Kuster, Suresh Govindan, Xin-Xin Chen
Publikováno v:
The Journal of Biological Chemistry
Journal of Biological Chemistry, 289(13), 8818-8827. American Society for Biochemistry and Molecular Biology Inc.
Witayavanitkul, N, Mou, Y A, Kuster, D W D, Khairallah, R J, Sarkey, J, Govindan, S, Chen, X, Ge, Y, Rajan, S, Wieczorek, D F, Irving, T, Westfall, M V, de Tombe, P P & Sadayappan, S 2014, ' Myocardial Infarction-induced N-terminal Fragment of Cardiac Myosin-binding Protein C ( cMyBP-C) Impairs Myofilament Function in Human Myocardium ', Journal of Biological Chemistry, vol. 289, no. 13, pp. 8818-8827 . https://doi.org/10.1074/jbc.M113.541128
Journal of Biological Chemistry, 289(13), 8818-8827. American Society for Biochemistry and Molecular Biology Inc.
Witayavanitkul, N, Mou, Y A, Kuster, D W D, Khairallah, R J, Sarkey, J, Govindan, S, Chen, X, Ge, Y, Rajan, S, Wieczorek, D F, Irving, T, Westfall, M V, de Tombe, P P & Sadayappan, S 2014, ' Myocardial Infarction-induced N-terminal Fragment of Cardiac Myosin-binding Protein C ( cMyBP-C) Impairs Myofilament Function in Human Myocardium ', Journal of Biological Chemistry, vol. 289, no. 13, pp. 8818-8827 . https://doi.org/10.1074/jbc.M113.541128
Background: Myocardial infarction (MI) leads to proteolytic cleavage of cMyBP-C (hC0C1f) and decreased contractility. Results: hC0C1f can incorporate into the human cardiac sarcomere, depressing force generation and increasing tension cost. Conclusio
Autor:
Marion L. Greaser, Karen Hsu, Pieter P. de Tombe, Younss Ait-Mou, Gerrie P. Farman, Mohit Kumar, Thomas C. Irving
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 113(8)
The Frank-Starling mechanism of the heart is due, in part, to modulation of myofilament Ca(2+) sensitivity by sarcomere length (SL) [length-dependent activation (LDA)]. The molecular mechanism(s) that underlie LDA are unknown. Recent evidence has imp
Autor:
Nicolas Blanchard-Gutton, Pablo Aguilar, Yves Unterfinger, Alain Berdeaux, Jin Bo Su, Jean Laurent Thibaud, Alain Bizé, Stéphane Blot, Luc Hittinger, Hubert Dabiré, Vassiliki Gouni, Alain Lacampagne, Jean Louis Pouchelon, Olivier Cazorla, Inès Barthélémy, Lucien Sambin, Valérie Chetboul, Bijan Ghaleh, Younss Ait Mou, Carolina Carlos Sampedrano
Publikováno v:
Cardiovascular Research
Cardiovascular Research, Oxford University Press (OUP), 2012, 95 (1), pp.86-96. ⟨10.1093/cvr/cvs161⟩
Cardiovascular Research, 2012, 95 (1), pp.86-96. ⟨10.1093/cvr/cvs161⟩
Cardiovascular Research, Oxford University Press (OUP), 2012, 95 (1), pp.86-96. ⟨10.1093/cvr/cvs161⟩
Cardiovascular Research, 2012, 95 (1), pp.86-96. ⟨10.1093/cvr/cvs161⟩
AIMS: Cardiomyopathy is a lethal result of Duchenne muscular dystrophy (DMD), but its characteristics remain elusive. The golden retriever muscular dystrophy (GRMD) dogs produce DMD pathology and mirror DMD patient's symptoms, including cardiomyopath
Publikováno v:
Biophysical Journal. 114:112a
Publikováno v:
Global Cardiology Science and Practice
Global Cardiology Science and Practice, 2015, 2015 (1), ⟨10.5339/gcsp.2015.10⟩
Global Cardiology Science & Practice
Global Cardiology Science and Practice, 2015, 2015 (1), ⟨10.5339/gcsp.2015.10⟩
Global Cardiology Science & Practice
The heart is subject to multiple sources of stress. To maintain its normal function, and successfully overcome these stresses, heart muscle is equipped with fine-tuned regulatory mechanisms. Some of these mechanisms are inherent within the myocardium
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cbca819040d7197ddedbd5ec295021c
https://hal.umontpellier.fr/hal-01762169
https://hal.umontpellier.fr/hal-01762169
Publikováno v:
Circulation. 130
The cellular basis of the Frank-Starling mechanism is sarcomere length (SL) modulation of myofilament Ca 2+ sensitivity (LDA). The molecular mechanism(s) that underlie LDA are unknown, but recent evidence has implicated the giant protein titin as pos
Publikováno v:
The FASEB Journal. 28
Cardiac myosin binding protein-C (cMyBP-C) phosphorylation is necessary for the regulation of sarcomeric structure and myocardial contractility in vivo. Different from skeletal isoforms, cMyBP-C has M-domain phosphorylation motifs in which three seri