نتائج البحث - "Yaeren Hernandez"

المصدر: Nature Communications, Vol 11, Iss 1, Pp 1-17 (2020)
Nature Communications, 11(1):2699. Nature Publishing Group UK
Lindqvist, J, Ma, W, Li, F, Hernandez, Y, Kolb, J, Kiss, B, Tonino, P, van der Pijl, R, Karimi, E, Gong, H, Strom, J, Hourani, Z, Smith, J E, Ottenheijm, C A C, Irving, T & Granzier, H 2020, ' Triggering typical nemaline myopathy with compound heterozygous nebulin mutations reveals myofilament structural changes as pathomechanism ', Nature Communications, vol. 11, no. 1, 2699 . https://doi.org/10.1038/s41467-020-16526-9
Nature Communications

مصطلحات موضوعية: Sarcomeres, 0301 basic medicine, Heterozygote, Myofilament, Mice, 129 Strain, Science, Mutation, Missense, Muscle Proteins, General Physics and Astronomy, Tropomyosin, macromolecular substances, Muscle disorder, Myopathies, Nemaline, Sarcomere, Article, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, Nebulin, 0302 clinical medicine, Nemaline myopathy, Microscopy, Electron, Transmission, Myofibrils, X-Ray Diffraction, medicine, Animals, Muscle, Skeletal, lcsh:Science, Cytoskeleton, Actin, Multidisciplinary, biology, Chemistry, Skeletal muscle, General Chemistry, Neuromuscular disease, medicine.disease, Troponin, Cell biology, Mice, Inbred C57BL, Actin Cytoskeleton, 030104 developmental biology, medicine.anatomical_structure, biology.protein, Muscle, lcsh:Q, Myofibril, 030217 neurology & neurosurgery

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::158f7f53cf1a448aeb85bc5d60978071
http://link.springer.com/article/10.1038/s41467-020-16526-9

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6

Implementation of docking, molecular dynamics and free energy to investigate drug potency of novel BCR-ABLT315I inhibitors as an alternative to ponatinib

المؤلفون: Atefe Ghodrati, Mahmood Fadaie, Seyed Sadegh Eslami, Parastoo Tarighi, Yaeren Hernandez, Mohammad Mahmoudi Gomari, Neda Rostami

المصدر: Computational Toxicology. 20:100180

مصطلحات موضوعية: business.industry, Health, Toxicology and Mutagenesis, Ponatinib, breakpoint cluster region, Myeloid leukemia, Cancer, Drug resistance, Toxicology, medicine.disease, Small molecule, Computer Science Applications, chemistry.chemical_compound, chemistry, In vivo, Docking (molecular), hemic and lymphatic diseases, Cancer research, Medicine, business

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_________::4ebe1da92e95198e47a5df0153ca6132
https://doi.org/10.1016/j.comtox.2021.100180

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7

Downsizing the molecular spring of the giant protein titin reveals that skeletal muscle titin determines passive stiffness and drives longitudinal hypertrophy

المؤلفون: J. D. T. Smith, Maya Adler, Johan Lindqvist, Jochen Gohlke, Joshua Strom, Robbert van der Pijl, Coen A.C. Ottenheijm, Balázs Kiss, Justin Kolb, Henk Granzier, Ambjorn Brynnel, Yaeren Hernandez

المساهمون: Physiology, ACS - Pulmonary hypertension & thrombosis, ACS - Heart failure & arrhythmias

المصدر: eLife, 7:e40532. eLife Sciences Publications Limited
eLife
Brynnel, A, Hernandez, Y, Kiss, B, Lindqvist, J, Adler, M, Kolb, J, van der Pijl, R, Gohlke, J, Strom, J, Smith, J, Ottenheijm, C & Granzier, H L 2018, ' Downsizing the molecular spring of the giant protein titin reveals that skeletal muscle titin determines passive stiffness and drives longitudinal hypertrophy ', eLife, vol. 7, e40532 . https://doi.org/10.7554/eLife.40532, https://doi.org/10.7554/eLife.40532
eLife, Vol 7 (2018)

مصطلحات موضوعية: 0301 basic medicine, Myofilament, Mouse, muscle, Physics of Living Systems, Sarcomere, Muscle hypertrophy, Extracellular matrix, Mice, Myofibrils, Connectin, Biology (General), biology, Chemistry, General Neuroscience, Molecular spring, General Medicine, musculoskeletal system, Extracellular Matrix, Actin Cytoskeleton, medicine.anatomical_structure, Medicine, Titin, Sarcomeres, animal structures, QH301-705.5, Science, titinopathies, passive stiffness, macromolecular substances, biomechanics, General Biochemistry, Genetics and Molecular Biology, Research Communication, 03 medical and health sciences, medicine, Animals, Humans, Muscle, Skeletal, Actin, General Immunology and Microbiology, Myocardium, Skeletal muscle, Hypertrophy, Elastic Tissue, Muscle, Striated, 030104 developmental biology, biology.protein, Biophysics, elasticity, myofilament function