Zobrazeno 1 - 10
of 73
pro vyhledávání: '"Montserrat Samsó"'
Autor:
Robyn T. Rebbeck, Bengt Svensson, Jingyan Zhang, Montserrat Samsó, David D. Thomas, Donald M. Bers, Razvan L. Cornea
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Calmodulin transduces [Ca2+] information regulating the rhythmic Ca2+ cycling between the sarcoplasmic reticulum and cytoplasm during contraction and relaxation in cardiac and skeletal muscle. However, the structural dynamics by which calmod
Externí odkaz:
https://doaj.org/article/7cf35385c2e841cd82d95bed6b88e184
Autor:
Ashok R. Nayak, Warin Rangubpit, Alex H. Will, Yifan Hu, Pablo Castro-Hartmann, Joshua J. Lobo, Kelly Dryden, Graham D. Lamb, Pornthep Sompornpisut, Montserrat Samsó
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract RyR1 is an intracellular Ca2+ channel important in excitable cells such as neurons and muscle fibers. Ca2+ activates it at low concentrations and inhibits it at high concentrations. Mg2+ is the main physiological RyR1 inhibitor, an effect th
Externí odkaz:
https://doaj.org/article/84e456c577cc459aa27a8ef47bfa4340
Publikováno v:
mBio, Vol 13, Iss 6 (2022)
ABSTRACT Type 4 pili (T4P) are retractable surface appendages found on numerous bacteria and archaea that play essential roles in various microbial functions, including host colonization by pathogens. An ATPase is required for T4P extension, but the
Externí odkaz:
https://doaj.org/article/f4340bd2b5764d8f9b7891913af3b376
Autor:
Ashok R Nayak, Montserrat Samsó
Publikováno v:
eLife, Vol 11 (2022)
Activation of the intracellular Ca2+ channel ryanodine receptor (RyR) triggers a cytosolic Ca2+ surge, while elevated cytosolic Ca2+ inhibits the channel in a negative feedback mechanism. Cryogenic electron microscopy of rabbit RyR1 embedded in nanod
Externí odkaz:
https://doaj.org/article/e5f82544a668419ba6a8f53a24598af8
Publikováno v:
Bio-Protocol, Vol 11, Iss 15 (2021)
High quantities of purified ryanodine receptor (RyR), a large (2.26 MDa) intracellular homotetrameric membrane protein, can be obtained from heterologous expression in HEK293 cells and used for structure determination by cryo-EM. The advantage of usi
Externí odkaz:
https://doaj.org/article/709a1a14f2b8468fa92bd9dbb82b2aea
Autor:
Montserrat Samsó
Publikováno v:
European Journal of Translational Myology, Vol 25, Iss 1, Pp 27-33 (2015)
Excitation contraction coupling, the rapid and massive Ca2+ release under control of an action potential that triggers muscle contraction, takes places at specialized regions of the cell called triad junctions. There, a highly ordered supramolecular
Externí odkaz:
https://doaj.org/article/01ab9ab6a64c46159b5dfc3dbe78724e
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e38594 (2012)
Fluorescent protein (FP) insertions have often been used to localize primary structure elements in mid-resolution 3D cryo electron microscopic (EM) maps of large protein complexes. However, little is known as to the precise spatial relationship betwe
Externí odkaz:
https://doaj.org/article/1c79fb5eebbf495f97e13b4473879c36
Autor:
Alex Perálvarez-Marín, Hanshen Tae, Philip G Board, Marco G Casarotto, Angela F Dulhunty, Montserrat Samsó
Publikováno v:
PLoS ONE, Vol 6, Iss 10, p e25813 (2011)
The type 1 skeletal muscle ryanodine receptor (RyR1) is principally responsible for Ca(2+) release from the sarcoplasmic reticulum and for the subsequent muscle contraction. The RyR1 contains three SPRY domains. SPRY domains are generally known to me
Externí odkaz:
https://doaj.org/article/104ae59be1d54bedb1b53b418169fa2a
Publikováno v:
PLoS Biology, Vol 7, Iss 4, p e85 (2009)
Ryanodine receptor type 1 (RyR1) produces spatially and temporally defined Ca2+ signals in several cell types. How signals received in the cytoplasmic domain are transmitted to the ion gate and how the channel gates are unknown. We used EGTA or neuro
Externí odkaz:
https://doaj.org/article/15e400c4c3c64e069f32f4e78037d9ca
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(30)
Ryanodine receptors (RyRs) are main regulators of intracellular Ca 2+ release and muscle contraction. The Y522S mutation of RyR1 causes central core disease, a weakening myopathy, and malignant hyperthermia, a sudden and potentially fatal response to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42fc9550da19bcddd2e3473ca0a1aa43
https://pubmed.ncbi.nlm.nih.gov/35867837
https://pubmed.ncbi.nlm.nih.gov/35867837