User profiles for Montserrat Samso
 | Montserrat SamsoAssociate Professor, Virginia Commonwealth University Verified email at vcu.edu Cited by 2646 |
Internal structure and visualization of transmembrane domains of the RyR1 calcium release channel by cryo-EM
RyR1 is an intracellular calcium channel with a central role in muscle contraction. We
obtained a three-dimensional reconstruction of the RyR1 in the closed state at a nominal …
obtained a three-dimensional reconstruction of the RyR1 in the closed state at a nominal …
[HTML][HTML] Coordinated movement of cytoplasmic and transmembrane domains of RyR1 upon gating
Ryanodine receptor type 1 (RyR1) produces spatially and temporally defined Ca 2+ signals
in several cell types. How signals received in the cytoplasmic domain are transmitted to the …
in several cell types. How signals received in the cytoplasmic domain are transmitted to the …
Structural mechanism of two gain-of-function cardiac and skeletal RyR mutations at an equivalent site by cryo-EM
Mutations in ryanodine receptors (RyRs), intracellular Ca 2+ channels, are associated with
deadly disorders. Despite abundant functional studies, the molecular mechanism of RyR …
deadly disorders. Despite abundant functional studies, the molecular mechanism of RyR …
Membrane proteins: the 'Wild West'of structural biology
J Torres, TJ Stevens, M Samsó - Trends in biochemical sciences, 2003 - cell.com
Historically, the task of determining the structure of membrane proteins has been hindered
by experimental difficulties associated with their lipid-embedded domains. Here, we provide …
by experimental difficulties associated with their lipid-embedded domains. Here, we provide …
Structural characterization of a dynein motor domain
Cytoplasmic dynein is a microtubule-based mechanochemical protein that plays an essential
role in cell division, vesicle transport, and cytoplasmic membrane organization. As a …
role in cell division, vesicle transport, and cytoplasmic membrane organization. As a …
[HTML][HTML] Apocalmodulin and Ca2+-calmodulin bind to neighboring locations on the ryanodine receptor
M Samsó, T Wagenknecht - Journal of Biological Chemistry, 2002 - ASBMB
Calmodulin (CaM) binds to the ryanodine receptor/calcium release channel of skeletal
muscle (RyR1), both in the absence and presence of Ca 2+ , and regulates the activity of the …
muscle (RyR1), both in the absence and presence of Ca 2+ , and regulates the activity of the …
A guide to the 3D structure of the ryanodine receptor type 1 by cryoEM
M Samsó - Protein Science, 2017 - Wiley Online Library
Signal transduction by the ryanodine receptor (RyR) is essential in many excitable cells
including all striated contractile cells and some types of neurons. While its transmembrane …
including all striated contractile cells and some types of neurons. While its transmembrane …
[PDF][PDF] Three-dimensional reconstruction of ryanodine receptors
T Wagenknecht, M Samsó - Front Biosci, 2002 - researchgate.net
… Terence Wagenknecht1,2 and Montserrat Samsó 1 … Samso, M. & Wagenknecht,T.
Contributions of electron microscopy and single-particle techniques to the determination of the …
Contributions of electron microscopy and single-particle techniques to the determination of the …
Enhanced excitation-coupled calcium entry in myotubes expressing malignant hyperthermia mutation R163C is attenuated by dantrolene
…, W Feng, E Cabrales, L Michaelson, M Samso… - Molecular …, 2008 - ASPET
Dantrolene is the drug of choice for the treatment of malignant hyperthermia (MH) and is
also useful for treatment of spasticity or muscle spasms associated with several clinical …
also useful for treatment of spasticity or muscle spasms associated with several clinical …
Structural characterization of the RyR1–FKBP12 interaction
The 12kDa FK506-binding protein (FKBP12) constitutively binds to the calcium release
channel RyR1. Removal of FKBP12 using FK506 or rapamycin causes an increased open …
channel RyR1. Removal of FKBP12 using FK506 or rapamycin causes an increased open …