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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, 07/2019, Volume 116, Issue 31, pp. 15540 - 15549
Journal Article
Science Signaling, ISSN 1945-0877, 11/2017, Volume 10, Issue 507, p. eaaq0618
How the store-operated channel Orai1 opens and the number of gates that control channel opening and conductance remain unclear. In this issue of Science... 
CHANNELS | STIM1 | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | Stromal Interaction Molecule 1 | ORAI1 Protein - chemistry | Calcium - chemistry | Ion Channel Gating | Humans | Neoplasm Proteins | Orai1 protein | Calcium channels
Journal Article
CELL, ISSN 0092-8674, 10/2002, Volume 111, Issue 2, pp. 231 - 239
Journal Article
Journal of Neuroscience, ISSN 0270-6474, 07/2016, Volume 36, Issue 29, pp. 7727 - 7739
Journal Article
Nature, ISSN 0028-0836, 09/2017, Volume 549, Issue 7670, pp. 60 - 65
AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid)-subtype ionotropic glutamate receptors mediate fast excitatory neurotransmission throughout... 
ELECTRON CRYOMICROSCOPY | ACTIVATION | ACID | TERMINAL DOMAIN | CRYOELECTRON MICROSCOPY | CRYSTAL-STRUCTURE | DESENSITIZATION | MULTIDISCIPLINARY SCIENCES | SEIZURE CONTROL | MEMBRANE-PROTEINS | HIPPOCAMPAL-NEURONS | Calcium Channels - metabolism | Humans | Protein Subunits - agonists | Receptors, AMPA - chemistry | Models, Molecular | Rats | Receptors, AMPA - ultrastructure | Protein Subunits - metabolism | Synaptic Transmission | Cryoelectron Microscopy | Animals | Claudins - metabolism | Receptors, AMPA - agonists | HEK293 Cells | Hydrophobic and Hydrophilic Interactions | Protein Conformation | Mice | Protein Subunits - antagonists & inhibitors | Protein Subunits - chemistry | Ion Channel Gating | Receptors, AMPA - antagonists & inhibitors | Physiological aspects | Glutamate | Neural transmission | Channel opening | Membranes | Desensitization | Synaptic strength | Glutamic acid receptors (ionotropic) | Channel gating | Propionic acid | Central nervous system | Ions | Glutamic acid receptors | Selectivity | Hydrophobicity | Electron microscopy | α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors | Neurological diseases | Proteins | Signal transduction | Signaling | Receptors | Neurotransmitters | Transmission electron microscopy | α-Amino-3-hydroxy-5-methyl-4-isoxazole propionic acid | Ion channels | Neurotransmission
Journal Article
Cell, ISSN 0092-8674, 10/2014, Volume 159, Issue 3, pp. 608 - 622
The Ca -free form of calmodulin (apoCaM) often appears inert, modulating target molecules only upon conversion to its Ca -bound form. This schema has appeared... 
CA(V)1.3 CHANNELS | PROTEIN INTERACTIONS | CRYSTAL-STRUCTURE | SODIUM-CHANNELS | CALMODULIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | DEPENDENT CALCIUM-CHANNEL | MIDBRAIN DOPAMINE NEURONS | CA2+-DEPENDENT INACTIVATION | FUNCTIONAL-PROPERTIES | PARKINSONS-DISEASE | CELL BIOLOGY
Journal Article
Acta Physiologica, ISSN 1748-1708, 02/2019, Volume 225, Issue 2, pp. e13240 - n/a
Journal Article