| the faster migrating Tg adduct C primarily engages the CaBP1/P5 oxidoreductase, whereas the slower migrating Tg adduct A primarily engages ERp72. | Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum.
Di Jeso B, Morishita Y, Treglia AS, Lofrumento DD, Nicolardi G, Beguinot F, Kellogg AP, Arvan P., Free PMC Article | 06/7/2014 |
| Present the NMR structure of full-length CaBP1 with Ca(2+) bound at the first, third, and fourth EF-hands. | Nuclear magnetic resonance structure of calcium-binding protein 1 in a Ca(2+) -bound closed state: implications for target recognition.
Park S, Li C, Ames JB., Free PMC Article | 04/20/2013 |
| Different kinetics of Ca-dependent binding step between caldendrin and calmodulin with AKAP79 suggest their different roles in synaptic function. | Kinetic and mechanistic differences in the interactions between caldendrin and calmodulin with AKAP79 suggest different roles in synaptic function.
Seeger C, Gorny X, Reddy PP, Seidenbecher C, Danielson UH. | 02/2/2013 |
| We demonstrate that calmodulin and caldendrin compete for a partially overlapping binding site on AKAP79 and that their binding is differentially dependent on calcium | AKAP79/150 interacts with the neuronal calcium-binding protein caldendrin.
Gorny X, Mikhaylova M, Seeger C, Reddy PP, Reissner C, Schott BH, Helena Danielson U, Kreutz MR, Seidenbecher C. | 09/29/2012 |
| CaBP1 regulates voltage-dependent inactivation and activation of Ca(V)1.2 (L-type) calcium channels | CaBP1 regulates voltage-dependent inactivation and activation of Ca(V)1.2 (L-type) calcium channels.
Oz S, Tsemakhovich V, Christel CJ, Lee A, Dascal N., Free PMC Article | 07/2/2011 |
| Structural basis for the differential effects of CaBP1 and calmodulin on Ca(V)1.2 calcium-dependent inactivation. | Structural basis for the differential effects of CaBP1 and calmodulin on Ca(V)1.2 calcium-dependent inactivation.
Findeisen F, Minor DL Jr., Free PMC Article | 04/2/2011 |
| CaBP1 may regulate Ca2+-dependent activity of inositol 1,4,5-trisphosphate receptors by promoting structural contacts between the suppressor and core domains | Structural insights into Ca2+-dependent regulation of inositol 1,4,5-trisphosphate receptors by CaBP1.
Li C, Chan J, Haeseleer F, Mikoshiba K, Palczewski K, Ikura M, Ames JB., Free PMC Article | 01/21/2010 |
| the importance of CaBP1s in modulating the stimulus-secretion coupling in excitable cells. | Ca2+ binding protein-1 inhibits Ca2+ currents and exocytosis in bovine chromaffin cells.
Chen ML, Chen YC, Peng IW, Kang RL, Wu MP, Cheng PW, Shih PY, Lu LL, Yang CC, Pan CY. | 01/21/2010 |
| We describe a new role for CaBP1 in regulation of Ca2+ influx through Ca(v)1.2 (L-type) Ca2+ channels. CaBP1 interacts directly with the alpha1 subunit of Ca(v)1.2 at sites that also bind Calmodulin | Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with Cav1.2 (L-type) Ca2+ channels.
Zhou H, Kim SA, Kirk EA, Tippens AL, Sun H, Haeseleer F, Lee A., Free PMC Article | 01/21/2010 |
| CaBP1 is able to specifically regulate InsP3 receptor-mediated alterations in [Ca2+]i during agonist stimulation. | Calcium-binding protein 1 is an inhibitor of agonist-evoked, inositol 1,4,5-trisphosphate-mediated calcium signaling.
Haynes LP, Tepikin AV, Burgoyne RD. | 01/21/2010 |
| the NT and IQ-domains of alpha(1)1.2 mediate functionally distinct interactions with CaBP1 and CaM that promote conformational alterations that either stabilize or inhibit inactivation of Ca(v)1.2. | Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by calmodulin and Ca2+-binding protein-1.
Zhou H, Yu K, McCoy KL, Lee A. | 01/21/2010 |
| NMR, microcalorimetry, and other biophysical studies that characterize Ca(2+) binding, Mg(2+) binding, and structural properties of recombinant CaBP1 are reported. | Structural analysis of Mg2+ and Ca2+ binding to CaBP1, a neuron-specific regulator of calcium channels.
Wingard JN, Chan J, Bosanac I, Haeseleer F, Palczewski K, Ikura M, Ames JB., Free PMC Article | 01/21/2010 |
| enhances inactivation, causes a depolarizing shift in the voltage dependence of activation, and does not support Ca2+-dependent facilitation of Ca(v)2.1 channels | Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-binding protein 1.
Lee A, Westenbroek RE, Haeseleer F, Palczewski K, Scheuer T, Catterall WA., Free PMC Article | 01/21/2010 |