Calcium Channel, Voltage-Dependent, N Type, alpha 1B Subunit (CACNA1B) ELISA Kits

Human Calcium Channel, Voltage-Dependent, N Type, alpha 1B Subunit (CACNA1B) interaction partners

1. CACNA1B protein expressions in tumorous tissues were correlated with NSCLC patients' clinical characteristics and overall survival. CACNA1B mRNA and protein expression levels were higher in NSCLC tumorous tissues than in nontumorous tissues.

2. These results do not support a causal association between the CACNA1B c.4166G>A; (p.R1389H) variant and M-D.

3. the consensus motifs of S-nitrosylation were much more abundant in Cav2.2 than in Cav1.2 (show CACNA1C ELISA Kits) and Cav2.1 (show CACNA1A ELISA Kits).

4. AP-1 (show FOSB ELISA Kits) binding motifs, present only in exon 37a, enhance intracellular trafficking of exon 37a-containing Ca(V)2.2 to the axons and plasma membrane of rat dorsal root ganglia neurons

5. CACNA1B mutation is linked to unique myoclonus-dystonia syndrome.

6. The first disease connection for Cav2.2 channels [review]

7. The interaction between LC1 (show MAP1B ELISA Kits) and the N-type channel (CaV2.2 channel) was demonstrated.

8. with membrane-localized CaV beta subunits, CaV2.2 channels are subject to Gbetagamma-mediated voltage-dependent inhibition, whereas cytosol-localized beta subunits confer more effective PIP2-mediated voltage-independent regulation

9. new mechanistic perspectives, and reveal unexpected variations in determinants, underlying inhibition of Ca(V)1.2 (show CACNA1C ELISA Kits)/Ca(V)2.2 channels by distinct RGK GTPases.

10. Ca(2 (show CA2 ELISA Kits)+) exits the channel through the Cav2.2.

Mouse (Murine) Calcium Channel, Voltage-Dependent, N Type, alpha 1B Subunit (CACNA1B) interaction partners

1. Thus, GHSR1a differentially inhibits CaV2 (show CAV2 ELISA Kits) channels by Gi/o or Gq protein pathways depending on its mode of activation.

2. Blockade of Cav2.2 in inflammatory arthritis leads to up-regulation of the osteoclast activator RANKL (show TNFSF11 ELISA Kits) and concomitant joint and bone destruction.

3. Results identified altered synaptic transmission in the olfactory system of Cav2.2-deficient mice and suggest that the olfactory system could become an attractive model to learn more about this channel and the consequences of its removal

4. Gaba B receptors were found to mediate Cav2.2 channel inhibition.

5. Cav2.1 (show CACNA1A ELISA Kits)-2.3 have unique contributions to the dynamics at the Schaffer collateral synapse that are engaged by the complex patterns of afferent activity seen in vivo

6. Results demonstrate that sensory neurons from Nf1 (show NF1 ELISA Kits)+/- mice, exhibit increased N-type (Cav2.2) ICa (show ICA ELISA Kits) and likely account for the increased release of substance P (show TAC1 ELISA Kits) and calcitonin gene-related peptide (show CALCA ELISA Kits) that occurs in Nf1 (show NF1 ELISA Kits)+/- sensory neurons

7. data suggest that the different roles that Ca(V)2.1 (show CACNA1A ELISA Kits) and Ca(V)2.2 play in MNC secretion may be a result of the different levels of expression of Ca(V)2.1 (show CACNA1A ELISA Kits) in VP and OT MNCs

8. CaV2.2 and alpha2delta-1 are intimately associated at the plasma membrane

9. These findings identify an interaction between ankyrin-B (show ANK2 ELISA Kits) and both Cav2.1 (show CACNA1A ELISA Kits) and Cav2.2 at the amino acid level that is necessary for proper Cav2.1 (show CACNA1A ELISA Kits) and Cav2.2 targeting in vivo.

10. Blocking Cav2.2 channels abolishes respiratory activity in all brainstem slices from Cav2.1 (show CACNA1A ELISA Kits) genetically ablated animals.

Rabbit Calcium Channel, Voltage-Dependent, N Type, alpha 1B Subunit (CACNA1B) interaction partners

1. these results unveil a novel functional coupling between Parkin (show PARK2 ELISA Kits) and the CaV2.2 channels

2. The CaVbeta Subunit Protects the I-II Loop of the Voltage-gated Calcium Channel CaV2.2 from Proteasomal Degradation but Not Oligoubiquitination.

3. The monomeric G proteins AGS1 (show RASD1 ELISA Kits) and Rhes selectively influence Galphai-dependent signaling to modulate N-type (CaV2.2) calcium channels.