NCS1 Antibody

1. NCS-1, a calcium-binding protein, is associated with clinicopathologic features of aggressiveness in breast cancer cells and worse outcome in two breast cancer patient cohorts PMID: 28275088
2. Results show that although NCS-1 Var2mRNA can be detected, protein expression was not detectable. When overexpressed in cell lines NCS-1 Var2 appears to be folded properly, yet it has a lower calcium affinity. Because most NCS-1 binding to its protein partners requires calcium binding, it is unlikely that NCS-1 Var2 would play a major regulatory role in cells. PMID: 27575489
3. structural and dynamical response of NCS-1 protein to elevated temperature may be one of its intrinsic functional properties PMID: 27007011
4. Lithium normalizes gamma band oscillations mediated by P/Q-type calcium channels modulated by NCS-1. PMID: 27033453
5. Study determined the salient features of the folding free-energy landscapes of the Mg2+-bound and apo states of NCS-1 PMID: 26153708
6. results reveal the important role of salt bridges on the structural properties of NCS-1 protein and that R102Q mutation disables the dynamic relocation of C-terminus, which may block the binding of NCS-1 protein to its receptors PMID: 25343687
7. single-molecule optical tweezers were used to monitor misfolding reactions of the human neuronal calcium sensor-1. PMID: 25157171
8. A strong liason was characterized between myristoylation and cryptic EF-1 in NCS-1. PMID: 25565019
9. The functional link in substantia nigra dopamine neurons between Cav1.3- L-type-Ca2+ channels and D2-autoreceptor activity is an adaptive signalling network controlled by NCS-1. PMID: 24934288
10. NCS1 has evolved a remarkable complex interdomain cooperativity and a fundamentally different folding mechanism compared to structurally related proteins. PMID: 24012477
11. data suggest that genetic variants in the NCS-1 gene contribute to susceptibility of Cocaine Abuse in individuals of African descent. PMID: 22999924
12. [review] Receptor interaction properties in schizophrenia are dependent upon NCS-1, a protein found to regulate the phosphorylation, trafficking, and signaling profile of the D2 dopamine receptor (D2R) in neurons. PMID: 21777187
13. the C-terminal tail is important for regulating the conformational stability of NCS1 in Ca(2+)-activated state PMID: 22227393
14. analysis of the interaction between the D2 dopamine receptor and neuronal calcium sensor-1 PMID: 21875085
15. it is possible to protect cells from paclitaxel-induced degradation of NCS-1 by inhibiting calpain activity PMID: 21808066
16. NCS-1 is a novel regulator of cardiac calcium signaling, specifically in immature and hypertrophic hearts. PMID: 21737792
17. Impairment of the normal cycling of NCS-1 by the R102Q mutation could have subtle effects on neuronal signalling and physiology in the developing and adult brain. PMID: 20479890
18. up-regulated in the prefrontal cortex of schizophrenic and bipolar patients PMID: 12496348
19. Analysis with chimeric proteins between KChIP2 and NCS-1 reveals that the three regions of KChIP2 are necessary and sufficient for its effective binding to Kv4.3 protein PMID: 12928444
20. may serve as regulator of certain isoforms of phosphatidylinositol 4-kinase PMID: 14512421
21. key role for residues within the motif EELTRK in NCS-1 in keeping the myristoyl group exposed and allowing the protein to be constitutively membrane-associated. PMID: 14726528
22. NCS-1 is shown to be mainly associated with azurophilic granules in human neutrophils and promyelocitic cells and, therefore could play an instrumental role in the calcium-dependent secretion of azurophilic granules PMID: 14760944
23. These results demonstrate a novel role for NCS-1 and PI4Kbeta in regulating ERK1/2 signaling and inflammatory reactions in mast cells. PMID: 16837555
24. NCS-1 expression was diminished in CD4+T lymphocytes, CD19+ B lymphocytes and CD14+ monocytes of bipolar disorder patients and also decreased in CD4+ T lymphocytes and CD56+ natural killer cells of schizophrenia patients PMID: 19091302
25. occurrence of an unusual TG 3' splice site in intron 2 PMID: 17672918

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HGNC: 3953

OMIM: 603315

KEGG: hsa:23413

STRING: 9606.ENSP00000361475

UniGene: Hs.642946