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10.1111/jcmm.12989 http://scihub22266oqcxt.onion/10.1111/jcmm.12989 C5323820!5323820!27680505     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Cell+Mol+Med 2017 ; 21 (3): 456-66 Nephropedia Template TP {{tp|p=27680505|t=2017. The possible roles of B?cell novel protein?1 (BCNP1) in cellular signalling pathways and in cancer |pdf=|usr=}}{{27680505}} gab.com Text The possible roles of B cell novel protein 1 (BCNP1) in cellular signalling pathways and in cancer JO: J Cell Mol Med http://www.kidney.de/pget.php?&tw=1&pmid=27680505 #FOAvip B?cell novel protein?1 (BCNP1) or Family member of 129C (FAM129C) was identified as a B?cell?specific plasma?membrane protein. Bioinformatics analysis predicted that BCNP1 might be heavily phosphorylated. The BCNP1 protein contains a pleckstrin homology (PH) domain, two proline?rich (PR) regions and a Leucine Zipper (LZ) domain suggesting that it may be involved in protein?protein interactions. Using The Cancer Genome Atlas (TCGA) data sets, we investigated the correlation of alteration of the BCNP1 copy?number changes and mutations in several cancer types. We also investigated the function of BCNP1 in cellular signalling pathways. We found that BCNP1 is highly altered in some types of cancers and that BCNP1 copy?number changes and mutations co?occur with other molecular alteration events for TP53 (tumour protein P53), PIK3CA (Phosphatidylinositol?4,5?Bisphosphate 3?Kinase, Catalytic Subunit Alpha), MAPK1 (mitogen?activated protein kinase?1; ERK: extracellular signal regulated kinase), KRAS (Kirsten rat sarcoma viral oncogene homolog) and AKT2 (V?Akt Murine Thymoma Viral Oncogene Homolog 2). We also found that PI3K (Phoshoinositide 3?kinase) inhibition and p38 MAPK (p38 mitogen?activated protein kinase) activation leads to reduction in phosphorylation of BCNP1 at serine residues, suggesting that BCNP1 phosphorylation is PI3K and p38MAPK dependent and that it might be involved in cancer. Its degradation depends on a proteasome?mediated pathway. Twit Text FOAVip The possible roles of B cell novel protein 1 (BCNP1) in cellular signalling pathways and in cancer ????J Cell Mol Med http://www.kidney.de/pget.php?&tw=1&pmid=27680505 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27680505 #FOAvip English Wikipedia <ref>{{Cite pmid|27680505}}</ref> The possible roles of B?cell novel protein?1 (BCNP1) in cellular signalling pathways and in cancer #MMPMID27680505 Patel SJ; Trivedi GL; Darie CC; Clarkson BD J Cell Mol Med 2017[Mar]; 21 (3): 456-66 PMID27680505show ga B?cell novel protein?1 (BCNP1) or Family member of 129C (FAM129C) was identified as a B?cell?specific plasma?membrane protein. Bioinformatics analysis predicted that BCNP1 might be heavily phosphorylated. The BCNP1 protein contains a pleckstrin homology (PH) domain, two proline?rich (PR) regions and a Leucine Zipper (LZ) domain suggesting that it may be involved in protein?protein interactions. Using The Cancer Genome Atlas (TCGA) data sets, we investigated the correlation of alteration of the BCNP1 copy?number changes and mutations in several cancer types. We also investigated the function of BCNP1 in cellular signalling pathways. We found that BCNP1 is highly altered in some types of cancers and that BCNP1 copy?number changes and mutations co?occur with other molecular alteration events for TP53 (tumour protein P53), PIK3CA (Phosphatidylinositol?4,5?Bisphosphate 3?Kinase, Catalytic Subunit Alpha), MAPK1 (mitogen?activated protein kinase?1; ERK: extracellular signal regulated kinase), KRAS (Kirsten rat sarcoma viral oncogene homolog) and AKT2 (V?Akt Murine Thymoma Viral Oncogene Homolog 2). We also found that PI3K (Phoshoinositide 3?kinase) inhibition and p38 MAPK (p38 mitogen?activated protein kinase) activation leads to reduction in phosphorylation of BCNP1 at serine residues, suggesting that BCNP1 phosphorylation is PI3K and p38MAPK dependent and that it might be involved in cancer. Its degradation depends on a proteasome?mediated pathway. äThe possible roles of B?cell novel protein?1 (BCNP1) in cellular signa(epmc).pdf DeepDyve Pubget Overpricing