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Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Zusätzlich bieten wir Ihnen Ribosomal Protein L22 Antikörper (64) und viele weitere Produktgruppen zu diesem Protein an.
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Casein kinase II (zeige CSNK2A1 Proteine) binds and phosphorylates ribosomal protein L22
RpL22 is essential for transcriptional gene repression
considering the high mutation frequency found, our data point toward an important role for RPL22 in microsatellite instability carcinogenesis
Study revealved that RPL22 binds CK2alpha in lung cancer cells.
Down-regulation of RPL22 might be involved in the carcinogenesis of NSCLC.
RPL22 is frequently mutated in MSI (zeige MSI1 Proteine)-high endometrioid endometrial cancers. The A8 mutation identified was not reported in the whole exome sequences analyzed by the TCGA.
Rpl22 inactivation promotes neoplastic transformation by inducing expression of Lin28B (zeige LIN28B Proteine)
Multiple domains of EBER 1 recruit ribosomal protein L22.
The EBER-ISH (zeige ANTXR2 Proteine) as an independent prognostic factor of NPC (zeige NPC1 Proteine) regardless of histopathology.
Growth-promoting properties of Epstein-Barr virus EBER-1 RNA correlate with ribosomal protein L22 binding
Rpl22, and its highly homologous paralog Rpl22-Like1 (Rpl22l1 or Like1) play critical, extraribosomal roles in embryogenesis.
finding that Rpl22 deficiency exacerbates endoplasmic reticulum stress responses and induces p53 (zeige TP53 Proteine) in alphabeta T cell progenitors provides insight into how a ubiquitously expressed RP can perform regulatory functions that are selectively required by some cell lineages but not others
RPL22 underexpression is associated with Dissemination of T-cell Lymphoma.
Rpl22 performs a critical, developmentally restricted role in supporting early B cell development by preventing p53 (zeige TP53 Proteine) induction.
either ribosomal protein can support translation, knockdown of Rpl22l1 impairs growth of cells lacking Rpl22. Mechanistically, Rpl22 regulates Rpl22l1 directly by binding to an internal hairpin structure and repressing its expression
Investigation of downstream effectors used by tumor protein p53 (zeige TP53 Proteine) to impair T cell lineage development finds many p53 (zeige TP53 Proteine) targets are induced in Rpl22-deficient thymocytes, including miR (zeige MLXIP Proteine)-34a, PUMA (zeige BBC3 Proteine), p21waf, Bax (zeige BAX Proteine), and Noxa (zeige PMAIP1 Proteine).
Rpl22 deficiency activated a p53 (zeige TP53 Proteine)-dependent checkpoint that produced a remarkably selective block in alphabeta T cell development.
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a cytoplasmic ribosomal protein that is a component of the 60S subunit. The protein belongs to the L22E family of ribosomal proteins. Its initiating methionine residue is post-translationally removed. The protein can bind specifically to Epstein-Barr virus-encoded RNAs (EBERs) 1 and 2. The mouse protein has been shown to be capable of binding to heparin. Transcript variants utilizing alternative polyA signals exist. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. It was previously thought that this gene mapped to 3q26 and that it was fused to the acute myeloid leukemia 1 (AML1) gene located at 21q22 in some therapy-related myelodysplastic syndrome patients with 3\;21 translocations\; however, these fusions actually involve a ribosomal protein L22 pseudogene located at 3q26, and this gene actually maps to 1p36.3-p36.2.
, PARP-binding protein-12
, ribosomal protein L22
, 60S ribosomal protein L22
, heparin-binding protein HBp15
, EBER-associated protein
, Epstein-Barr virus small RNA-associated protein
, Epstein-Barr-encoded RNA-associated protein
, heparin-binding protein 15
, ribosomal protein homologue to human L22