PIM1 Protein Overview Sequence, Structure, Function and Protein Interaction Sino Biological


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The pim-1 oncogene encodes two related protein-serine/threonine kinases by alternative initiation at AUG and CUG. EMBO J. 10 , 655-664 (1991). Article CAS PubMed PubMed Central Google Scholar


Preparation and characteristics of PIM1 and CPIM1 membranes. (a)... Download Scientific Diagram

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Molecular structure of PIM1 (only repeating unit) and the studied... Download Scientific Diagram

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Use of regulators and inhibitors of Pim1, a serine/threonine kinase, for tumour therapy (Review)

Clinical trials for PIM kinases as biomarkers or targets for drugs are ongoing and will determine their potential in patients with hematologic malignancies or solid tumors ( clinicaltrials.gov; identifiers: NCT02066883, NCT01588548 ); melanoma patients in the future could benefit from such studies.


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PIM1 Protein Overview Sequence, Structure, Function and Protein Interaction Sino Biological

Results: 1 Our investigation showed that Pim-1 is up-regulated in around 15% of acute myeloid leukemia (AML) patients. 2 As shown in growth curves and apoptosis assays, over expression of Pim-1induces growth up-regulation and anti-apoptosis. We hypothesized that phenomenon could be originated from the enhanced expression of c-myc, cyclin D1 and.


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The Proviral Integration of Molony murine leukemia virus (PIM)-1 protein contributes to the solid cancers and hematologic malignancies, cell growth, proliferation, differentiation, migration, and other life activities. Many studies have related these functions to its molecular structure, subcellular localization and expression level..


IR spectra of nanofiltrationsupported PIM1 and PIM1/MOFs membranes. Download Scientific Diagram

The serine threonine kinase Pim-1 has documented roles in hematopoietic progenitor and B cell precursor proliferation and survival. Pim-1 is a molecular target of the transcription factor Hoxa9. Previous studies showed that Pim-1 deficiency phenocopied the hematopoietic progenitor defect in hoxa9-/- mice and forced expression of Pim-1 normalized the in vitro proliferation defect inherent to.


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PIM kinases play a key part in several vital biological processes, such as cell differentiation, cell proliferation, and programmed cell death (apoptosis),in addition to signaling mechanisms associated with tumorigenesis [1], [2].The PIM's name is originated from the original gene PIM-1 which is the moloney murine leukaemia virus's proviral insertion site (PIM) [3], [4].


Figure 5 from PIM 1 kinase as a target for cancer therapy Semantic Scholar

Xie, Y. et al. The 44-kDa Pim-1 kinase phosphorylates BCRP/ABCG2 and thereby promotes its multimerization and drug-resistant activity in human prostate cancer cells. J. Biol. Chem. 283, 3349.


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On the contrary, Pim-1 overexpression can down-regulate E-cadherin, up-regulate vimentin, and increase stem-like characteristics, ultimately. 24,25 In light of the vital roles of Pim1 in tumor progression, it is our believe that Pim-1 maybe a promising candidate biomarker for cancer with great clinical significance.


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Background/aims: Pim-1 is a serine/threonine kinase that is highly expressed in the heart, and exerts potent cardiac protective effects through enhancing survival, proliferation, and regeneration of cardiomyocytes. Its myocardial specific substrates, however, remain unknown. In the present study, we aim to investigate whether Pim-1 modulates myofilament activity through phosphorylation of.


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PIM1 mixed matrix membranes for gas separations using costeffective hypercrosslinked

When overexpressed, pim genes are able to synergize with myc, or gfi-1 oncogenes to promote lymphomagenesis. 12 Interestingly, studies with transgenic mice overexpressing either gfi-1 or pim-1 have revealed that these two genes act in opposite ways in β-selection, which is a critical step in thymocyte differentiation. 22 In addition, gfi-1 and.


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Pim1 kinase as cancer drug target An update (Review)

Therefore, Pim-1 activity prevents Drp1 compartmentalization to the mitochondria and preserves reticular mitochondrial morphology in response to sI. Ischemic heart disease is a leading cause of death in the Western world. Many simultaneous cellular changes occur during cardiac ischemia and inevitably cause cell death.