Bibliografías temáticas / NSC87877

Literatura académica sobre el tema "NSC87877"

Autor: Grafiati
Publicado: 11 de septiembre de 2023

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Artículos de revistas sobre el tema "NSC87877"

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Raghav, Pawan Kumar, Ajay Kumar Singh y Gurudutta Gangenahalli. "Stem cell factor and NSC87877 synergism enhances c-Kit mediated proliferation of human erythroid cells". Life Sciences 214 (diciembre de 2018): 84–97. http://dx.doi.org/10.1016/j.lfs.2018.09.055.

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Raghav, Pawan Kumar, Ajay Kumar Singh y Gurudutta Gangenahalli. "Stem cell factor and NSC87877 combine to enhance c-Kit mediated proliferation of human megakaryoblastic cells". PLOS ONE 13, n.º 11 (2 de noviembre de 2018): e0206364. http://dx.doi.org/10.1371/journal.pone.0206364.

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Raghav, Pawan Kumar, Ajay Kumar Singh y Gurudutta Gangenahalli. "Correction: Stem cell factor and NSC87877 combine to enhance c-Kit mediated proliferation of human megakaryoblastic cells". PLOS ONE 13, n.º 12 (28 de diciembre de 2018): e0210133. http://dx.doi.org/10.1371/journal.pone.0210133.

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Jalsrai, Aldarmaa, Tadahiro Numakawa, Yoshiko Ooshima, Naoki Adachi y Hiroshi Kunugi. "Phosphatase-Mediated Intracellular Signaling Contributes to Neuroprotection by Flavonoids of Iris tenuifolia". American Journal of Chinese Medicine 42, n.º 01 (enero de 2014): 119–30. http://dx.doi.org/10.1142/s0192415x14500086.

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A variety of flavonoids are suggested to be useful for the treatment of brain-related disorders, including dementia and depression. An investigation on the characteristics of the extracted compounds of Iris tenuifolia Pall. (IT) is of much interest, as this plant has been used as a traditional medicine. In the present study, we examined the effect of total flavonoids obtained from IT on cultured cortical neurons under oxidative-stress and found that pretreatment with IT flavonoids significantly inhibited H 2 O 2-induced cell death in cortical neurons. Such a survival-promoting effect by IT flavonoids was partially blocked by inhibitors for extracellular signal-regulated kinase (ERK) and phosphoinositide 3-kinase/Akt (PI3K/Akt) cascades, both of which are known as survival-promoting signaling molecules. Furthermore, the phosphorylation of Src homology-2 (SH2) domain-containing phosphatase2 (Shp2) was induced by IT flavonoids, and the protective effect of IT flavonoids was abolished by NSC87877, an inhibitor for Shp2, suggesting the involvement of Shp2-mediated intracellular signaling in flavonoid-dependent neuroprotection.
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5

Kim, Soo Hyeon, Young-Rak Cho, Hyeon-Ju Kim, Joa Sub Oh, Eun-Kyung Ahn, Hye-Jin Ko, Byung Joon Hwang et al. "Antagonism of VEGF-A–induced increase in vascular permeability by an integrin α3β1-Shp-1-cAMP/PKA pathway". Blood 120, n.º 24 (6 de diciembre de 2012): 4892–902. http://dx.doi.org/10.1182/blood-2012-05-428243.

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Abstract In cancer, VEGF-induced increase in vascular permeability results in increased interstitial pressure, reducing perfusion and increasing hypoxia, which reduce delivery of chemotherapeutic agents and increase resistance to ionizing radiation. Here, we show that both TIMP-2 and Ala + TIMP-2, a TIMP-2 mutant without matrix metalloproteinase inhibitory activity, antagonize the VEGF-A–induced increase in vascular permeability, both in vitro and in vivo. Like other agents known to preserve endothelial barrier function, TIMP-2 elevates cytosolic levels of cAMP and increases cytoskeletal-associated vascular endothelial cadherin in human microvascular endothelial cells. All of these effects are completely ablated by selective knockdown of integrin α3β1 expression, expression of a dominant negative protein tyrosine phosphatase Shp-1 mutant, administration of the protein tyrosine phosphatase inhibitor orthovanadate, or the adenylate cyclase inhibitor SQ22536. This TIMP-2–mediated inhibition of vascular permeability involves an integrin α3β1-Shp-1-cAMP/protein kinase A-dependent vascular endothelial cadherin cytoskeletal association, as evidenced by using siRNAs to integrin α3β1 and Shp-1, or treatment with Shp-1 inhibitor NSC87877 and protein kinase A inhibitor H89. Our results demonstrate the potential utility for TIMP-2 in cancer therapy through “normalization” of vascular permeability in addition to previously described antiangiogenic effects.
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Klebanovych, Sládková, Sulimenko, Vosecká, Čapek, Dráberová, Dráber y Sulimenko. "Regulation of Microtubule Nucleation in Mouse Bone Marrow-Derived Mast Cells by Protein Tyrosine Phosphatase SHP-1". Cells 8, n.º 4 (11 de abril de 2019): 345. http://dx.doi.org/10.3390/cells8040345.

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The antigen-mediated activation of mast cells initiates signaling events leading to their degranulation, to the release of inflammatory mediators, and to the synthesis of cytokines and chemokines. Although rapid and transient microtubule reorganization during activation has been described, the molecular mechanisms that control their rearrangement are largely unknown. Microtubule nucleation is mediated by γ-tubulin complexes. In this study, we report on the regulation of microtubule nucleation in bone marrow-derived mast cells (BMMCs) by Src homology 2 (SH2) domain-containing protein tyrosine phosphatase 1 (SHP-1; Ptpn6). Reciprocal immunoprecipitation experiments and pull-down assays revealed that SHP-1 is present in complexes containing γ-tubulin complex proteins and protein tyrosine kinase Syk. Microtubule regrowth experiments in cells with deleted SHP-1 showed a stimulation of microtubule nucleation, and phenotypic rescue experiments confirmed that SHP-1 represents a negative regulator of microtubule nucleation in BMMCs. Moreover, the inhibition of the SHP-1 activity by inhibitors TPI-1 and NSC87877 also augmented microtubule nucleation. The regulation was due to changes in γ-tubulin accumulation. Further experiments with antigen-activated cells showed that the deletion of SHP-1 stimulated the generation of microtubule protrusions, the activity of Syk kinase, and degranulation. Our data suggest a novel mechanism for the suppression of microtubule formation in the later stages of mast cell activation.
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DRABER, Pavel, Anastasiya Klebanovych, Vladimira Sladkova, Tetyana Sulimenko, Vera Vosecka, Zuzana Rubikova, Eduarda Draberova y Vadym Sulimenko. "Protein tyrosine phosphatase SHP-1 modulates microtubule organization in later stages of mast cell activation". Journal of Immunology 204, n.º 1_Supplement (1 de mayo de 2020): 152.16. http://dx.doi.org/10.4049/jimmunol.204.supp.152.16.

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Abstract Antigen-mediated activation of mast cells initiates signaling events leading to degranulation and release of inflammatory mediators. Although rapid and transient microtubule reorganization during activation has been described, the molecular mechanisms that control their rearrangement are largely unknown. Important role in microtubule nucleation from centrosomes play γ-tubulin complexes. Here we report on the regulation of microtubule organization in bone marrow-derived mast cells (BMMCs) by Src homology 2 (SH2) domain-containing protein tyrosine phosphatase 1 (SHP-1). Reciprocal immunoprecipitation experiments revealed that SHP-1 is present in complexes containing γ-tubulin complex proteins and protein tyrosine kinase Syk. Pull-down experiments with truncated forms of γ-tubulin and SHP-1 unveiled corresponding interaction domains. When compared to controls, activated BMMCs without SHP-1 had more protrusions containing microtubules, higher level of tyrosine phosphorylation, enhanced activity of Syk kinase, as well as increased expression of cytokines and prostaglandins. Intracellular calcium mobilization and degranulation also increased. Microtubule regrowth experiments in cells lacking SHP-1 revealed stimulation of microtubule nucleation, and phenotypic rescue experiments confirmed that SHP-1 represents a negative regulator of microtubule nucleation in BMMCs. Moreover, inhibition of the SHP-1 activity by inhibitors TPI-1 and NSC87877 also augmented microtubule nucleation. The regulation was due to changes of γ-tubulin accumulation in centrosomes. Our data suggest a novel SHP-1 dependent mechanism for the suppression of microtubule formation in later stages of mast cell activation.
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Tesis sobre el tema "NSC87877"

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BHARTI, SAUMYA. "IN-SILICO APPROACH TO DESIGN A NOVEL INHIBITOR OF SHP1/2:ENHANCEMENT OF HSCS PROLIFERATION". Thesis, 2016. http://dspace.dtu.ac.in:8080/jspui/handle/repository/15366.

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Hematopoiesis is a lifelong process of the production and maintenance of all the cells of the blood system from the hematopoietic stem cells (HSCs) in a hierarchical manner. In adult mammals the hematopoietic stem cells (HSCs) reside in the bone marrow cavity. HSCs give rise to all the types of blood cells of the lymphoid and myeloid lineages. Radiation therapy in cancer leads to loss of a large number of immune cells, so HSCs are transplanted into the bone marrow of irradiated patients but HSCs differentiate before reaching the bone marrow, so the main aim is to maintain the HSCs in their proliferative state until they reach bone marrow. HSCs have three main characteristics of proliferation, self- renewal and differentiation. The proliferative property of HSCs is regulated by a number of signaling pathways, ligands and molecules, but one of the main regulators is the c-kit/SCF signaling. The binding of the SCF (Stem Cell Factor) to the c-kit receptor results in receptor dimerization, thereby activating c-kit activity. Src homology 2 (SH2) domain containing phosphatase 1 (SHP1) negatively regulates the c-kit activity. Hence in this work we have identified the structural variations using structural alignment between the PTPases and observed that HePTP is having high identity with SHP1. Based on this result we have screened known inhibitors of HePTP against SHP1 and identified some ligands having higher binding affinity than NSC87877. In order to design SHP1 specific inhibitor a pharmacophore model was designed to search for a NCE (Novel Chemical Entity).
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