... , Authors: Atsuhiro Tanabe, Maho Saito. Published in: Atlas Genet Cytogenet Oncol Haematol.
The mitogen-activated protein kinase-activated protein kinase MK5 is a substrate of the mitogen-activated protein kinases p38, ERK3 and ERK4. Cell culture and animal studies have demonstrated that MK5 is involved in tumour suppression and promotion, embryogenesis, anxiety, cell motility and cell cycle regulation. In the present study, homology models of MK5 were used for molecular dynamics (MD) simulations of: (1) MK5 alone; (2) MK5 in complex with an inhibitor; and (3) MK5 in complex with the interaction partner p38α. The calculations showed that the inhibitor occupied the active site and disrupted the intramolecular network of amino acids. However, intramolecular interactions consistent with an inactive protein kinase fold were not formed. MD with p38α showed that not only the p38 docking region, but also amino acids in the activation segment, αH helix, P-loop, regulatory phosphorylation region and the C-terminal of MK5 may be involved in forming a very stable MK5-p38α complex, and that p38α
Background: Although suicide is a leading cause of death in the United States and represents a significant public health threat, little is known about the neurobiological or molecular factors that contribute to its pathophysiology. A number of studies now indicate that lithium has considerable efficacy in the prevention of suicide in patients with affective disorders, and accumulating evidence indicates that protein kinase C (PKC) and its substrates, in particular the myristoylated alanine-rich C kinase substrate (MARCKS), are primary targets of chronic lithium treatment. We therefore hypothesized that a dysregulation in MARCKS expression in key brain regions could contribute to the pathophysiology associated with suicide. To address this, we examined MARCKS, as well as the closely related MARCKS-related protein (MRP), mRNA expression in the hippocampus and dorsolateral prefrontal cortex of suicide victims and normal controls. Method: MARCKS and MRP mRNA expression was assessed by quantitative ...
MARCKS (myristoylated alanine-rich C kinase substrate) is a major cytoskeletal protein substrate of PKC (protein kinase C) whose cellular functions are still unclear. However numerous studies have implicated MARCKS in the stabilization of cytoskeletal structures during cell differentiation. The present study was performed to investigate the potential role of Ca2+-dependent proteinases (calpains) during myogenesis via proteolysis of MARCKS. It was first demonstrated that MARCKS is a calpain substrate in vitro. Then, the subcellular expression of MARCKS was examined during the myogenesis process. Under such conditions, there was a significant decrease in MARCKS expression associated with the appearance of a 55 kDa proteolytic fragment at the time of intense fusion. The addition of calpastatin peptide, a specific calpain inhibitor, induced a significant decrease in the appearance of this fragment. Interestingly, MARCKS proteolysis was dependent of its phosphorylation by the conventional PKCα. ...
Protein kinases have become central in the efforts to understand the nature of various diseases, and a lot is invested into creating effective therapeutic strategies and finding effective and selective protein kinase inhibitors. In order to succeed it is also important to focus on the structure of the kinases, their exact biological role, and how they interact and cooperate in the signaling. The exact structure of MAPKAPK5 is still unknown, and selective inhibitors are yet to be identified. Even though some of its biological roles are starting to emerge more work is required, including searching for selective inhibitors, analyzing its structure and interactions with its interaction partners. In order to analyze the structure of MAPKAPK5, homology models were generated and their ability to discriminate between binders and non-binders were analyzed. Based on the results, one model was found satisfactory and may be used as a working tool for further experimental studies and possibly structure aided ...
Following denervation skeletal muscles change their functional and structural properties. Some changes resemble conditions in developing muscles and may be important for reinnervation. Due to inactivity following denervation most skeletal muscles loose muscle mass and become atrophic. The hemidiaphragm muscle, however, undergoes a phase of transient hypertrophy following denervation, gaining weight during the first 6-10 days followed by a decrease in weight. In this thesis the expression (mRNA, protein and protein phosphorylations) of potential factors involved in the regulation of muscle mass were examined in denervated hind-limb and hemidiaphragm muscles.. NIFK is a protein that associates with Ki67, a protein expressed predominantly in proliferating cells. The mRNA expression of NIFK was upregulated in denervated atrophic muscles but unaltered in denervated hypertrophic muscles, suggesting a potential role in the regulation of skeletal muscle mass (Paper I). p38 MAPK has previously been ...
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The contribution of linked background genes to the phenotype of mutant mice has been documented (7) as have the significant behavioral differences between inbred mouse strains (6). The 129Sv strain used in the generation of our mutant mice exhibit IP-MF hypoplasia (2) and impaired spatial learning in the Morris water maze (6). In our study, comparison of 129B6(N3) mice, which posses on average 12.5% residual 129Sv-linked genes; 129B6(N9) mice, which posses on average 0.2% residual 129Sv-linked genes; and inbred C57BL/6J mice, which possess no 129Sv-linked genes, revealed the significant contribution of 129Sv background genes to the phenotype. First, mutant 129B6(N3) mice, but not mutant 129B6(N9) mice, exhibited a significant elevation in hippocampal PKCɛ expression relative to wild-type controls. Second, wild-type 129B6(N3) mice exhibited significant IP-MF hypoplasia relative to both inbred C57BL/6J and wild-type 129B6(N9) mice, which is consistent with the 129Sv phenotype (2), and likely ...
In a differential gene experiment, a cell perturbation can be measured on a microarray before and after the perturbation. The information from these microarrays can then be used to inference genetic pathways and protein-protein interaction networks. In this paper we reverse this idea somewhat and measure a cell perturbation through microarrays and then rely on a protein interaction map to assess which proteins are most likely influenced by the specific perturbation. This in turn helps to elucidate the functional effect the perturbation has on the cell system. The first part of the paper focuses on the propagation model we developed to obtain this information. The second part of the paper reports on a specific experiment that was driven by the interpretation we obtained through such a gene influence network. We applied a PC12 cell line that allows doxocyclin-dependent expression of constitutive active mitogen-activated protein kinase-activated protein kinase (MAPKAPK5 or MK5) to compare the
Materials. CEP-1347, also known as KT7515, is a semisynthetic derivative of K-252a provided by Kyowa-Hakko Kogyo (Tokyo, Japan) (Kaneko et al., 1997). CEP-1347 was dissolved in cell culture grade dimethylsulfoxide (DMSO) and stored in the dark at 4°C. All dilutions of CEP-1347 were made in DMEM containing 1% bovine serum albumin. c-Jun N-terminal kinase 1 (JNK1) antibody (catalog #sc-474-G) was purchased from Santa Cruz Biotechnology (Santa Cruz, CA). ERK1 antibody (catalog #06-182), mitogen-activated protein kinase-activated protein kinase 2 (MAPKAP2) antibody (catalog #06-534), and MAPKAP2 peptide substrate (catalog #12-240) were purchased from Upstate Biotechnology (Lake Placid, NY). HA antibody was purchased from Babco (Richmond, CA). AP-1 (c-jun) substrate was purchased from Promega (Madison, WI). Myelin basic protein substrate, Hoechst dye, and tunicamycin were purchased from Sigma (St. Louis, MO). SB203580 was custom-synthesized by RIT International Technology (Snellville, GA). ...
PRAK antibody [N3C3] (mitogen-activated protein kinase-activated protein kinase 5) for ICC/IF, WB. Anti-PRAK pAb (GTX107938) is tested in Human samples. 100% Ab-Assurance.
View mouse Mapkapk5 Chr5:121525038-121545905 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
MAP kinase-activated protein kinase 2 (MAPKAPK2) is an enzyme that in humans is encoded by the MAPKAPK2 gene. MAPKAP kinase-2 (MK2) is originally identified by its phosphorylation of glycogen synthase at serine-7 and the corresponding serine in a peptide (GS peptide-1) modelled after the N-terminus of glycogen synthase.. MAPKAP kinase-2 is a novel protein kinase activated by mitogen-activated protein kinase. This MAP kinase activated protein kinase, termed MAPKAP kinase-2, is distinguished from S6 kinase-II (MAPKAP kinase-1) by its response to inhibitors, lack of phosphorylation of S6 peptides and amino acid sequence.. ...
MAP kinase-activated protein kinase 2 is an enzyme that in humans is encoded by the MAPKAPK2 gene. This gene encodes a member of the Ser/Thr protein kinase family. This kinase is regulated through direct phosphorylation by p38 MAP kinase. In conjunction with p38 MAP kinase, this kinase is known to be involved in many cellular processes including stress and inflammatory responses, nuclear export, gene expression regulation and cell proliferation. Heat shock protein HSP27 was shown to be one of the substrates of this kinase in vivo. Two transcript variants encoding two different isoforms have been found for this gene. SB 203580, suppresses the activation of MAPKAPK2 MAPKAPK2 has been shown to interact with: AKT1, MAPK14, PHC2, and SHC1. GRCh38: Ensembl release 89: ENSG00000162889 - Ensembl, May 2017 GRCm38: Ensembl release 89: ENSMUSG00000016528 - Ensembl, May 2017 "Human PubMed Reference:". "Mouse PubMed Reference:". Zu YL, Wu F, Gilchrist A, Ai Y, Labadia ME, Huang CK (Jun 1994). "The primary ...
In this report, we have found that anti-DLL4 has broad spectrum activity in pancreatic xenografts based on testing a panel of patient-derived tumor models. In vivo studies showed that anti-DLL4 was efficacious, alone and in combination with gemcitabine, in reducing tumor growth in all pancreatic tumors tested, including both low- and high-grade tumors. Anti-DLL4 treatment had a potent effect in delaying tumor recurrence after gemcitabine treatment. Furthermore, anti-DLL4 was found to reduce tumor initiating cell frequency as a single agent and in combination with gemcitabine. Agents that reduce CSC frequency have the potential to provide significant clinical benefit by reducing tumor recurrence after therapy and by inhibiting the metastatic spread of the disease. In contrast to anti-DLL4, treatment with gemcitabine alone was ineffective at reducing CSC frequency. While gemcitabine is a standard agent for treatment of pancreatic cancer, the effect of gemcitabine on survival has been disappointing ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
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Protein kinase B (PKB) isoforms became activated [and glycogen synthase kinase-3 (GSK3) became inhibited] when mouse Swiss 3T3 fibroblasts were exposed to oxidative stress (H2O2) or heat shock, but not when they were exposed to osmotic shock (0.5 M sorbitol or 0.7 M NaCl), chemical stress (sodium arsenite), the protein-synthesis inhibitor anisomycin, or UV radiation. In contrast, all seven stimuli activated mitogen-activated protein kinase-activated protein kinase-2 (MAPKAP-K2). The activation of MAPKAP-K2 was suppressed by the drug SB 203580, but not by inhibitors of phosphoinositide (phosphatidylinositide, PI) 3-kinase. In contrast, the activation of PKB isoforms and the inhibition of GSK3 by oxidative stress or heat shock were prevented by inhibitors of PI 3-kinase, but not by SB 203580. Thus the activation of PKB by oxidative stress or heat shock is mediated by PI 3-kinase and not by MAPKAP-K2. PKBα and PKBγ were also activated by heat shock and oxidative stress in human embryonic kidney ...
90 kDa ribosomal protein S6 kinase 1; HU-1; MAP kinase-activated protein kinase 1a; MAPK-activated protein kinase 1a; MAPKAP kinase 1a; MAPKAPK-1a; MAPKAPK1A; RSK; RSK-1; RSK1; S6K-alpha 1; S6K-alpha-1; dJ590P13.1 (ribosomal protein S6 kinase, 90kD, polypeptide 1); p90-RSK 1; p90RSK1; p90S6K; ribosomal S6 kinase 1; ribosomal protein S6 kinase alpha 1; ribosomal protein S6 kinase alpha-1; ribosomal protein S6 kinase, 90kD, polypeptide 1; ribosomal protein S6 kinase, 90kDa, polypeptide ...
The Hippo pathway inactivates genes involved in organ size and when aberrant, can lead to cancer. To control organ size, the Hippo pathway inhibits Yorkie (Yki), a transcriptional coactivator that works with Scalloped (Sd), a DNA binding protein. When active, Yki translocates into the nucleus and initiates transcription. Conversely, when inactive, Yki remains in the cytoplasm. However, my work shows that cytoplasmic, inactive Yki interacts with other proteins in the Hippo pathway by recruiting them to the plasma membrane. Accordingly, this study challenges the notion that cytoplasmic Yki is inactive and instead, may play a dual role in the Hippo pathway.
The spleen tyrosine kinase Syk was mainly studied in immunoreceptor-activated signaling in hematopoietic cells. We first demonstrated that Syk is also present in mammary epithelial cells and that its expression is lost in malignant breast cancer cells. Using mouse xenograft models injected with Syk-transfected cells we and others established that Syk acts as a tumor and metastasis suppressor. Moreover, clinical studies reveal a correlation between reduced Syk expression and a decreased survival and increased metastasis risk in breast cancer and other carcinomas. The main objective of our investigations is to unravel the mechanisms of the anti-oncogenic activity of Syk. For this, identification of its substrates and signaling pathways is crucial. A quantitative phospho-proteomic approach allowed to identify novel potential Syk substrates involved in intercellular adhesion and epithelial polarity, both characteristics of cell differentiation that are lost during tumor invasion and ...
Hippo signaling pathway, also known as the Salvador/Warts/Hippo (SWH) pathway, controls organ size in animals through the regulation of cell proliferationand apoptosis. The Hippo pathway consists of a core kinase cascade in which Hpo phosphorylates the protein kinase Warts (Wts) Hpo (MST1/2 in mammals) is a member of the Ste-20 family of protein kinases. This highly conserved group of serine/threonine kinases regulates several cellular processes, including cell proliferation, apoptosis, and various stress responses.. ...
The Wnt-5a protein has been implicated in breast cancer metastasis by affecting DDR1-dependent adhesion and motility of breast tumor cells (6, 8). The activation of DDR1 requires Wnt-5a-mediated stimulation of Src non-receptor tyrosine kinases (8), and a well-known downstream signaling target of Src kinases is the tyrosine kinase Syk (9). This is intriguing, because Syk expression is associated with an increased risk of metastatic spread in human breast carcinomas (11, 12). In the present study, we found a covariation between Syk and Wnt-5a protein expressions in mammary cell lines. It is hard to directly correlate the presence of Wnt-5a and Syk with the reported tumorigenic and metastatic potential of the presently used cell lines due to variations in the properties of a distinct cell lines between different laboratories and the use of different animals models. However, it is interesting to note that the two cell lines that exhibit no or a low expression of Wnt-5a and lack of Syk expression ...
Syk-dependent actin dynamics regulate endocytic trafficking and processing of antigens internalized through the B-cell receptor.: Antigen binding to the B-cell
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A new drug appears to destroy lingering senescent cells, and it achieves this without using any of the previously known mechanisms or pathways.
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I rarely remember my dreams, but for the past week, GOP vice-presidential nominee Sarah Palin has been haunting me. Night after night, she appears in m ...
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A new jab that works even if the virus mutates and can spell the end of annual flu jabs for millions has been developed by scientists.
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A novel approach to design selective spleen tyrosine kinase (Syk) inhibitors is described. Inhibition of spleen tyrosine kinase has attracted much attention as a mechanism for the treatment of autoimmune diseases such as asthma, rheumatoid arthritis,
Purpose: To investigate the role of mitogen-activated protein kinase-activated protein kinase-2 (MK2) in ocular surface damage of dry eye. Methods: MK2 inhibition was performed in mice subjected to desiccating stress (DS) by topical application of MK2 inhibitor (MK2i) or vehicle eye drops. The total and phosphorylated MK2 in conjunctiva were detected by Western blot. The phenol red cotton test was used to measure tear production, and Oregon green dextran staining was performed to assess corneal epithelial barrier function. PAS staining was used to quantify conjunctival goblet cells. Immunofluorescent staining and quantitative RT-PCR were used to assess the expression of matrix metalloproteinase (MMP)-3 and -9 in corneal epithelium. Apoptosis in ocular surface was assessed by TUNEL and immunofluorescent staining for activated caspase-3 and -8. Inflammation was evaluated by CD4+ T-cell infiltration and production of T helper (Th) cytokines, including IFN-γ, IL-13, and IL-17A in conjunctiva. ...