118494 Results for: "Szufelki+do+pr\u00F3bek&pageNo=30"

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FUT5

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Retinoids are metabolites of vitamin A (retinal) and are believed to represent important signaling molecules during vertebrate development and tissue differentiation. Two families of retinoid receptors have been identified. Retinoic acid receptors (RARs) include RAR alpha, RAR beta and RAR gamma, each of which has a high affinity for all trans retinoic acids and belongs to the same class of nuclear transcription factors as thyroid hormone receptors, vitamin D3 receptor and ecdysone receptor. The ligand binding domains of the RARs are highly conserved and RAR isoforms are expressed in distinct patterns through out development and in the mature organism. Members of the retinoid X receptor (RXR) family, RXR alpha, RXR beta and RXR gamma, are activated by 9 cis retinoic acid, a stereo and photoisomer of all trans RA that is expressed in vivo in both liver and kidney and may represent a widely used hormone.

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Induces susceptibility to atherosclerosis (By similarity). Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-69 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).

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The TRIM motif includes three zinc binding domains, a RING, a B box type 1 and a B box type 2, and a coiled-coil region. The protein localizes to both the cytoplasm and the nucleus. Its function has not been identified.

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Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4.

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STAC2

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Ligand for members of the frizzled family of seven transmembrane receptors. Probable developmental protein. May be a signaling molecule which affects the development of discrete regions of tissues. Is likely to signal over only few cell diameters (By similarity). Overexpression may be associated with abnormal proliferation in human breast tissue.

Supplier: Bioss

May function actively to stimulate axon fasciculation. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase.

Supplier: Bioss

The cell division control protein cdc2, also known as cyclin dependent kinase 1 (Cdk1) or p34/cdk1, plays a key role in the control of the eukaryotic cell cycle, where it is required for entry into S phase and mitosis. Cdc2 exists as a complex with both cyclin A and cyclin B. The best characterized of these associations is the Cdc2 p34 cyclin B complex, which is required for the G2 to M phase transition. Activation of Cdc2 is controlled at several steps including cyclin binding and phosphorylation of threonine 161. However, the critical regulatory step in activating cdc2 during progression into mitosis appears to be dephosphorylation of Tyr15 and Tyr14. Phosphorylation at Tyr15 and inhibition of Cdc2 is carried out by WEE1 and MIK protein kinases while Tyr15 dephosphorylation and activation of Cdc2 is carried out by the cdc25 phosphatase. The isoform CDC2deltaT is found in breast cancer tissues. Furthermore, cdc2/Cdk1 is a key mediator of neuronal cell death in brain development and degeneration.

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Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.

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Fibroblast growth factors (FGFs) produce mitogenic and angiogenic effects in target cells by signaling through the cellular surface tyrosine kinase receptors. There are four members of the FGF receptor family: FGFR-1 (flg), FGFR-2 (bek, KGFR), FGFR-3 and FGFR-4. Each receptor contains an extracellular ligand binding domain, a transmembrane region and a cytoplasmic kinase domain (1). Following ligand binding and dimerization, the receptors are phosphorylated at specific tyrosine residues (2). Seven tyrosine residues in the cytoplasmic tail of FGFR-1 can be phosphorylated: Tyr463, Tyr583, Tyr585, Tyr653, Tyr654, Tyr730 and Tyr766. Tyrosine 653 and 654 are important for catalytic activity of the activated FGFR and are essential for signaling (3). The other phosphorylated tyrosine residues may provide docking sites for downstream signaling components such as Crk and PLCgamma.

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Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

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Fc (Ig constant fragment) receptors ensure protection of the host against foreign antigens, such as microorganisms and pathogens, by removing Ig-coated antigen complexes from circulation. Fc receptors are present on lymphoid and myeloid derivatives, where they mediate endocytosis of Ig-antigen complexes, antibody production in B cells through T cell antigen presentation, cytotoxicity and the release of cytokines and reactive oxygen species. The Fc γ-binding protein (FCGBP) interacts with the Fc portion of IgG and MUC2 to mediate the maintenance of the mucosal structure. FCGBP is a 5,405 amino acid protein that contains twelve TIL (trypsin inhibitory-like) domains and thirteen VWFD domains. It is predominantly expressed in placenta and colon epithelium as well as in thyroid and serum. Patients with various autoimmune diseases seemingly have higher levels of FCGBP protein present in their serum.

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Serine protease which exhibits a preference for Arg over Lys in the substrate P1 position and for Ser or Pro in the P2 position. Shows activity against amyloid precursor protein, myelin basic protein, gelatin, casein and extracellular matrix proteins such as fibronectin, laminin, vitronectin and collagen. Degrades alpha-synuclein and prevents its polymerization, indicating that it may be involved in the pathogenesis of Parkinson disease and other synucleinopathies. May be involved in regulation of axon outgrowth following spinal cord injury. Tumor cells treated with a neutralizing KLK6 antibody migrate less than control cells, suggesting a role in invasion and metastasis.

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May be involved in the control of the cell cycle at the G1/S (start) and G2/M (mitosis) transitions. May primarily function in the control of the germline meiotic cell cycle and additionally in the control of mitotic cell cycle in some somatic cells.

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Plays a role in the regulation of the circadian clock. Modulates the period length and phase of circadian gene expression and also regulates expression and interaction of the core clock components PER1/2 and CRY1/2. Seems to have an immune potentiation function.

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Apoptotic suppressor. The BIR motifs region interacts with TNF receptor associated factors 1 and 2 (TRAF1 and TRAF2) to form an heteromeric complex, which is then recruited to the tumor necrosis factor receptor 2 (TNFR2).

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GLUD2 is both mitochondrial matrix enzymes belonging to the Glu/Leu/Phe/Val dehydrogenases family. Exisiting as homohexamers, GLUD1 catalyzes the oxidative deamination of glutamate to ?ketoglutarate and ammonia while GLUD2 is involved in the recycling of glutamate during neurotransmission. GLUD1 is critical for regulating amino acid induced insulin secretion and is allosterically activated by ADP and inhibited by GTP and ATP. Mutations in the gene encoding GLUD1 causes hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 may also be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate. GLUD2 is expressed in testis and retina, with lower levels found in brain.

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G Gamma14 (GNGT2) is a Guanine nucleotide-binding protein. G proteins are composed of 3 units, alpha, beta and gamma and are involved in various transmembrane signaling systems as signal modulators or transducers. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction. This G protein is specific to retinal cones and is involved in regulation of phototransduction.

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In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at 'Lys-4' of histone H3. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation.

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Lysosome associated membrane protein (LAMP1), also known as lgp120 or lgpA, is a type 1 integral membrane protein that is transported from trans Golgi networks to endosomes and then lysosomes. Upon cell activation, LAMP1 transfer to the plasma membrane is dependent on a carboxyl terminal tyrosine based motif (YXXI). Perturbation in the spacing between the tyrosine based motif relative to the membrane abolishes lysosome localization of LAMP1. This mutant protein then cycles between the plasma membrane and the endosome. Cell surface LAMP1 and LAMP2 have been shown to promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium, therefore they are possibly involved in the adhesion of PBMCs to the site of inflammation.

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WD-repeats are motifs that are found in a variety of proteins and are characterized by a conserved core of 40-60 amino acids that commonly form a tertiary propeller structure. While proteins that contain WD-repeats participate in a wide range of cellular functions, they are generally involved in regulatory mechanisms concerning chromatin assembly, cell cycle control, signal transduction, RNA processing, apoptosis and vesicular trafficking. WDFY1 (WD repeat and FYVE domain containing 1), also known as WDF1, FENS-1 or ZFYVE17, is a 410 amino acid protein that localizes to the early endosome and contains one FYVE-type zinc finger and seven WD repeats through which it may play a role in protein trafficking and signal transduction.

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Receptor for a number of inflammatory CC-chemokines including MIP-1-alpha, MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Acts as a coreceptor (CD4 being the primary receptor) for HIV-1 R5 isolates.

Supplier: Bioss

May play a role in Notch signaling (By similarity). May be involved in the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins.

Supplier: Bioss

GTPases from the MMR1/HSR1 GTP-binding protein subfamily are circularly rearranged G-motifs that play a critical role in maintaining normal cell growth. Deletion of these genes results in severe growth defects with a marked reduction in mature rRNA species and a concomitant accumulation of the 35S pre-rRNA transcript. Deletion also causes the ribosomal protein Rpl25a to fail exportation from the nucleolus. Deletion of any of the G-domain motifs will result in a null phenotype and nuclear/nucleolar localization that lacks the nucleolar export of preribosomes and is accompanied by a distortion of the nucleolar structure. GNL3L (guanine nucleotide binding protein-like 3 (nucleolar)-like) is a 582 amino acid nuclear protein that belongs to the MMR1/HSR1 GTP-binding protein family. Containing one G (guanine nucleotide-binding) domain, GNL3L is required for normal processing of ribosomal pre-rRNA and for cell proliferation.

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HYAL3 is a protein which is similar in structure to hyaluronidases. Hyaluronidases intracellularly degrade hyaluronan, one of the major glycosaminoglycans of the extracellular matrix. Hyaluronan is thought to be involved in cell proliferation, migration and differentiation. However, this protein has not yet been shown to have hyaluronidase activity.

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B and T lymphocyte attenuator (BTLA), an immunoglobulin domain-containing glycoprotein with two immunoreceptor tyrosine-based inhibitory motifs. BTLA is not expressed by naive T cells, but it is induced during activation and remains expressed on T helper type 1 (T(H)1) but not T(H)2 cells. Crosslinking BTLA with antigen receptors induces its tyrosine phosphorylation and association with the Src homology domain 2 (SH2)-containing protein tyrosine phosphatases SHP-1 and SHP-2, and attenuates production of interleukin 2 (IL-2). BTLA-deficient T cells show increased proliferation, and BTLA-deficient mice have increased specific antibody responses and enhanced sensitivity to experimental autoimmune encephalomyelitis. B7x, a peripheral homolog of B7, is a ligand of BTLA. Thus, BTLA is a third inhibitory receptor on T lymphocytes with similarities to cytotoxic T lymphocyte-associated antigen 4 (CTLA-4) and programmed death 1 (PD-1).

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Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. AVEN is a recently discovered protein that blocks apoptosis induced by Apaf-1 and caspase-9. It is thought that AVEN functions by binding to Bcl-xL, an antiapoptotic member of the Bcl-2 family, and to Apaf-1, possibly interfering with the ability of Apaf-1 to self-associate, suggesting that AVEN impedes Apaf-1-mediated caspase activation. Higher levels of AVEN mRNA are seen in patients with acute leukemia than in control patients, suggesting that AVEN may be useful as a prognostic indicator in leukemia patients.

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This protein is associated with nerve growth. It is a major component of the motile "growth cones" that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction.

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Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate (By similarity).