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Descrição: There is accumulating evidence to suggest that progesterone plays an essential role in the regulation of growth and differentiation of mammary glands and thus may play a key role in breast cancer. The biological response to progesterone is mediated by two distinct forms of the human progesterone receptor (A and B forms). In most cell contexts, the B form functions as a transcriptional activator, whereas the A form functions as a transcriptional inhibitor of steroid hormones. Recently it has been demonstrated that there is differential hormone dependent regulation of the phosphorylation of the A and B forms of the receptor. Treatment of T47D breast cancer cells with progestin agonist increases the phosphorylation of Ser190 and Ser294 with different kinetics. These phosphorylation events may differentially affect the transcriptional activity of the receptor.
Código de Artigo: PRSIXPS-1024
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: It is well known that the control of gene expression involves activation of protein kinase cascades that regulate transcription factors within the nucleus (Karin and Hunter, 1995). The cyclic AMP response element binding protein (CREB) is one of the best characterized stimulus-induced transcription factors (Montminy, 1997). This transcription factor is a component of intracellular signaling events that regulate a wide range of biological functions, from spermatogenesis to circadian rhythms and memory (Shaywitz and Greenberg, 1999; Silva et al., 1998). A variety of protein kinases including protein kinase A (PKA), mitogenactivated protein kinases (MAPKs), and Ca2+/calmodulin-dependent protein kinases (CaMKs) phosphorylate CREB at serine 133 (Ser133), and phosphorylation of Ser133 are required for CREB-mediated transcription (Johannessen et al., 2004; Kornhauser et al., 2002).
Código de Artigo: PRSI50-221
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: Tryptophan hydroxylase (TPH) catalyzes the 5-hydroxylation of tryptophan, which is the first step in the biosynthesis of indoleamines (serotonin and melatonin) (Martinez et al., 2001). In mammals, serotonin biosynthesis occurs predominantly in neurons which originate in the Raphe nuclei of the brain, and melatonin synthesis takes place within the pineal gland. Although TPH catalyzes the same reaction within the Raphe nuclei and the pineal gland, TPH activity is rate-limiting for serotonin but not melatonin biosynthesis. Serotonin functions mainly as a neurotransmitter, whereas melatonin is the principal hormone secreted by the pineal gland. The activity of TPH is enhanced by phosphorylation by cAMP-dependent protein kinase (PKA) and Ca2+/calmodulin kinase II (CaM K II) (Jiang et al., 2000; Johansen et al., 1996). CaM K II phosphorylates Ser19 which lies within the regulatory domain of TPH2 (McKinney et
Código de Artigo: PRSI50-242
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: The NMDA receptor (NMDAR) plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002; Wenthold et al., 2003; Carroll and Zukin, 2002). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993). Phosphorylation of Tyr1252 is thought to potentiate NMDA receptor-dependent influx of calcium (Takasu et al., 2002).
Código de Artigo: PRSI50-232
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR) while those activated by alpha-amino-3-hydroxy-5-methyl-4-isoxalone propionic acid (AMPA) are known as AMPA receptors (AMPAR). The AMPAR are comprised of four distinct Glutamate Receptor Subunits designated (GluR1-4) and they play key roles in virtually all excitatory neurotransmission in the brain (Keinänen et al., 1990;Hollmann and Heinemann, 1994). The GluR2 subunit is widely expressed throughout the nervous system where it is thought to play key roles in synaptic plasticity and learning and memory (Duprat et al., 2003; Seidenman et al., 2003; Chung et al., 2003; Yan et al., 2002).
Código de Artigo: PRSI50-219
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: In mammals, there are several identified isoforms of p21-activated protein kinases or PAKs: alpha-PAK (also known as PAK-1) and beta-PAK (also known as PAK-3) are mostly brain-specific, while -PAK (also known as PAK-2) is expressed ubiquitously (Jakobi et al., 2003). Mutations of the gene coding for PAK-3 are associated with X-linked mental retardation and recent work indicates that PAK-3 is a key regulator of synapse formation and plasticity in the hippocampus (Boda et al., 2004). PAK-3 is thought to play a key role in regulation of cell shape and motility as well as cell death (Jakobi et al., 2003; Walter et al., 1998). Autophosphorylation of Thr402 in the protein has been found to be essential for activation of PAK (Jakobi et al., 2000).
Código de Artigo: PRSI50-246
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: The enzyme 5-lipoxygenase (5-LO) plays a key role in regulating the production of leukotrienes (LTs) (Funk, 2001). Overproduction of LTs contributes to several diseases, most notably chronic inflammatory diseases, including asthma (Drazen et al., 1994), fibrosis (Wilborn et al., 1996) and atherosclerosis (Dwyer et al., 2004). Recent work has demonstrated that the activity of 5-LO is regulated by PKA phosphorylation of serine-523 in 5-LO (Luo et al., 2004). Under normal conditions, this phosphorylation may be important in limiting inflammation. Abnormal signaling through cAMP and PKA, then, could contribute to a variety of diseases, including those characterized by chronic inflammation. The phospho-specific antibody to Ser523 on 5-LO is thus likely to provide a valuable tool for studies of the role of 5-LO regulation in diseases such as asthma, fibrosis and atherosclerosis.
Código de Artigo: PRSI50-244
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR) while those activated by alpha-amino-3-hydroxy-5-methyl-4-isoxalone propionic acid (AMPA) are known as AMPA receptors (AMPAR). The AMPAR are comprised of 4 distinct subunits (GluR1-4) and they play key roles in virtually all excitatory neurotransmission in the brain. The GluR1 subunit is widely expressed throughout the nervous system. GluR1 is also potentiated by phosphorylation at Ser845. In addition, phosphorylation of this site has been linked to synaptic plasticity as well and learning and memory.
Código de Artigo: PRSIXPS-1013
UOM: 1 * 150 µl
Fornecedor: ProSci Inc.


Descrição: EphrinB proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development (Flanagan and Vanderhaeghen, 1998; Dufour et al., 2003; Oike et al., 2002). EphrinB molecules expressed at the membrane surface bind to the EphB family receptors on target cells during cell-to cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing EphrinB on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of EphrinB is thought to be a critical component of this reverse signaling event (Palmer et al., 2002). Recent work suggests that phosphorylation of a specific EphrinB residue (Tyr298) plays a key role in EphrinB signaling (Kalo, et al., 2001).
Código de Artigo: PRSI50-223
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR) while those activated by beta-amino-3-hydroxy-5-methyl-4-isoxalone propionic acid (AMPA) are known as AMPA receptors (AMPAR). The AMPAR are comprised of four distinct subunits GluR1-4 and they play key roles in virtually all excitatory neurotransmission in the brain. The GluR1 subunit is widely expressed throughout the nervous system. GluR1 is also potentiated by phosphorylation at Ser831. In addition, phosphorylation of this site has been linked to synaptic plasticity as well and learning and memory.
Código de Artigo: PRSIXPS-1012
UOM: 1 * 150 µl
Fornecedor: ProSci Inc.


Descrição: The NMDAR plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002; Wenthold et al., 2003; Carroll and Zukin, 2002). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993). Phosphorylation of Tyr1336 is thought to potentiate NMDA receptor-dependent influx of calcium (Takasu et al., 2002) and ischemia may also increase the phosphorylation of this site (Takagi et al., 2003).
Código de Artigo: PRSI50-233
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: The NMDA receptor (NMDAR) plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002; Wenthold et al., 2003; Carroll and Zukin, 2002). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993). It has been shown that phosphorylation of Ser1480 disrupts the interaction of NR2B with the PDZ domains of PSD-95 and SAP102 and decreases surface NR2B expression in neurons (Chung et al., 2004).
Código de Artigo: PRSI50-234
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: EphrinB proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development (Flanagan and Vanderhaeghen, 1998; Dufour et al., 2003; Oike et al., 2002). EphrinB molecules expressed at the membrane surface bind to the EphB family receptors on target cells during cell-to cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing EphrinB on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of EphrinB is thought to be a critical component of this reverse signaling event (Palmer et al., 2002). Recent work demonstrated that Tyr331 of EphrinB was phosphorylated in HEK293 cells after stimulation by the soluble EphB2 receptor tyrosine kinase (Kalo et al., 2001).
Código de Artigo: PRSI50-224
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: EphrinB proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development (Flanagan and Vancerhaeghen, 1998; Dufour et al., 2003; Oike et al., 2002). EphrinB molecules expressed at the membrane surface bind to the EphB family receptors on target cells during cellto cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing EphrinB on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of EphrinB is thought to be a critical component of this reverse signaling event (Palmer et al., 2002). Recent work suggests that phosphorylation of a specific EphrinB residue (Tyr298) plays a key role in EphrinB signaling (Kalo, et al., 2001).
Código de Artigo: PRSI50-222
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: The activating transcription factor ATF-2 (also called CRE-BP1) binds to both AP-1 and CRE DNA response elements and is a member of the ATF/CREB family of leucine zipper proteins. ATF-2 has been implicated in the transcriptional regulation of a number of genes including cytokines, cell cycle control and apoptosis. Various forms of cellular stress, including inflammatory cytokines and UV irradiation, stimulate the transcriptional activity of ATF-2. Stress induced ATF-dependent transcription is dependent on phosphorylation of ATF. Serine 490 and serine 498 are novel phosphorylation sites on ATF that have recently been identified. In addition, ATF2 is particularly abundant in the brain and the ATF2 family of transcription factors is considered important substrates of signals upstream of the activation of genes associated with neuronal growth and differentiation. ATF expression has also been linked to the depression in humans.
Código de Artigo: PRSIXPS-1002
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


Descrição: 14-3-3 proteins are a family of highly conserved proteins that appear to have multiple roles in cell signaling (Bridges and Moorhead, 2005). The proteins are abundantly expressed in the brain and have been detected in the cerebrospinal fluid of patients with different neurological disorders (Berg et al., 2003). 14-3-3 proteins bind protein ligands that are typically phosphorylated on
serine or threonine residues and regulate the functions of these binding partners by a number of different mechanisms (Silhan et al., 2004; Dougherty and Morrison, 2004). The14-3-3 proteins affect a diverse array of cellular processes including the cell cycle and transcription, signal transduction and intracellular trafficking. These functions of 14-3-3 proteins are facilitated by, if not dependent on, its dimeric structure. Recent work has demonstrated that the dimeric status of the 14-3-3 protein is regulated by site-specific serine phosphorylation (Woodcock et al., 2003).
Código de Artigo: PRSI50-231
UOM: 1 * 100 µl
Fornecedor: ProSci Inc.


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