Orai1
Mostrando 1-12 de 19 artigos, teses e dissertações.
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1. Pharmacological characterization of the calcium influx pathways involved in nitric oxide production by endothelial cells
RESUMO Objetivo: Caracterizar as vias do influxo de cálcio envolvidas no aumento sustentado da concentração intracelular de cálcio na célula endotelial, essencial para a síntese e a liberação de fatores relaxantes. Métodos: Analisamos o efeito de derivados pirazólicos sintetizados recentemente, descritos como inibidores seletivos para canais ORAI
Einstein (São Paulo). Publicado em: 03/06/2019
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2. STIM1/Orai1-mediated store-operated Ca2+ entry: the tip of the iceberg
Highly efficient mechanisms regulate intracellular calcium (Ca2+) levels. The recent discovery of new components linking intracellular Ca2+ stores to plasma membrane Ca2+ entry channels has brought new insight into the understanding of Ca2+ homeostasis. Stromal interaction molecule 1 (STIM1) was identified as a Ca2+ sensor essential for Ca2+ store depletion-
Brazilian Journal of Medical and Biological Research. Publicado em: 2011-11
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3. Contribuição da via STIM1/Orai1 para as diferenças relacionadas ao sexo na entrada de cálcio em miócitos vasculares durante a hipertensão arterial. / Activation of STIM1/Orai1 mediates sex-differences in the calcium influx in vascular miocytes from hypertensive rats.
Os distúrbios na regulação da concentração de cálcio (Ca2+) citoplasmático contribuem para a patogênese da hipertensão arterial. Evidências sugerem que as moléculas de interação estromal (STIM) atuam como sensores dos estoques intracelulares de Ca2+, enquanto as proteínas Orai representam as subunidades que formam os canais de Ca2+ ativados pel
Publicado em: 2010
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4. Efeitos do extrato liofilizado da Euphorbia tirucalli sobre a resposta hematopoetica em camundongos portadores do tumor ascistico de Ehrlich
In this work, we have investigated the effects of the liofilizated extract of the Euphorbia tiruca1li(TEE), onthe growthand differentiation of hematopoietic progenitors for granuiocyte/macrophage (CFU-GM) in the bone marrOWanelspieen of Ehrlich ascites tumor-bearing mice (EAT). !vWeBaib/c mice were inoculated intraperitoneaily (i.p.) with 6xI06 viabie tumorc
Publicado em: 2003
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5. Molecular Determinants of the Coupling between STIM1 and Orai Channels: DIFFERENTIAL ACTIVATION OF Orai1–3 CHANNELS BY A STIM1 COILED-COIL MUTANT*
STIM1 and Orai1 have been reported to interact upon store depletion culminating in Ca2+ release-activated Ca2+ current activation. Recently, the essential region has been identified within the STIM1 C terminus that includes the second coiled-coil domain C-terminally extended by ∼50 amino acids and exhibits a strong binding to the Orai1 C terminus. Based on
American Society for Biochemistry and Molecular Biology.
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6. Properties of Orai1 mediated store-operated current depend on the expression levels of STIM1 and Orai1 proteins
Two cellular proteins, stromal interaction molecule 1 (STIM1) and Orai1, are recently discovered essential components of the Ca2+ release activated Ca2+ (CRAC) channel. Orai1 polypeptides form the pore of the CRAC channel, while STIM1 plays the role of the endoplasmic reticulum Ca2+ sensor required for activation of CRAC current (ICRAC) by store depletion. I
Blackwell Science Inc.
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7. Plasticity in Ca2+ selectivity of Orai1/Orai3 heteromeric channel
A general cellular response following depletion of intracellular calcium stores involves activation of store-operated channels (SOCs). While Orai1 forms the native Ca2+ release-activated Ca2+ (CRAC) channel in mast and T cells, the molecular architecture of less Ca2+ selective SOCs is insufficiently defined. Here we present evidence that diminished Ca2+ sele
National Academy of Sciences.
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8. Increased Hydrophobicity at the N Terminus/Membrane Interface Impairs Gating of the Severe Combined Immunodeficiency-related ORAI1 Mutant*
Patients with severe combined immune deficiency (SCID) suffer from defective T-cell Ca2+ signaling. A loss of Ca2+ entry has been linked at the molecular level to single missense mutation R91W in the store-operated Ca2+ channel ORAI1. However, the mechanistic impact of this mutation on ORAI1 function remains unclear. Confocal Förster resonance energy transf
American Society for Biochemistry and Molecular Biology.
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9. The Short N-terminal Domains of STIM1 and STIM2 Control the Activation Kinetics of Orai1 Channels*
STIM1 and STIM2 are dynamic transmembrane endoplasmic reticulum Ca2+ sensors, coupling directly to activate plasma membrane Orai Ca2+ entry channels. Despite extensive sequence homology, the STIM proteins are functionally distinct. We reveal that the short variable N-terminal random coil sequences of STIM1 and STIM2 confer profoundly different activation pro
American Society for Biochemistry and Molecular Biology.
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10. The molecular architecture of the arachidonate-regulated Ca2+-selective ARC channel is a pentameric assembly of Orai1 and Orai3 subunits
The activation of Ca2+ entry is a critical component of agonist-induced cytosolic Ca2+ signals in non-excitable cells. Although a variety of different channels may be involved in such entry, the recent identification of the STIM and Orai proteins has focused attention on the channels in which these proteins play a key role. To date, two distinct highly Ca2+-
Blackwell Science Inc.
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11. Orai1, a critical component of store-operated Ca2+ entry, is functionally associated with Na+/Ca2+ exchanger and plasma membrane Ca2+ pump in proliferating human arterial myocytes
Ca2+ entry through store-operated channels (SOCs) in the plasma membrane plays an important role in regulation of vascular smooth muscle contraction, tone, and cell proliferation. The C-type transient receptor potential (TRPC) channels have been proposed as major candidates for SOCs in vascular smooth muscle. Recently, two families of transmembrane proteins,
American Physiological Society.
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12. A Ca2+ Release-activated Ca2+ (CRAC) Modulatory Domain (CMD) within STIM1 Mediates Fast Ca2+-dependent Inactivation of ORAI1 Channels*♦
STIM1 and ORAI1, the two limiting components in the Ca2+ release-activated Ca2+ (CRAC) signaling cascade, have been reported to interact upon store depletion, culminating in CRAC current activation. We have recently identified a modulatory domain between amino acids 474 and 485 in the cytosolic part of STIM1 that comprises 7 negatively charged residues. A ST
American Society for Biochemistry and Molecular Biology.