Snare Proteins
Mostrando 1-12 de 134 artigos, teses e dissertações.
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1. Biochemical and Molecular Mechanisms of Glucose Uptake Stimulated by Physical Exercise in Insulin Resistance State: Role of Inflammation
Resumo A obesidade associada à inflamação sistêmica induz resistência à insulina (RI), com consequente hiperglicemia crônica. Este processo envolve o aumento na liberação de citocinas pró-inflamatórias, ativação da enzima c-Jun N-terminal cinase (JNK), do fator nuclear kappa-B (NF-κB) e dos receptores do tipo Toll 4 (TLR4). Dentre as ferramenta
Arq. Bras. Cardiol.. Publicado em: 21/10/2019
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2. Increased expression levels of Syntaxin 1A and Synaptobrevin 2/Vesicle-Associated Membrane Protein-2 are associated with the progression of bladder cancer
Abstract Gene expression is tightly regulated in time and space through a multitude of factors consisting of signaling molecules. Soluble N-ethylmaleimide-sensitive-factor attachment protein receptors (SNARE) are membrane proteins responsible for the intercellular trafficking of signals through endocytosis and exocytosis of vesicles. Altered expression of SN
Genet. Mol. Biol.. Publicado em: 21/01/2019
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3. Prolactina potencializa a secreção de insulina via formação do complexo SNARE em ilhotas pancreaticas / Prolactin modulates the insulin secretion by SNARE complex formation in neonatal rat islets
Prolactin induces maturation of insulin secretion in cultured neonatal rat islets. In this study, we investigated whether the improved secretory response to glucose caused by prolactin involves alteration in the expression, association and phosphorylation of several proteins that participate in these processes. Messenger RNA was extracted from neonatal rat i
Publicado em: 2006
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4. Prolactina induz aumento na expressão das proteinas SNARE e da sinaptotagmina 4 em ilhotas de ratos
The soluble N-ethylmaleimide-sensitive factor attached protein receptor (SNARE) molecules SNAP-25, syntaxin and VAMP-2 as well as synaptotagmins participate in the extrusion of insulin containing granules in pancreatic β -cells. During pregnancy and the perinatal periods of life, prolactin (PRL) and other lactogenic substances induce maturation of the s
Publicado em: 2004
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5. Dynamic transport of SNARE proteins in the Golgi apparatus
Localization of a membrane protein in a subcellular compartment can be achieved by its retention in the compartment or by its continuous transport toward this compartment. Previous results have suggested that specific enzymes are localized in the Golgi apparatus at least in part by selective retention and exclusion from transport vesicles. However, the funct
National Academy of Sciences.
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6. SNARE proteins contribute to calcium cooperativity of synaptic transmission
A hallmark of calcium-triggered synaptic transmission is the cooperative relationship between calcium and the amount of transmitter released. This relationship is thought to be important for improving the efficiency of synaptic vesicle exocytosis. Although it is generally held that cooperativity arises from the interaction of multiple calcium ions with
The National Academy of Sciences.
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7. Phosphorylation of SNAP-23 by the Novel Kinase SNAK Regulates t-SNARE Complex Assembly
The docking and fusion of cargo-containing vesicles with target membranes of eukaryotic cells is mediated by the interaction of SNARE proteins present on both vesicle and target membranes. In many cases, the target membrane SNARE, or t-SNARE, exists as a complex of syntaxin with a member of the SNAP-25 family of palmitoylated proteins. We have identified a n
The American Society for Cell Biology.
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8. Three SNARE complexes cooperate to mediate membrane fusion
Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins of the syntaxin, SNAP-25, and VAMP families mediate intracellular membrane fusion through the formation of helical bundles that span opposing membranes. Soluble SNARE domains that lack their integral membrane anchors inhibit membrane fusion by forming nonfunctional complex
The National Academy of Sciences.
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9. The specificity of SNARE-dependent fusion is encoded in the SNARE motif
Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins constitute the core of the fusion machinery, and isolated SNAREs fuse membranes with exquisite specificity by cognate pairing. Most SNAREs have a membrane-spanning region, an N-terminal domain, and a membrane proximal SNARE motif domain. Although the SNARE motif is critica
National Academy of Sciences.
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10. Analysis of Sec22p in Endoplasmic Reticulum/Golgi Transport Reveals Cellular Redundancy in SNARE Protein Function
Membrane-bound soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins form heteromeric complexes that are required for intracellular membrane fusion and are proposed to encode compartmental specificity. In yeast, the R-SNARE protein Sec22p acts in transport between the endoplasmic reticulum (ER) and Golgi compartments but is n
The American Society for Cell Biology.
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11. Selective Formation of Sed5p-containing SNARE Complexes Is Mediated by Combinatorial Binding Interactions
Sed5p is the only syntaxin family member required for protein transport through the yeast Golgi and it is known to bind up to nine other soluble N-ethylmaleimide-sensitive factor attachment receptor (SNARE) proteins in vivo. We describe in vitro binding experiments in which we identify ternary and quaternary Sed5p-containing SNARE complexes. The formati
The American Society for Cell Biology.
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12. Three-dimensional structure of the amino-terminal domain of syntaxin 6, a SNAP-25 C homolog
Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins are required for intracellular membrane fusion, and are differentially localized throughout the cell. SNAREs on vesicle and target membranes contain “SNARE motifs” which interact to form a four-helix bundle that contributes to the fusion of two membranes. SNARE motif s
The National Academy of Sciences.