Phosphoproteins
Mostrando 1-12 de 279 artigos, teses e dissertações.
-
1. Castração, dieta hiperlipídica e DHEA: efeitos sobre a sensibilidade à insulina e secreção em ilhotas isolatas de ratas. / Oophorectomy high fat diet and DHEA: effects on insulin sensitivity and insulin secretion on isolated islets rats.
A privação dos hormônios sexuais, natural ou induzida, contribui para o aparecimento de diversas desordens metabólicas e endócrinas. Esse estudo investigou se a suplementação em dose única com DHEA, esteróide mais abundante em humanos, melhora a sensibilidade à insulina, bem como sua secreção e ou tolerância à glicose em ratas castradas aliment
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 15/07/2011
-
2. Distribuição de receptores ionotrópicos de glutamato e sua co-localização com a fosfoproteína neural DARPP-32 no córtex pré-frontal de ratos. / Distribution of ionotropic glutamate receptors and their co-localization with the phosphoprotein DARPP-32 in the medial prefrontal córtex of rats.
O córtex pré-frontal medial (PFCm) é caracterizado por entradas glutamatérgicas e dopaminérgicas que convergem sobre os mesmos neurônios alvos. Devido à escassa informação sobre as bases anatômicas das interações entre a dopamina (DA) e o glutamato (Glu), mapeamos a distribuição de subunidades (Su) de receptores (Rs) de Glu do tipo AMPA, NMDA e
Publicado em: 2009
-
3. Padronização da expressão heterologa e de modelo de ensaio de atividade para a proteina quinase humana S6K / Standardization of the heterologous expression and of a model assay of activity for the human protein kinase S6K
The 70kDa ribosomal S6 protein kinase 1 (S6K1) is a phosphoprotein involved in the regulation of genes related to translational control in mammals. S6K1 shows distinct nuclear (a1) and cytoplasmic (a2) forms. Phosphorylation of the S6K1 best characterized target, the protein of the small ribosomal subunit (RPS6), has been generally associated to the selectiv
Publicado em: 2009
-
4. Aspectos do envelhecimento cerebral e função cognitiva em modelo experimental animal e estudo de mecanismos de neurodegeneração em cultura celular
The two phenomena, biological and behavioural, approached in the present work are brain aging and spatial memory. Several studies, comparative and experimental, have shown that aged subjects present significantly impaired performances in different types of cognitive tasks. It is also known that contradictions in literature exist in relation to consequences o
Publicado em: 2007
-
5. The rate-determining step in cAMP-mediated exocytosis in the rat parotid and submandibular glands appears to involve analogous 26-kDa integral membrane phosphoproteins.
The possible direct involvement of protein phosphorylation in the regulation of exocytosis during beta-adrenergic receptor stimulation in rat parotid and submandibular salivary glands was investigated in vitro using dispersed cells. The dispersed cells were labeled with [32P]orthophosphate for 40 min prior to experimental manipulation. Subcellular fractions
-
6. Changes in protein phosphorylation in Rous sarcoma virus-transformed chicken embryo cells.
Rous sarcoma virus encodes a tyrosine-specific protein kinase (p60src) which is necessary for cell transformation. To identify substrates for this kinase, we set out to detect phosphotyrosine-containing proteins in Rous sarcoma virus-transformed chicken embryo cells, making use of the known alkali stability of phosphotyrosine. 32P-labeled phosphoproteins wer
-
7. Striatal phosphoproteins in Parkinson disease and progressive supranuclear palsy.
This study was undertaken to evaluate the levels of cAMP-regulated phosphoproteins in the striatum of patients with neurodegenerative diseases of the dopaminergic system. Postmortem samples of caudate nucleus and putamen from 24 control subjects, 23 patients with Parkinson disease, and 13 patients with progressive supranuclear palsy were studied with immunob
-
8. Identification of phosphoproteins correlated with proliferation and cell cycle arrest in Saccharomyces cerevisiae: positive and negative regulation by cAMP-dependent protein kinase.
Recent genetic and biochemical studies of two mutants of the cAMP pathway in yeast, cyr1 and bcy1, have demonstrated that cAMP-dependent protein phosphorylation plays a major regulatory role in the control of proliferation and differentiation. As a first step in examining this regulatory system in more detail and in identifying the protein substrates of cAMP
-
9. Four different classes of retroviruses induce phosphorylation of tyrosines present in similar cellular proteins.
Chicken embryo cells transformed by the related avian sarcoma viruses PRC II and Fujinami sarcoma virus, or by the unrelated virus Y73, contain three phosphoproteins not observed in untransformed cells and increased levels of up to four other phosphoproteins. These same phosphoproteins are present in increased levels in cells transformed by Rous sarcoma viru
-
10. Immunological characterization of proteins detected by phosphotyrosine antibodies in cells transformed by Rous sarcoma virus.
Phosphotyrosine antibodies were used to identify tyrosine-phosphorylated proteins in Rous sarcoma virus (RSV)-transformed chicken embryo fibroblasts. A large number of tyrosine phosphoproteins were detected. A similar set of proteins was observed in RSV-transformed murine cells. An 85,000-dalton protein, however, was present in transformed avian cells but mi
-
11. UL34, the target of the herpes simplex virus U(S)3 protein kinase, is a membrane protein which in its unphosphorylated state associates with novel phosphoproteins.
Previous studies (F. C. Purves, D. Spector, and B. Roizman, J. Virol. 65:5757-5764, 1991) have shown that the protein kinase encoded by the U(S)3 gene mediates posttranslational modification of a viral phosphoprotein with an apparent M(r) of 30,000 encoded by the UL34 gene. Here we report the following. (i) UL34 protein is not phosphorylated in cells infecte
-
12. Investigation of the Calcium-Transporting ATPases at the Endoplasmic Reticulum and Plasma Membrane of Red Beet (Beta vulgaris).
Calcium-transporting ATPases were compared in endoplasmic reticulum (ER)- and plasma membrane-enriched fractions of red beet (Beta vulgaris L.) storage tissue by measuring 45Ca uptake and calcium-dependent phosphoenzyme formation. The plasma membrane fraction was prepared by aqueous two-phase partitioning of a microsomal fraction and collecting the upper pha