Calreticulin
Mostrando 1-12 de 106 artigos, teses e dissertações.
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1. Proteomic analysis of excretory-secretory products from young adults of Angiostrongylus cantonensis
BACKGROUND Angiostrongyliasis is caused by the nematode Angiostrongylus cantonensis and can lead to eosinophilic meningitis and meningoencephalitis in humans. The young adult worms play central pathogenic roles in the central nervous system (CNS); however, the underlying mechanism is unclear. Excretory-secretory products (ESPs) are good investigation targe
Mem. Inst. Oswaldo Cruz. Publicado em: 19/06/2019
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2. Complement system contributes to modulate the infectivity of susceptible TcI strains of Trypanosoma cruzi
BACKGROUND Trypanosoma cruzi is a protozoan parasite and an etiological agent of Chagas disease. There is a wide variability in the clinical outcome of its infection, ranging from asymptomatic individuals to those with chronic fatal mega syndromes. Both parasite and host factors, as well as their interplay, are thought to be involved in the process. OBJECT
Mem. Inst. Oswaldo Cruz. Publicado em: 19/02/2018
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3. Somatic mutations of calreticulin in a Brazilian cohort of patients with myeloproliferative neoplasms
Rev. Bras. Hematol. Hemoter.. Publicado em: 2015-06
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4. Efeito da resistência de Spodoptera frugiperda (J.E.Smith, 1797) (Lepidoptera: Noctuidae) a lambda-cyhalothrin na interação com o milho geneticamente modificado (MON810) e na resposta imunológica ao parasitismo por Campoletis af / Effect of resistance of Spodoptera frugiperda (J.E. Smith, 1797) (Lepidoptera: Noctuidae) to lambda-cyhalothrin on the interaction with genetically modified maize (MON810) and the immune response to parasitization by Campoletis aff. flavicincta (Hymenoptera: Ichneumonidae)
Fitness costs of insect resistance to insecticides can be exploited by integrating other pest control strategies in Integrated Pest Management (IPM) programs. The objective of this research was to evaluate the existence of fitness costs associated with the resistance of Spodoptera frugiperda (J. E. Smith) (Lepidoptera: Noctuidae) to the pyrethroid insecticid
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 24/05/2012
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5. CLONAGEM, CARACTERIZAÇÃO E EXPRESSÃO HETERÓLOGA DE UMA CALNEXINA HOMÓLOGA DO FUNGO PATOGÊNICO Paracoccidioides brasiliensis / Cloning, characterization and heterologue expression of a calnexin homologue from the pathogenic fungus Paracoccidioides brasiliensis. / CLONAGEM, CARACTERIZAÇÃO E EXPRESSÃO HETERÓLOGA DE UMA CALNEXINA HOMÓLOGA DO FUNGO PATOGÊNICO Paracoccidioides brasiliensis / Cloning, characterization and heterologue expression of a calnexin homologue from the pathogenic fungus Paracoccidioides brasiliensis.
We report the cloning of a Paracoccidioides brasiliensis cDNA, here named PbCnx, encoding the homologue of the endoplasmic reticulum calnexin. This chaperone specifically recognizes monoglucosylated glycoproteins in the endoplasmic reticulum. Thus, it is an essential component of the folding process of nascent secreted glycoproteins. PbCnx open reading frame
Publicado em: 2006
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6. Evaluation of the immunologic response from synthetic mimetic peptides of total larva proteins of Boophilus microplus tick (Acari: ixodidae) in mice and bovines / Avaliação da resposta imunológica a peptídeos sintéticos mimetopos de proteínas totais de larvas do carrapato Boophilus microplus (Acari: ixodidae) em camundongos e bovinos
O carrapato Boophilus microplus é um dos mais importantes artrópodes que parasitam os bovinos, causando grandes prejuízos à pecuária mundial pelos seus efeitos diretos e indiretos. A aplicação de produtos químicos é o principal método de controle deste parasita, mas em função das desvantagens desta prática, o uso de vacinas é uma boa alternativ
Publicado em: 2004
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7. Suppressive Roles of Calreticulin in Prostate Cancer Growth and Metastasis
Calreticulin is an essential, multifunctional Ca2+-binding protein that participates in the regulation of intracellular Ca2+ homeostasis, cell adhesion, and chaperoning. Calreticulin is abundantly expressed and regulated by androgens in prostate epithelial cells. Given the importance of both calreticulin in multiple essential cellular activities and androgen
American Society for Investigative Pathology.
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8. Identification of calreticulin as a rubella virus RNA binding protein.
Previously, we observed that sequences at the 3' end of rubella virus (RV) genomic RNA that form a stable stem-loop structure are necessary for initiation of RNA replication. A cytosolic protein found in Vero 76 cells (simian origin) specifically bound to the 3' (+)-stem-loop sequence. In the present study, we have purified the RNA binding protein and identi
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9. BiP and calreticulin form an abundant complex that is independent of endoplasmic reticulum stress
BiP is found in association with calreticulin, both in the presence and absence of endoplasmic reticulum stress. Although the BiP-calreticulin complex can be disrupted by ATP, several properties suggest that the calreticulin associated with BiP is neither unfolded nor partially or improperly folded. (1) The complex is stable in vivo and does not dissociate d
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10. Calreticulin recognizes misfolded HLA-A2 heavy chains
Our studies investigated functional interactions between calreticulin, an endoplasmic reticulum chaperone, and major histocompatibility complex (MHC) class I molecules. Using in vitro thermal aggregation assays, we established that calreticulin can inhibit heat-induced aggregation of soluble, peptide-deficient HLA-A2 purified from supernatants of insect cell
The National Academy of Sciences.
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11. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.
The soluble, calcium-binding protein calreticulin shares high sequence homology with calnexin, a transmembrane chaperone of glycoprotein folding. Our experiments demonstrated that calreticulin, like calnexin, associated transiently with numerous newly synthesized proteins in the endoplasmic reticulum. The population of proteins that bound to calreticulin was
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12. Trypanosoma cruzi Calreticulin Is a Lectin That Binds Monoglucosylated Oligosaccharides but Not Protein Moieties of Glycoproteins
Trypanosoma cruzi is a protozoan parasite that belongs to an early branch in evolution. Although it lacks several features of the pathway of protein N-glycosylation and oligosaccharide processing present in the endoplasmic reticulum of higher eukaryotes, it displays UDP-Glc:glycoprotein glucosyltransferase and glucosidase II activities. It is herewith report
The American Society for Cell Biology.