Gdpase
Mostrando 1-6 de 6 artigos, teses e dissertações.
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1. Imunolocalização da Nucleosídeo Trifosfato Difosfohidrolase 1 (NTP Dase-1) de Trypanossoma cruzi / Immunolocalization of Nucleoside Triphosphate Difosfohidrolase 1 (NTP Dase-1) of Trypanossoma cruzi
Trypanosoma cruzi é um protozoário flagelado da Ordem Kinetoplastida, agente etiológico da Doença de Chagas. As ecto-nucleotidases da família E-NTPDases são enzimas capazes de hidrolisar nucleotídeos tri e/ou difosfatados nos seus produtos monofosfatados. Os nucleotídeos extracelulares são conhecidos como moléculas sinalizadoras envolvidas com vár
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 15/03/2010
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2. Use of Kluyveromyces lactis in the Expression of Leishmania major s GDPase. / Utilização de Kluyveromyces lactis na expressão da GDPase de Leishmania major.
The yeast Kluyveromyces lactis has a potential applicability as a host in biotechnological production of heterologous recombinant proteins of biotechnological interest. In this context the objective of this work was to express the protein of Leishmania major GDPase for biotechnology applied to human and canine leishmaniasis. The GDPase of L. major belongs to
Publicado em: 2009
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3. A Role for the Lumenal Domain in Golgi Localization of the Saccharomyces cerevisiae Guanosine Diphosphatase
Integral membrane proteins (IMPs) contain localization signals necessary for targeting to their resident subcellular compartments. To define signals that mediate localization to the Golgi complex, we have analyzed a resident IMP of the Saccharomyces cerevisiae Golgi complex, guanosine diphosphatase (GDPase). GDPase, which is necessary for Golgi-specific glyc
The American Society for Cell Biology.
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4. Topography of glycosylation in yeast: characterization of GDPmannose transport and lumenal guanosine diphosphatase activities in Golgi-like vesicles.
"Outer-chain" addition of mannose residues to yeast glycoproteins occurs in the Golgi compartment of the cell. Essential steps in this process are thought to include transport of GDPmannose from the cytoplasm into the lumen of Golgi vesicles, transfer of mannose to glycoprotein acceptors, hydrolysis of the resulting GDP to GMP, and return of GMP and inorgani
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5. GDP-Fucose Uptake into the Golgi Apparatus during Xyloglucan Biosynthesis Requires the Activity of a Transporter-Like Protein Other Than the UDP-Glucose Transporter1
The molecular mechanisms regulating hemicelluloses and pectin biosynthesis are poorly understood. An important question in this regard is how glycosyltransferases are oriented in the Golgi cisternae, and how nucleotide sugars are made available for the synthesis of the polymers. Here we show that the branching enzyme xyloglucan α,1–2 fucosyltransferase (X
American Society of Plant Physiologists.
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6. The Golgi GDPase of the Fungal Pathogen Candida albicans Affects Morphogenesis, Glycosylation, and Cell Wall Properties
Cell wall mannoproteins are largely responsible for the adhesive properties and immunomodulation ability of the fungal pathogen Candida albicans. The outer chain extension of yeast mannoproteins occurs in the lumen of the Golgi apparatus. GDP-mannose must first be transported from the cytosol into the Golgi lumen, where mannose is transferred to mannans. GDP
American Society for Microbiology.