Sbe
Mostrando 25-36 de 65 artigos, teses e dissertações.
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25. Gruta do Salitre (MG 361): geoespeleologia e espeleotemas
Esse artigo sintetiza os estudos realizados na Gruta do Salitre, situada a 5 km de Cordisburgo, MG, e que está cadastrada sob o número MG 361 junto ao Cadastro Nacional de Cavidades da Sociedade Brasileira de Espeleologia (SBE, 1991). As atividades constaram do mapeamento topográfico parcial da caverna, descrições dos espeleotemas e da rocha hospedeira
Rem: Revista Escola de Minas. Publicado em: 2002-10
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26. Sbe2p and Sbe22p, Two Homologous Golgi Proteins Involved in Yeast Cell Wall Formation
The cell wall of fungal cells is important for cell integrity and cell morphogenesis and protects against harmful environmental conditions. The yeast cell wall is a complex structure consisting mainly of mannoproteins, glucan, and chitin. The molecular mechanisms by which the cell wall components are synthesized and transported to the cell surface are poorly
The American Society for Cell Biology.
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27. The Two Genes Encoding Starch-Branching Enzymes IIa and IIb Are Differentially Expressed in Barley1
The sbeIIa and sbeIIb genes, encoding starch-branching enzyme (SBE) IIa and SBEIIb in barley (Hordeum vulgare L.), have been isolated. The 5′ portions of the two genes are strongly divergent, primarily due to the 2064-nucleotide-long intron 2 in sbeIIb. The sequence of this intron shows that it contains a retro-transposon-like element. Expression of
American Society of Plant Physiologists.
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28. Identification of Mutator Insertional Mutants of Starch-Branching Enzyme 2a in Corn1
Starch-branching enzymes (SBE) break the α-1,4 linkage of starch, re-attaching the chain to a glucan chain by an α-1,6 bond, altering starch structure. SBEs also facilitate starch accumulation by increasing the number of non-reducing ends on the growing chain. In maize (Zea mays), three isoforms of SBE have been identified. To examine the function of the S
American Society of Plant Physiologists.
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29. Maize Starch-Branching Enzyme Isoforms and Amylopectin Structure. In the Absence of Starch-Branching Enzyme IIb, the Further Absence of Starch-Branching Enzyme Ia Leads to Increased Branching1
Previous studies indicated that the deficiency of starch-branching enzyme (SBE) Ia in the single mutant sbe1a∷Mu (sbe1a) has no impact on endosperm starch structure, whereas the deficiency of SBEIIb in the ae mutant is well known to reduce the branching of starch. We hypothesized that in maize (Zea mays) endosperm, the function of SBEIIb is predominant to
American Society of Plant Biologists.
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30. Independent genetic control of maize starch-branching enzymes IIa and IIb. Isolation and characterization of a Sbe2a cDNA.
In maize (Zea mays L.) three isoforms of starch-branching enzyme (SBEI, SBEIIa, and SBEIIb) are involved in the synthesis of amylopectin, the branched component of starch. To isolate a cDNA encoding SBEIIa, degenerate oligonucleotides based on domains highly conserved in Sbe2 family members were used to amplify Sbe2-family cDNA from tissues lacking SBEIIb ac
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31. Tissue-Specific Autoregulation of the stat3 Gene and Its Role in Interleukin-6-Induced Survival Signals in T Cells
Signal transducer and activator of transcription 3 (STAT3) mediates signals of various growth factors and cytokines, including interleukin-6 (IL-6). In certain IL-6-responsive cell lines, the stat3 gene is autoregulated by STAT3 through a composite IL-6 response element in its promoter that contains a STAT3-binding element (SBE) and a cyclic AMP-responsive e
American Society for Microbiology.
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32. Specimen Storage in Transport Medium and Detection of Group B Streptococci by Culture
Recovery of group B streptococci (GBS) was assessed in 1,204 vaginorectal swabs stored in Amies transport medium at 4 or 21°C for 1 to 4 days either by direct inoculation onto Granada agar (GA) or by culture in blood agar (BA) and GA after a selective broth enrichment (SBE) step. Following storage at 4°C, GBS detection in GA was not affected after 72 h by
American Society for Microbiology.
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33. Allelic Analysis of the Maize amylose-extender Locus Suggests That Independent Genes Encode Starch-Branching Enzymes IIa and IIb.
Starch branching enzymes (SBE) catalyze the formation of [alpha]-1,6-glucan linkages in the biosynthesis of starch. Three distinct SBE isoforms have been identified in maize (Zea mays L.) endosperm, SBEI, IIa, and IIb. Independent genes have been identified that encode maize SBEI and IIb; however, it has remained controversial as to whether SBEIIa and IIb re
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34. Overexpression of Sbe2p, a Golgi Protein, Results in Resistance to Caspofungin in Saccharomyces cerevisiae
Caspofungin inhibits the synthesis of 1, 3-β-d-glucan, an essential cell wall target in fungi. Genetic studies in the model yeast Saccharomyces cerevisiae have shown that mutations in FKS1 and FKS2 genes result in caspofungin resistance. However, direct demonstration of the role of gene overexpression in caspofungin resistance has been lacking. We transform
American Society for Microbiology.
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35. Identification of cis-Acting Elements Important for Expression of the Starch-Branching Enzyme I Gene in Maize Endosperm1
The genes encoding the starch-branching enzymes (SBE) SBEI, SBEIIa, and SBEIIb in maize (Zea mays) are differentially regulated in tissue specificity and during kernel development. To gain insight into the regulatory mechanisms controlling their expression, we analyzed the 5′-flanking sequences of Sbe1 using a transient gene expression system. Although the
American Society of Plant Physiologists.
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36. Functional Interactions between Heterologously Expressed Starch-Branching Enzymes of Maize and the Glycogen Synthases of Brewer's Yeast1
Starch-branching enzymes (SBEs) catalyze the formation of α(1→6) glycoside bonds in glucan polymers, thus, affecting the structure of amylopectin and starch granules. Two distinct classes of SBE are generally conserved in higher plants, although the specific role(s) of each isoform in determination of starch structure is not clearly understood. This study
American Society of Plant Physiologists.