Glycine Rich Proteins
Mostrando 1-12 de 158 artigos, teses e dissertações.
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1. Identification of the soybean HyPRP family and specific gene response to Asian soybean rust disease
Soybean [Glycine max (L.) Merril], one of the most important crop species in the world, is very susceptible to abiotic and biotic stress. Soybean plants have developed a variety of molecular mechanisms that help them survive stressful conditions. Hybrid proline-rich proteins (HyPRPs) constitute a family of cell-wall proteins with a variable N-terminal domain
Genet. Mol. Biol.. Publicado em: 19/04/2013
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2. Identificação e caracterização de genes codificantes de proteínas ricas em glicina ligantes de RNA em soja (Glycine max (L.) Merril)
Molecular information on plant developmental process, as well as detailed knowledge of the interaction between stress conditions and plant response to environmental factors are essential for understanding the adaptive response. Glycine-Rich Proteins (GRP) have the amino acid glycine well represented in their primary structure. The genes encoding GRPs are dev
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 2011
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3. Caracterização e expressão do gene SERK durante a indução de embriogênese somática em soja / Characterization and expression of SERK gene during induction of somatic embryogenesis in soybean
Somatic embryogenesis is a useful tool for plant propagation and a suitable model system for deciphering early events during embryo development. Molecular and genetic studies focused in plant development have reported the involvement of SERK (Somatic Embryogenesis Receptor Kinase) gene in the acquisition of embryogenic competence. In order to increase the ef
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 20/09/2010
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4. Survey of glycine-rich proteins (GRPs) in the Eucalyptus expressed sequence tag database
The occurrence of quasi-repetitive glycine-rich peptides has been reported in different organisms. Glycine-rich regions are proposed to be involved in protein-protein interactions in some mammalian protein families. In plants, a set of glycine-rich proteins (GRPs) was characterized several years ago, and since then a wealth of new GRPs have been identified.
Publicado em: 2010
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5. Survey of glycine-rich proteins (GRPs) in the Eucalyptus expressed sequence tag database (ForEST)
The occurrence of quasi-repetitive glycine-rich peptides has been reported in different organisms. Glycine-rich regions are proposed to be involved in protein-protein interactions in some mammalian protein families. In plants, a set of glycine-rich proteins (GRPs) was characterized several years ago, and since then a wealth of new GRPs have been identified.
Genetics and Molecular Biology. Publicado em: 2005
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6. A tobacco cDNA reveals two different transcription patterns in vegetative and reproductive organs
In order to identify genes expressed in the pistil that may have a role in the reproduction process, we have established an expressed sequence tags project to randomly sequence clones from a Nicotiana tabacum stigma/style cDNA library. A cDNA clone (MTL-8) showing high sequence similarity to genes encoding glycine-rich RNA-binding proteins was chosen for fur
Braz J Med Biol Res. Publicado em: 2002-08
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7. Classification, expression pattern and comparative analysis of sugarcane expressed sequences tags (ESTs) encoding glycine-rich proteins (GRPs)
Desde o isolamento da primeira proteína rica em glicina (GRP) em plantas, um grande número de novas GRPs vem sendo identificado. Seu padrão de expressão altamente específico, embora variado, em conjunto com as diferentes localizações sub-celulares de alguns dos tipos de GRPs, claramente indica que estas proteínas encontram-se envolvidas em diversos p
Genetics and Molecular Biology. Publicado em: 2001-12
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8. Glycine-rich cell wall proteins in bean: gene structure and association of the protein with the vascular system.
A single genomic clone (14 kb) isolated from bean (Phaseolus vulgaris L.) contains two genes that encode glycine-rich proteins. These genes are present as single copies in the genome, are separated by 2.85 kb and encode transcripts of 1.8 kb and 1.0 kb respectively. The encoded proteins contain 60% glycine and have amino-terminal signal peptides. The 1.8 kb
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9. Differential expression of five Arabidopsis genes encoding glycine-rich proteins.
Five cDNA clones coding for glycine-rich proteins in Arabidopsis thaliana were isolated. The corresponding genes are present in the genome as single copies. The derived protein sequences contain highly repetitive glycine-rich motifs. There is, however, little homology among them, nor with previously described glycine-rich proteins from other species. All fiv
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10. Conservation of structure and cold-regulation of RNA-binding proteins in cyanobacteria: probable convergent evolution with eukaryotic glycine-rich RNA-binding proteins.
The rbp gene family of the cyanobacterium Anabaena variabilis strain M3 consists of eight members that encode small RNA-binding proteins containing a single RNA recognition motif (RRM). Similar genes are found in the genomes of Synechocystis sp. PCC6803, Helicobacter pylori and Treponema pallidum, but are absent from the other completely sequenced prokaryoti
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11. Secretion of CyaA-PrtB and HlyA-PrtB fusion proteins in Escherichia coli: involvement of the glycine-rich repeat domain of Erwinia chrysanthemi protease B.
Protease B from Erwinia chrysanthemi was shown previously to have a C-terminal secretion signal located downstream of a domain that contains six glycine-rich repeats. This domain is conserved in all known bacterial proteins secreted by the signal peptide-independent pathway. The role of these repeats in the secretion process is controversial. We compared the
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12. Identification of the Small Protein Rich in Arginine and Glycine (SRAG): A NEWLY IDENTIFIED NUCLEOLAR PROTEIN THAT CAN REGULATE CELL PROLIFERATION*S⃞
The characterization of new proteins will aid in our explanation of normal biology and disease. Toward that goal, we describe the initial characterization of the small protein rich in arginine and glycine (SRAG). Human and mouse SRAG are 248/249-amino acid arginine- and glycine-rich proteins that are widely expressed in tissues and cell lines. Two SRAG
American Society for Biochemistry and Molecular Biology.