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Tat-mediated protein delivery in living Caenorhabditis elegans
Biochemical and Biophysical Research Communications, 2007The Tat protein from HIV-1 fused with heterologous proteins traverses biological membranes in a transcellular process called: protein transduction. This has already been successfully exploited in various biological models, but never in the nematode worm Caenorhabditis elegans. TAT-eGFP or GST-eGFP proteins were fed to C.
Frédéric, Delom +3 more
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Delaying aging in Caenorhabditis elegans with protein aggregation inhibitors
Biochemical and Biophysical Research Communications, 2017Recent evidence suggests that during aging there is widespread accumulation of aggregated insoluble proteins, even in the absence of pathological conditions. Pharmacological manipulation of protein aggregation might be helpful to unveil the involvement of protein aggregates during aging, as well as to develop novel strategies to delay aging.
Karina Cuanalo-Contreras +4 more
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Protein oxidation during aging of the nematode Caenorhabditis elegans
Free Radical Biology and Medicine, 2002The nematode Caenorhabditis elegans has proven a robust genetic model for studies of aging, including the roles of oxidative stress and protein damage. In this review, we focus on the genetics of select long-lived (e.g., age-1, daf-2, daf-16) and short-lived (e.g., mev-1) mutants that have proven useful in revealing the relationships that exist among ...
Naoaki, Ishii +2 more
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The location of the major protein in Caenorhabditis elegans sperm and spermatocytes
Developmental Biology, 1982Abstract Using an affinity-purified antibody to the major sperm protein (MSP) in Caenorhabditis elegans sperm we have shown by immunofluorescence that the MSP is localized in the fibrous bodies of spermatocytes and early spermatids, in the cytoplasm of late spermatids, and in the pseudopods of spermatozoa.
S, Ward, M, Klass
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Protein glycosylation lessons from Caenorhabditis elegans
Current Opinion in Structural Biology, 2004From observations on human diseases and mutant mice, it has become clear that glycosylation plays a major role in metazoan development. Caenorhabditis elegans provides powerful tools to study this problem that are not available in men or mice. The worm has many genes homologous to mammalian genes involved in glycosylation.
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Cadherin superfamily proteins in Caenorhabditis elegans and Drosophila melanogaster
Journal of Molecular Biology, 2001The ability to form selective cell-cell adhesions is an essential property of metazoan cells. Members of the cadherin superfamily are important regulators of this process in both vertebrates and invertebrates. With the advent of genome sequencing projects, determination of the full repertoire of cadherins available to an organism is possible and here ...
E, Hill +3 more
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Tissue-specific synthesis of yolk proteins in Caenorhabditis elegans
Developmental Biology, 1983The primary site of yolk protein synthesis in the nematode, Caenorhabditis elegans, has been determined. In animals containing no gonadal cells (obtained by laser ablation of the gonadal precursor cells early in development), yolk proteins are present in abundance. This demonstrates that yolk proteins are made outside the gonad.
J, Kimble, W J, Sharrock
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Patterns of proteins synthesized during development of Caenorhabditis elegans
Developmental Biology, 1979Abstract Two-dimensional gel electrophoresis has been used to analyze proteins synthesized during postembryonic development of the nematode Caenorhabditis elegans . This organism is favorable for these studies because it has a limited number of cells, it is genetically well-defined, and its development is currently under investigation in several ...
K, Johnson, D, Hirsh
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Gene, 1999
In the free-living model nematode, Caenorhabditis elegans, a protein-folding co-transcribed gene pair has previously been described. The degree and form of trans-splicing, orientation and spacing of the genes, and the co-ordinate co-expression of protein folding catalysts in the nematode's hypodermis indicated this to be a functionally important operon.
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In the free-living model nematode, Caenorhabditis elegans, a protein-folding co-transcribed gene pair has previously been described. The degree and form of trans-splicing, orientation and spacing of the genes, and the co-ordinate co-expression of protein folding catalysts in the nematode's hypodermis indicated this to be a functionally important operon.
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Genetic Analysis of RGS Protein Function in Caenorhabditis elegans
2004Caenorhabditis elegans has close homologs or orthologs of most mammalian (RGS) and G proteins, and mutants for all the RGS and G-protein genes of C. elegans have been generated. C. elegans RGS proteins can be matched to the specific Galpha proteins they regulate in vivo by comparing the defects in animals lacking or transgenically overexpressing an RGS
Daniel L, Chase, Michael R, Koelle
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