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Relevant bibliographies by topics / Caenorhabditis elegans Caenorhabditis elegans Caenorhabditis elegans Proteins Intestines

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Academic literature on the topic 'Caenorhabditis elegans Caenorhabditis elegans Caenorhabditis elegans Proteins Intestines'

Author: Grafiati

Published: 4 June 2021

Last updated: 10 February 2022

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Journal articles on the topic "Caenorhabditis elegans Caenorhabditis elegans Caenorhabditis elegans Proteins Intestines"

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Chauhan, Veeren M., and David I. Pritchard. "Haematophagic Caenorhabditis elegans." Parasitology 146, no. 3 (October 25, 2018): 314–20. http://dx.doi.org/10.1017/s0031182018001518.

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AbstractCaenorhabditis elegans is a free-living nematode that resides in soil and typically feeds on bacteria. We postulate that haematophagic C. elegans could provide a model to evaluate vaccine responses to intestinal proteins from hematophagous nematode parasites, such as Necator americanus. Human erythrocytes, fluorescently labelled with tetramethylrhodamine succinimidyl ester, demonstrated a stable bright emission and facilitated visualization of feeding events with fluorescent microscopy. C. elegans were observed feeding on erythrocytes and were shown to rupture red blood cells upon capture to release and ingest their contents. In addition, C. elegans survived equally on a diet of erythrocytes. There was no statistically significant difference in survival when compared with a diet of Escherichia coli OP50. The enzymes responsible for the digestion and detoxification of haem and haemoglobin, which are key components of the hookworm vaccine, were found in the C. elegans intestine. These findings support our postulate that free-living nematodes could provide a model for the assessment of neutralizing antibodies to current and future hematophagous parasite vaccine candidates.

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Baylis, H. A., and K. Goyal. "TRPM channel function in Caenorhabditis elegans." Biochemical Society Transactions 35, no. 1 (January 22, 2007): 129–32. http://dx.doi.org/10.1042/bst0350129.

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The nematode Caenorhabditis elegans contains over 20 genes for TRP (transient receptor potential) channels which include members of all of the subclasses identified in mammalian cells. These proteins include three members of the TRPM (TRP melastatin) family: gon-2 (abnormal gonad development), gtl-1 (gon-2-like 1) and gtl-2. Although studies of these genes are at an early stage, we are beginning to understand their functions in the life of C. elegans. Mutations in gon-2 have defective gonad formation because of failures in the cell division of the somatic gonad precursor cells. gon-2 and gtl-1 are both expressed in the intestine of the animal. Experiments on gon-2,gtl-1 double mutants show that they have a severe growth defect that is ameliorated by the addition of high levels of Mg2+ to the growth medium. gon-2,gtl-1 double mutants have defective magnesium homoeostasis and also have altered sensitivity to toxic levels of Ni2+. Furthermore gon-2 mutants have reduced levels of IORCa (outwardly rectifying calcium current) in the intestinal cells. Thus these two channels appear to play an important role in cation homoeostasis in C. elegans. In addition, perturbing the function of gon-2 and gtl-1 disrupts the ultradian defecation rhythm in C. elegans, suggesting that these channels play an important role in regulating this calcium-dependent rhythmic process. The tractability of C. elegans as an experimental animal and its amenability to techniques such as RNAi (RNA interference) and in vivo imaging make it an excellent system for an integrative analysis of TRPM function.

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Yuet, Kai P., Meenakshi K. Doma, John T. Ngo, Michael J. Sweredoski, Robert L. J. Graham, Annie Moradian, Sonja Hess, Erin M. Schuman, Paul W. Sternberg, and David A. Tirrell. "Cell-specific proteomic analysis in Caenorhabditis elegans." Proceedings of the National Academy of Sciences 112, no. 9 (February 17, 2015): 2705–10. http://dx.doi.org/10.1073/pnas.1421567112.

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Proteomic analysis of rare cells in heterogeneous environments presents difficult challenges. Systematic methods are needed to enrich, identify, and quantify proteins expressed in specific cells in complex biological systems including multicellular plants and animals. Here, we have engineered a Caenorhabditis elegans phenylalanyl-tRNA synthetase capable of tagging proteins with the reactive noncanonical amino acid p-azido-l-phenylalanine. We achieved spatiotemporal selectivity in the labeling of C. elegans proteins by controlling expression of the mutant synthetase using cell-selective (body wall muscles, intestinal epithelial cells, neurons, and pharyngeal muscle) or state-selective (heat-shock) promoters in several transgenic lines. Tagged proteins are distinguished from the rest of the protein pool through bioorthogonal conjugation of the azide side chain to probes that permit visualization and isolation of labeled proteins. By coupling our methodology with stable-isotope labeling of amino acids in cell culture (SILAC), we successfully profiled proteins expressed in pharyngeal muscle cells, and in the process, identified proteins not previously known to be expressed in these cells. Our results show that tagging proteins with spatiotemporal selectivity can be achieved in C. elegans and illustrate a convenient and effective approach for unbiased discovery of proteins expressed in targeted subsets of cells.

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Li, Ying-Xiu, Nan-Nan Wang, Yan-Xia Zhou, Chun-Guo Lin, Jing-Shan Wu, Xin-Qi Chen, Guan-Jun Chen, and Zong-Jun Du. "Planococcus maritimus ML1206 Isolated from Wild Oysters Enhances the Survival of Caenorhabditis elegans against Vibrio anguillarum." Marine Drugs 19, no. 3 (March 12, 2021): 150. http://dx.doi.org/10.3390/md19030150.

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With the widespread occurrence of aquaculture diseases and the broad application of antibiotics, drug-resistant pathogens have increasingly affected aquatic animals’ health. Marine probiotics, which live under high pressure in a saltwater environment, show high potential as a substitute for antibiotics in the field of aquatic disease control. In this study, twenty strains of non-hemolytic bacteria were isolated from the intestine of wild oysters and perch, and a model of Caenorhabditis elegans infected by Vibrio anguillarum was established. Based on the model, ML1206, which showed a 99% similarity of 16S rRNA sequence to Planococcus maritimus, was selected as a potential marine probiotic, with strong antibacterial capabilities and great acid and bile salt tolerance, to protect Caenorhabditis elegans from being damaged by Vibrio anguillarum. Combined with plate counting and transmission electron microscopy, it was found that strain ML1206 could significantly inhibit Vibrio anguillarum colonization in the intestinal tract of Caenorhabditis elegans. Acute oral toxicity tests in mice showed that ML1206 was safe and non-toxic. The real-time qPCR results showed a higher expression level of genes related to the antibacterial peptide (ilys-3) and detoxification (ugt-22, cyp-35A3, and cyp-14A3) in the group of Caenorhabditis elegans protected by ML1206 compared to the control group. It is speculated that ML1206, as a potential probiotic, may inhibit the infection caused by Vibrio anguillarum through stimulating Caenorhabditis elegans to secrete antibacterial effectors and detoxification proteins. This paper provides a new direction for screening marine probiotics and an experimental basis to support the potential application of ML1206 as a marine probiotic in aquaculture.

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Espelt, Maria V., Ana Y. Estevez, Xiaoyan Yin, and Kevin Strange. "Oscillatory Ca2+ Signaling in the Isolated Caenorhabditis elegans Intestine." Journal of General Physiology 126, no. 4 (September 26, 2005): 379–92. http://dx.doi.org/10.1085/jgp.200509355.

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Defecation in the nematode Caenorhabditis elegans is a readily observable ultradian behavioral rhythm that occurs once every 45–50 s and is mediated in part by posterior body wall muscle contraction (pBoc). pBoc is not regulated by neural input but instead is likely controlled by rhythmic Ca2+ oscillations in the intestinal epithelium. We developed an isolated nematode intestine preparation that allows combined physiological, genetic, and molecular characterization of oscillatory Ca2+ signaling. Isolated intestines loaded with fluo-4 AM exhibit spontaneous rhythmic Ca2+ oscillations with a period of ∼50 s. Oscillations were only detected in the apical cell pole of the intestinal epithelium and occur as a posterior-to-anterior moving intercellular Ca2+ wave. Loss-of-function mutations in the inositol-1,4,5-trisphosphate (IP3) receptor ITR-1 reduce pBoc and Ca2+ oscillation frequency and intercellular Ca2+ wave velocity. In contrast, gain-of-function mutations in the IP3 binding and regulatory domains of ITR-1 have no effect on pBoc or Ca2+ oscillation frequency but dramatically increase the speed of the intercellular Ca2+ wave. Systemic RNA interference (RNAi) screening of the six C. elegans phospholipase C (PLC)–encoding genes demonstrated that pBoc and Ca2+ oscillations require the combined function of PLC-γ and PLC-β homologues. Disruption of PLC-γ and PLC-β activity by mutation or RNAi induced arrhythmia in pBoc and intestinal Ca2+ oscillations. The function of the two enzymes is additive. Epistasis analysis suggests that PLC-γ functions primarily to generate IP3 that controls ITR-1 activity. In contrast, IP3 generated by PLC-β appears to play little or no direct role in ITR-1 regulation. PLC-β may function instead to control PIP2 levels and/or G protein signaling events. Our findings provide new insights into intestinal cell Ca2+ signaling mechanisms and establish C. elegans as a powerful model system for defining the gene networks and molecular mechanisms that underlie the generation and regulation of Ca2+ oscillations and intercellular Ca2+ waves in nonexcitable cells.

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Mosquera, Jose Verdezoto, Meghan C. Bacher, and James R. Priess. "Nuclear lipid droplets and nuclear damage in Caenorhabditis elegans." PLOS Genetics 17, no. 6 (June 16, 2021): e1009602. http://dx.doi.org/10.1371/journal.pgen.1009602.

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Fat stored in the form of lipid droplets has long been considered a defining characteristic of cytoplasm. However, recent studies have shown that nuclear lipid droplets occur in multiple cells and tissues, including in human patients with fatty liver disease. The function(s) of stored fat in the nucleus has not been determined, and it is possible that nuclear fat is beneficial in some situations. Conversely, nuclear lipid droplets might instead be deleterious by disrupting nuclear organization or triggering aggregation of hydrophobic proteins. We show here that nuclear lipid droplets occur normally in C. elegans intestinal cells and germ cells, but appear to be associated with damage only in the intestine. Lipid droplets in intestinal nuclei can be associated with novel bundles of microfilaments (nuclear actin) and membrane tubules that might have roles in damage repair. To increase the normal, low frequency of nuclear lipid droplets in wild-type animals, we used a forward genetic screen to isolate mutants with abnormally large or abundant nuclear lipid droplets. Genetic analysis and cloning of three such mutants showed that the genes encode the lipid regulator SEIP-1/seipin, the inner nuclear membrane protein NEMP-1/Nemp1/TMEM194A, and a component of COPI vesicles called COPA-1/α-COP. We present several lines of evidence that the nuclear lipid droplet phenotype of copa-1 mutants results from a defect in retrieving mislocalized membrane proteins that normally reside in the endoplasmic reticulum. The seip-1 mutant causes most germ cells to have nuclear lipid droplets, the largest of which occupy more than a third of the nuclear volume. Nevertheless, the nuclear lipid droplets do not trigger apoptosis, and the germ cells differentiate into gametes that produce viable, healthy progeny. Thus, our results suggest that nuclear lipid droplets are detrimental to intestinal nuclei, but have no obvious deleterious effect on germ nuclei.

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Kostich, M., A. Fire, and D. M. Fambrough. "Identification and molecular-genetic characterization of a LAMP/CD68-like protein from Caenorhabditis elegans." Journal of Cell Science 113, no. 14 (July 15, 2000): 2595–606. http://dx.doi.org/10.1242/jcs.113.14.2595.

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Lysosome associated membrane proteins (LAMPs) constitute a family of vertebrate proteins located predominantly in lysosomes, with lesser amounts present in endosomes and at the cell surface. Macrosialin/CD68s are similar to LAMPs in their subcellular distribution and amino acid sequence and presumed structure across the carboxyl terminal two thirds of their length. The functions of LAMPs and CD68s are not known. In the present study, a bioinformatics approach was used to identify a Caenorhabditis elegans protein (LMP-1) with sequence and presumed structural similarity to LAMPs and CD68s. LMP-1 appears to be the only membrane protein in C. elegans that carries a GYXX(phi) vertebrate lysosomal targeting sequence at its C terminus (where (phi) is a large, hydrophobic residue). LMP-1 was found to be present from early embryonic stages through adulthood and to be predominantly localized at the periphery of a population of large, membrane-bound organelles, called granules, that are seen throughout the early embryo but in later stages are restricted to the cells of the intestine. Analysis of an LMP-1 deficient C. elegans mutant revealed that LMP-1 is not required for viability under laboratory conditions, but the absence of LMP-1 leads to an alteration in intestinal granule populations, with apparent loss of one type of granule.

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Sornda, Thanet, Marina Ezcurra, Carina Kern, Evgeniy R. Galimov, Catherine Au, Yila de la Guardia, and David Gems. "Production of YP170 Vitellogenins Promotes Intestinal Senescence in Caenorhabditis elegans." Journals of Gerontology: Series A 74, no. 8 (March 15, 2019): 1180–88. http://dx.doi.org/10.1093/gerona/glz067.

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Abstract During aging, etiologies of senescence cause multiple pathologies, leading to morbidity and death. To understand aging requires identification of these etiologies. For example, Caenorhabditis elegans hermaphrodites consume their own intestinal biomass to support yolk production, which in later life drives intestinal atrophy and ectopic yolk deposition. Yolk proteins (YPs; vitellogenins) exist as three abundant species: YP170, derived from vit-1–vit-5; and YP115 and YP88, derived from vit-6. Here, we show that inhibiting YP170 synthesis leads to a reciprocal increase in YP115/YP88 levels and vice versa, an effect involving posttranscriptional mechanisms. Inhibiting YP170 production alone, despite increasing YP115/YP88 synthesis, reduces intestinal atrophy as much as inhibition of all YP synthesis, which increases life span. By contrast, inhibiting YP115/YP88 production alone accelerates intestinal atrophy and reduces life span, an effect that is dependent on increased YP170 production. Thus, despite copious abundance of both YP170 and YP115/YP88, only YP170 production is coupled to intestinal atrophy and shortened life span. In addition, increasing levels of YP115/YP88 but not of YP170 increases resistance to oxidative stress; thus, longevity resulting from reduced vitellogenin synthesis is not attributable to oxidative stress resistance.

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Elle, Ida C., Karina T. Simonsen, Louise C. B. Olsen, Pernille K. Birck, Sidse Ehmsen, Simon Tuck, Thuc T. Le, and Nils J. Færgeman. "Tissue- and paralogue-specific functions of acyl-CoA-binding proteins in lipid metabolism in Caenorhabditis elegans." Biochemical Journal 437, no. 2 (June 28, 2011): 231–41. http://dx.doi.org/10.1042/bj20102099.

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ACBP (acyl-CoA-binding protein) is a small primarily cytosolic protein that binds acyl-CoA esters with high specificity and affinity. ACBP has been identified in all eukaryotic species, indicating that it performs a basal cellular function. However, differential tissue expression and the existence of several ACBP paralogues in many eukaryotic species indicate that these proteins serve distinct functions. The nematode Caenorhabditis elegans expresses seven ACBPs: four basal forms and three ACBP domain proteins. We find that each of these paralogues is capable of complementing the growth of ACBP-deficient yeast cells, and that they exhibit distinct temporal and tissue expression patterns in C. elegans. We have obtained loss-of-function mutants for six of these forms. All single mutants display relatively subtle phenotypes; however, we find that functional loss of ACBP-1 leads to reduced triacylglycerol (triglyceride) levels and aberrant lipid droplet morphology and number in the intestine. We also show that worms lacking ACBP-2 show a severe decrease in the β-oxidation of unsaturated fatty acids. A quadruple mutant, lacking all basal ACBPs, is slightly developmentally delayed, displays abnormal intestinal lipid storage, and increased β-oxidation. Collectively, the present results suggest that each of the ACBP paralogues serves a distinct function in C. elegans.

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Chen, Carlos Chih-Hsiung, Peter J. Schweinsberg, Shilpa Vashist, Darren P. Mareiniss, Eric J. Lambie, and Barth D. Grant. "RAB-10 Is Required for Endocytic Recycling in the Caenorhabditis elegans Intestine." Molecular Biology of the Cell 17, no. 3 (March 2006): 1286–97. http://dx.doi.org/10.1091/mbc.e05-08-0787.

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The endocytic pathway of eukaryotes is essential for the internalization and trafficking of macromolecules, fluid, membranes, and membrane proteins. One of the most enigmatic aspects of this process is endocytic recycling, the return of macromolecules (often receptors) and fluid from endosomes to the plasma membrane. We have previously shown that the EH-domain protein RME-1 is a critical regulator of endocytic recycling in worms and mammals. Here we identify the RAB-10 protein as a key regulator of endocytic recycling upstream of RME-1 in polarized epithelial cells of the Caenorhabditis elegans intestine. rab-10 null mutant intestinal cells accumulate abnormally abundant RAB-5-positive early endosomes, some of which are enlarged by more than 10-fold. Conversely most RME-1-positive recycling endosomes are lost in rab-10 mutants. The abnormal early endosomes in rab-10 mutants accumulate basolaterally recycling transmembrane cargo molecules and basolaterally recycling fluid, consistent with a block in basolateral transport. These results indicate a role for RAB-10 in basolateral recycling upstream of RME-1. We found that a functional GFP-RAB-10 reporter protein is localized to endosomes and Golgi in wild-type intestinal cells consistent with a direct role for RAB-10 in this transport pathway.

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Dissertations / Theses on the topic "Caenorhabditis elegans Caenorhabditis elegans Caenorhabditis elegans Proteins Intestines"

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Leung, Benjamin Hong Nien. "Intestinal morphogenesis in the Caenorhabditis elegans embryo /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/5073.

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Ou, Gangwei. "Human intestinal epithelial cells in innate immunity : interactions with normal microbiota and pathogenic bacteria." Doctoral thesis, Umeå : Umeå University, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-18388.

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Benner, Jacqueline [Verfasser], Hannelore [Akademischer Betreuer] Daniel, Dirk [Akademischer Betreuer] Haller, and Michael [Akademischer Betreuer] Schemann. "Amino acid homeostasis in Caenorhabditis elegans lacking the intestinal peptide transporter PEPT-1 and identification of PEPT-1 modulator proteins / Jacqueline Benner. Gutachter: Hannelore Daniel ; Dirk Haller ; Michael Schemann. Betreuer: Hannelore Daniel." München : Universitätsbibliothek der TU München, 2011. http://d-nb.info/1056935480/34.

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Williams, Corey L. "Analysis of cystic kidney disease-related genes in Caenorhabditis elegans." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2009. https://www.mhsl.uab.edu/dt/2009p/williams.pdf.

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Goldmark, Jesse P. "How and why to stop and wait : a graduate education in mechanisms and benefits of suspended animation /." Thesis, Connect to this title online; UW restricted, 2006. http://hdl.handle.net/1773/5040.

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Harrington, Laura Susanna. "Investigating the function of centaurin proteins from 'Caenorhabditis elegans'." Thesis, University of Cambridge, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.421653.

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Nettell, Julia Joy. "Studies of the Rh (Rhesus)-related proteins in Caenorhabditis elegans." Thesis, University of Bristol, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.340354.

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Stear, Jeffrey Hamilton. "Studies of chromosome structure and movement in C. elegans /." Thesis, Connect to this title online; UW restricted, 2003. http://hdl.handle.net/1773/5056.

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Yigit, Erbay. "The Argonaute Family of Genes in Caenorhabditis Elegans: a Dissertation." eScholarship@UMMS, 2007. https://escholarship.umassmed.edu/gsbs_diss/328.

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Members of the Argonaute family of proteins, which interact with small RNAs, are the key players of RNAi and other related pathways. The C. elegans genome encodes 27 members of the Argonaute family. During this thesis research, we sought to understand the functions of the members of this gene family in C. elegans. Among the Argonaute family members, rde-1 and alg-1/2have previously been shown to be essential for RNAi and development, respectively. In this work, we wanted to assign functions to the remaining members of this large family of proteins. Here, we describe the phenotype of 31 deletion alleles representing all of the previously uncharacterized Argonaute members. In addition to rde-1, our analysis revealed that two other Argonaute members csr-1 and prg-1 are also essential for development. csr-1 is partially required for RNAi, and essential for proper chromosome segregation. prg-1, a member of PIWI subfamily of Argonaute genes, exhibits reduced brood size and temperature-sensitive sterile phenotype, implicating that it is required for germline maintenance. Additionally, we showed that RDE-1 interacts with trigger-derived sense and antisense siRNAs (primary siRNAs) to initiate RNAi, while several other Argonaute proteins, SAGO-1, SAGO-2, and perhaps others, functioning redundantly, interact with amplified siRNAs (secondary siRNAs) to mediate downstream silencing. Moreover, our analysis uncovered that another member of Argonaute gene family, ergo-1, is essential for the endogenous RNAi pathway. Furthermore, we built an eight-fold Argonaute mutant, MAGO8, and analyzed its developmental phenotype and sensitivity to RNAi. Our analysis revealed that the genes deleted in the MAGO8 mutant function redundantly with each other, and are required for RNAi and the maintenance of the stem cell totipotency.

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Tenlen, Jennifer R. "Linking PAR polarity proteins to cell fate regulation : analysis of MEX-5 localization in Caenorhabditis elegans embryos /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/5009.

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Books on the topic "Caenorhabditis elegans Caenorhabditis elegans Caenorhabditis elegans Proteins Intestines"

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Protein metabolism and homeostasis in aging. New York, N.Y: Springer Science+Business Media, 2010.

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Mehra, Arun. Protein-protein interaction between FEM-3 and TRA-2A, two sex determining proteins of Caenorhabditis elegans. Ottawa: National Library of Canada, 1994.

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Interactions between two caenorhabditis elegans sex determining proteins: HER-1 and TRA-2A. Ottawa: National Library of Canada, 2000.

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Wang, Yanqing. Analysis of the role of HSP110 in the development and physiology of caenorhabditis elegans: A thesis in biology. 2004.

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Gaudet, Jeffrey P. C. Molecular analysis of the role of the FEM proteins in Caenorhabditis elegans sex determination. 2000.

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Tavernarakis, Nektarios. Protein Metabolism and Homeostasis in Aging. Springer, 2016.

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Book chapters on the topic "Caenorhabditis elegans Caenorhabditis elegans Caenorhabditis elegans Proteins Intestines"

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Nomura, Kazuya, Sayaka Akiyoshi, Ayako Matsuda, and Kazuko H. Nomura. "Glycosaminoglycans and Glycosylphosphatidylinositol-Anchor Proteins in Development of Caenorhabditis elegans Caenorhabditis elegans." In Glycoscience: Biology and Medicine, 817–24. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_159.

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Simske, Jeffrey S., and Jeff Hardin. "Claudin Family Proteins in Caenorhabditis elegans." In Methods in Molecular Biology, 147–69. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-185-7_11.

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Culetto, Emmanuel, Marta Grauso, Didier Combes, Yann Fedon, Rita Romani, Jean-Pierre Toutant, and Martine Arpagaus. "Four Acetylcholinesterase Genes in the Nematodes caenorhabditis Elegans and Caenorhabditis Briggsae." In Structure and Function of Cholinesterases and Related Proteins, 87–92. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_12.

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Wilson, Kristy J., Hiroshi Qadota, and Guy M. Benian. "Immunofluorescent Localization of Proteins in Caenorhabditis elegans Muscle." In Methods in Molecular Biology, 171–81. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-343-1_10.

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Combes, Didier, Emmanuel Culetto, Marta Grauso, Rita Romani, Yann Fedon, Jean-Pierre Toutant, and Martine Arpagaus. "Four Acetylcholinesterase Genes in the Nematode Caenorhabditis Elegans." In Structure and Function of Cholinesterases and Related Proteins, 136–37. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_31.

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Grauso, Marta, Emmanuel Culetto, Didier Combes, Yann Fedon, Jean-Pierre Toutant, and Martine Arpagaus. "Four Acetylcholinesterase Genes in the Nematode Caenorhabditis Elegans." In Structure and Function of Cholinesterases and Related Proteins, 138–39. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4899-1540-5_32.

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Brenner, John L., and Tim Schedl. "Indirect Immunofluorescence of Proteins in Oogenic Germ Cells of Caenorhabditis elegans." In Methods in Molecular Biology, 9–17. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3795-0_2.

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Peter, E., and M. Candido. "The Small Heat Shock Proteins of the Nematode Caenorhabditis elegans: Structure, Regulation and Biology." In Small Stress Proteins, 61–78. Berlin, Heidelberg: Springer Berlin Heidelberg, 2002. http://dx.doi.org/10.1007/978-3-642-56348-5_4.

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Largeau, Céline, and Renaud Legouis. "Correlative Light and Electron Microscopy to Analyze LC3 Proteins in Caenorhabditis elegans Embryo." In Methods in Molecular Biology, 281–93. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8873-0_18.

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Bastiani, Carol A., Melvin I. Simon, and Paul W. Sternberg. "Control of Caenorhabditis Elegans Behaviour and Development by G Proteins Big and Small." In Cell Signalling in Prokaryotes and Lower Metazoa, 195–242. Dordrecht: Springer Netherlands, 2004. http://dx.doi.org/10.1007/978-94-017-0998-9_7.

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Conference papers on the topic "Caenorhabditis elegans Caenorhabditis elegans Caenorhabditis elegans Proteins Intestines"

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Stenflo, J., A.-K. öhlin, Å. Lundvall, and B. Dahlback. "β-HYDROXY ASPARTIC ACID AND ft-HYDROXYASPARAGINE IN THEEGF-HOMOLOGY REGIONS OF PROTEIN C AND PROTEINS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643995.

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Abstract:

The amino acid sequence has been determined for all of the vitamin K-dependent proteins and the gene structure is known for some of them. These findings have shown the proteins to consist of four clearly discernible domains, except protein S which has six domains. The protein domains seem to be coded on separate exons (Foster, D. C. et. al. 1985 Proc. Natl. Acad. Sci. USA 82,4673). The vitamin K-dependent γ-carboxyglutamic acid (Gla) containing domain isthe common structural denominator of the members of this protein family. In addition, all of these proteins except prothrombin contain domains that are homologous to the precursor of the epidermal growth factor (EGF). Such domains arealso found in proteins that are not vitamin K-dependent, such as the low density lipoprotein receptor, thrombomodulin, factor XII, plasminogen, the tissue type plasminogen activator, urokinase and the complement protein Clr. The vitamin K-dependent proteins can be dividedinto three groups. Factors VII, IX, X, protein C and protein Z form one group, which in addition to the Gla-region have two EGF-homology regions and one domain that is homologous to the serine proteases. Prothrombin has two 'kringle' structures and a serine protease domain and constitutes a group of its own. Protein S is also unique in that it has four EGF-homology regions and a COOH-terminal region that is homologous to the sexual hormone binding globulin (see poster by Edenbrand et. al.).Recently a posttranslationally modified amino acid, B-hydroxyaspatic acid (Hya), was identified in position 71 in the NH2-terminal EGF-homology region ofbovine protein C. The amino acid is formed by hydroxylation of aspartic acid. It has also been identified in the corresponding positions in factors VII, IX,X and protein Z (i. e. proteins which like protein C have two EGF-homology regions each). In protein S the N2-terminal of four EGF-homology regions has hydroxy lated aspartic acid .whereas the following three EGF-like domains have B-hydroxyasparagine. The nucleotide sequence codes for asparagine in the three latter positions. Neither vitamin K nor vitamin C seem to be involvedin the formation of the two hydroxylated amino acids. Recently, Hya was identified in acid hydrolysates of the complement protein Clr. Hya and Hyn have onlybeen found in domains that are homologous to the EGF precursor. In an attempt to identify the structural requirement of the hydroxylating enzyme, we have compared the sequences of EGF-homology regions that contain Hya or Hyn with the corresponding sequences that have been shown not to contain the modified amino acids. The domains that have Hya or Hyn have the consensus sequence Cx xxxx xCxC. This sequence has been found in three EGF-like domains in the EGF-precursor, in two in the LDL-receptor and in two in thrombomodulin. Furthermore, the neurogenic Notch locus in Drosophila melanogaster codes for 36 EGF-homolgy regions, 22 of which contain the consensussequence, whereas the Lin-12 locus in Caenorhabditis elegans codes for at least 11 EGF-like repeats, two of which comply with the consensus sequence. Whether any of these proteins contain Hya orHyn is not yet known with certainty.It has been hypothesized that Hya isinvolved in the Gla independent Ca2+binding of factors IX, X and protein C. In an attempt to resolve this issue, we have isolated the EGF-homology region from human protein C and been able to demonstrate that it binds Ca2+ (see poster by öhlin and Stenflo). However, we do not yet know whether Hya is directly involved in the Ca2+binding.

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