Relevant bibliographies by topics / Fucose

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  2. Dissertations / Theses
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Academic literature on the topic 'Fucose'

Author: Grafiati
Published: 4 June 2021
Last updated: 4 May 2024

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Journal articles on the topic "Fucose"

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Becerra, Jimmy E., María J. Yebra, and Vicente Monedero. "An l-Fucose Operon in the Probiotic Lactobacillus rhamnosus GG Is Involved in Adaptation to Gastrointestinal Conditions." Applied and Environmental Microbiology 81, no. 11 (March 27, 2015): 3880–88. http://dx.doi.org/10.1128/aem.00260-15.

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ABSTRACTl-Fucose is a sugar present in human secretions as part of human milk oligosaccharides, mucins, and other glycoconjugates in the intestinal epithelium. The genome of the probioticLactobacillus rhamnosusGG (LGG) carries a gene cluster encoding a putativel-fucose permease (fucP),l-fucose catabolic pathway (fucI,fucK,fucU, andfucA), and a transcriptional regulator (fucR). The metabolism ofl-fucose in LGG results in 1,2-propanediol production, and theirfucIandfucPmutants displayed a severe and mild growth defect onl-fucose, respectively. Transcriptional analysis revealed that thefucgenes are induced byl-fucose and subject to a strong carbon catabolite repression effect. This induction was triggered by FucR, which acted as a transcriptional activator necessary for growth onl-fucose. LGG utilized fucosyl-α1,3-N-acetylglucosamine and contrarily to other lactobacilli, the presence offucgenes allowed this strain to use thel-fucose moiety. InfucIandfucRmutants, but not infucPmutant,l-fucose was not metabolized and it was excreted to the medium during growth on fucosyl-α1,3-N-acetylglucosamine. Thefucgenes were induced by this fucosyl-disaccharide in the wild type and thefucPmutant but not in afucImutant, showing that FucP does not participate in the regulation offucgenes and thatl-fucose metabolism is needed for FucR activation. Thel-fucose operon characterized here constitutes a new example of the many factors found in LGG that allow this strain to adapt to the gastrointestinal conditions.
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Liu, Xixi, Zhexian Zhang, Hui Mao, Pin Wang, Zhichuang Zuo, Li Gao, Xiang Shi, Ronghua Yin, Na Gao, and Jinhua Zhao. "Characterization of the Hydrolysis Kinetics of Fucosylated Glycosaminoglycan in Mild Acid and Structures of the Resulting Oligosaccharides." Marine Drugs 18, no. 6 (May 29, 2020): 286. http://dx.doi.org/10.3390/md18060286.

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Mild acid hydrolysis is a common method for the structure analysis of fucosylated glycosaminoglycan (FG). In this work, the effects of acid hydrolysis on the structure of FG from S. variegatus (SvFG) and the reaction characteristic were systemically studied. The degree of defucosylation (DF) and molecular weights (Mw) of partial fucosylated glycosaminoglycans (pFs) were monitored by 1H NMR and size-exclusion chromatography, respectively. The kinetic plots of DF, degree of desulfation (DS) from fucose branches, and degree of hydrolysis (DH) of the backbone are exponentially increased with time, indicating that acid hydrolysis of SvFG followed a first-order kinetics. The kinetic rate constants kDF, kDS, and kDH were determined to be 0.0223 h-1, 0.0041 h-1, and 0.0005 h-1, respectively. The structure of the released sulfated fucose branches (FucS) from SvFG and HfFG (FG from H. fuscopunctata) was characterized by 1D/2D NMR spectroscopy, suggesting the presence of six types of fucose: α/β Fuc2S4S, Fuc3S4S, Fuc3S, Fuc4S, Fuc2S, and Fuc. The Fuc3S4S was more susceptible to acid than Fuc2S4S, and that the sulfate ester in position of O-2 and O-3 than in O-4 of fucose. The structure characteristic of pF18 indicated the cleavage of backbone glycosidic bonds. The APTT prolonged activity reduced with the decrease of the DF and Mw of the pFs, and became insignificant when its DF was 87% with Mw of 3.5 kDa.
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Pérez-Escalante, Emmanuel, Luis Guillermo González-Olivares, Araceli Castañeda-Ovando, Alma Elizabeth Cruz-Guerrero, John F. Trant, Wendolyne López-Orozco, Luis Humberto Mendoza-Huizar, and Sergio Alatorre-Santamaría. "An In Silico Approach to Enzymatic Synthesis of Fucooligosaccharides Using α-l-Fucosidase from Thermotoga maritima." Chemistry Proceedings 3, no. 1 (November 14, 2020): 10. http://dx.doi.org/10.3390/ecsoc-24-08303.

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Fucooligosaccharides comprise the primary group of human milk oligosaccharides. Due to their beneficial properties, a series of synthetic methods have been proposed to obtain them. Enzymatic methods show great promise, and α-l-fucosidase from Thermotoga maritima has emerged as a powerful catalyst for their production. Nonetheless, the enzyme’s limited substrate scope has delayed its wider application. The present work aims to compare the relative reactivity of fucose, pNP-fucose, and ethyl-fucose, while also exploring the molecular interactions of these fucosyl-donors with the enzyme through a combination DFT and docking analysis. The HOMO-LUMO band gaps range from −7.14571 to −4.24429 eV, with α/β-pNP-fucose and α-fucose being the three most reactive compounds. Moderate association energies between −6.4 to −5.5 kcal·mol−1 were found in the docking analysis, with α-pNP-fucose and both anomers of ethyl-fucose demonstrating the poorest affinity. In the case of α/β-lactose affinity to the β-fucose/enzyme complex, no significant differences were shown. We conclude that the best fucosyl-donors for transfucosylation are those that maintain an enzyme affinity and reactivity similar to pNP-fucose.
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Ojeda, Kristylea J., Jodie M. Box, and K. Dale Noel. "Genetic Basis for Rhizobium etli CE3 O-Antigen O-Methylated Residues That Vary According to Growth Conditions." Journal of Bacteriology 192, no. 3 (November 30, 2009): 679–90. http://dx.doi.org/10.1128/jb.01154-09.

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ABSTRACT The Rhizobium etli CE3 O antigen is a fixed-length heteropolymer with O methylation being the predominant type of sugar modification. There are two O-methylated residues that occur, on average, once per complete O antigen: a multiply O-methylated terminal fucose and 2-O methylation of a fucose residue within a repeating unit. The amount of the methylated terminal fucose decreases and the amount of 2-O-methylfucose increases when bacteria are grown in the presence of the host plant, Phaseolus vulgaris, or its seed exudates. Insertion mutagenesis was used to identify open reading frames required for the presence of these O-methylated residues. The presence of the methylated terminal fucose required genes wreA, wreB, wreC, wreD, and wreF, whereas 2-O methylation of internal fucoses required the methyltransferase domain of bifunctional gene wreM. Mutants lacking only the methylated terminal fucose, lacking only 2-O methylation, or lacking both the methylated terminal fucose and 2-O methylation exhibited no other lipopolysaccharide structural defects. Thus, neither of these decorations is required for normal O-antigen length, transport, or assembly into the final lipopolysaccharide. This is in contrast to certain enteric bacteria in which the absence of a terminal decoration severely affects O-antigen length and transport. R. etli mutants lacking only the methylated terminal fucose were not altered in symbiosis with host Phaseolus vulgaris, whereas mutants lacking only 2-O-methylfucose exhibited a delay in nodule development during symbiosis. These results support previous conclusions that the methylated terminal fucose is dispensable for symbiosis, whereas 2-O methylation of internal fucoses somehow facilitates early events in symbiosis.
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Nuñez, Samantha, Maria Barra, and Daniel Garrido. "Developing a Fluorescent Inducible System for Free Fucose Quantification in Escherichia coli." Biosensors 13, no. 3 (March 15, 2023): 388. http://dx.doi.org/10.3390/bios13030388.

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L-Fucose is a monosaccharide abundant in mammalian glycoconjugates. In humans, fucose can be found in human milk oligosaccharides (HMOs), mucins, and glycoproteins in the intestinal epithelium. The bacterial consumption of fucose and fucosylated HMOs is critical in the gut microbiome assembly of infants, dominated by Bifidobacterium. Fucose metabolism is important for the production of short-chain fatty acids and is involved in cross-feeding microbial interactions. Methods for assessing fucose concentrations in complex media are lacking. Here we designed and developed a molecular quantification method of free fucose using fluorescent Escherichia coli. For this, low- and high-copy plasmids were evaluated with and without the transcription factor fucR and its respective fucose-inducible promoter controlling the reporter gene sfGFP. E. coli BL21 transformed with a high copy plasmid containing pFuc and fucR displayed a high resolution across increasing fucose concentrations and high fluorescence/OD values after 18 h. The molecular circuit was specific against other monosaccharides and showed a linear response in the 0–45 mM range. Adjusting data to the Hill equation suggested non-cooperative, simple regulation of FucR to its promoter. Finally, the biosensor was tested on different concentrations of free fucose and the supernatant of Bifidobacterium bifidum JCM 1254 supplemented with 2-fucosyl lactose, indicating the applicability of the method in detecting free fucose. In conclusion, a bacterial biosensor of fucose was validated with good sensitivity and precision. A biological method for quantifying fucose could be useful for nutraceutical and microbiological applications, as well as molecular diagnostics.
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Chan, Pan F., Karen M. O'Dwyer, Leslie M. Palmer, Jennifer D. Ambrad, Karen A. Ingraham, Chi So, Michael A. Lonetto, et al. "Characterization of a Novel Fucose-Regulated Promoter (PfcsK) Suitable for Gene Essentiality and Antibacterial Mode-of-Action Studies in Streptococcus pneumoniae." Journal of Bacteriology 185, no. 6 (March 15, 2003): 2051–58. http://dx.doi.org/10.1128/jb.185.6.2051-2058.2003.

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ABSTRACT The promoter of the Streptococcus pneumoniae putative fuculose kinase gene (fcsK), the first gene of a novel fucose utilization operon, is induced by fucose and repressed by glucose or sucrose. When the streptococcal polypeptide deformylase (PDF) gene (def1, encoding PDF) was placed under the control of P fcsK , fucose-dependent growth of the S. pneumoniae (P fcsK ::def1) strain was observed, confirming the essential nature of PDF in this organism. The mode of antibacterial action of actinonin, a known PDF inhibitor, was also confirmed with this strain. The endogenous fuculose kinase promoter is a tightly regulated, titratable promoter which will be useful for target validation and for confirmation of the mode of action of novel antibacterial drugs in S. pneumoniae.
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Robles-Gómez, Laura, Paula Sáez-Espinosa, Eliana Marina López-Viloria, Andrea López-Botella, Jon Aizpurua, and María José Gómez-Torres. "Quantification and Topographical Distribution of Terminal and Linked Fucose Residues in Human Spermatozoa by Using Field Emission Scanning Electron Microscopy (FE-SEM)." International Journal of Molecular Sciences 22, no. 21 (November 4, 2021): 11947. http://dx.doi.org/10.3390/ijms222111947.

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The modification of sperm glycocalyx is an essential process during sperm capacitation. The presence and redistribution of terminal and linked fucose have been described during in vitro capacitation in humans. However, the influence of the capacitation time on the quantification and localization of terminal and linked fucose is still unknown. In this study, the quantitative and qualitative changes in fucosyl residues during different in vitro capacitation times (1 and 4 h), are simultaneously characterized by using Aleuria aurantia (AAA) lectin–gold labelling and high-resolution field emission scanning electron microscopy (FE-SEM) in human sperm. A significant decrease was found in the number of terminal fucose registered in the whole sperm head during the in vitro capacitation. Nevertheless, the quantification of fucose residues after 1 h of in vitro capacitation was very similar to those found after 4 h. Therefore, the changes observed in terminal and linked fucose during capacitation were not time-dependent. Furthermore, the comprehensive analysis of the topographic distribution showed the preferential fucosyl location in the acrosomal region and the presence of distinct clusters distributed over the head in all the studied conditions. Overall, these findings corroborate the validity of FE-SEM combined with gold labelling to register changes in surface molecules during in vitro sperm capacitation.
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Tollefsen, S. E., and J. L. Rosenblum. "Role of terminal fucose residues in clearance of human glycosylated alpha-amylase." American Journal of Physiology-Gastrointestinal and Liver Physiology 255, no. 3 (September 1, 1988): G374—G381. http://dx.doi.org/10.1152/ajpgi.1988.255.3.g374.

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Human glycosylated alpha-amylase contains a single biantennary N-linked oligosaccharide that terminates with the structure Fuc alpha 1,3(Gal beta 1,4)GlcNAc. To examine the role of terminal fucose in the clearance of alpha-amylase, we used lectin affinity chromatography to isolate an alpha-amylase fraction that contains two terminal fucoses (one in each branch of the oligosaccharide) and a fraction from which both terminal fucoses have been enzymatically removed. In the rat, the rate of clearance of the radioiodinated fraction with terminal fucoses is rapid (t1/2 = 12 min) and is slowed by mannosylated but not galactosylated bovine serum albumin. The rate of clearance of the radioiodinated alpha-amylase fraction with no terminal fucoses is also rapid (t1/2 = 9.5 min), but the clearance is now slowed by galactosylated bovine serum albumin. These findings indicate that the fucosylated and defucosylated alpha-amylase fractions are recognized by different carbohydrate-specific receptors. We conclude therefore that terminal fucose is the recognition marker that effects the physiological clearance of this glycoprotein.
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Kim, In Jung, and Kyoung Heon Kim. "Thermophilic l-fucose isomerase from Thermanaeromonas toyohensis for l-fucose synthesis from l-fuculose." Process Biochemistry 96 (September 2020): 131–37. http://dx.doi.org/10.1016/j.procbio.2020.05.017.

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Ropartz, David, Lery Marion, Mathieu Fanuel, Jasna Nikolic, Murielle Jam, Robert Larocque, Elizabeth Ficko-Blean, Gurvan Michel, and Helene Rogniaux. "In-depth structural characterization of oligosaccharides released by GH107 endofucanase MfFcnA reveals enzyme subsite specificity and sulfated fucan substructural features." Glycobiology 32, no. 4 (December 4, 2021): 276–88. http://dx.doi.org/10.1093/glycob/cwab125.

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Abstract The extracellular matrix of brown algae represents an abundant source of fucose-containing sulfated polysaccharides (FCSPs). FCSPs include sulfated fucans, essentially composed of fucose, and highly heterogeneous fucoidans, comprising various monosaccharides. Despite a range of potentially valuable biological activities, the structures of FCSPs are only partially characterized and enzymatic tools leading to their deconstruction are rare. Previously, the enzyme MfFcnA was isolated from the marine bacterium Mariniflexile fucanivorans and biochemically characterized as an endo-α-1 → 4-l-fucanase, the first member of glycoside hydrolase family 107. Here, MfFcnA was used as an enzymatic tool to deconstruct the structure of the sulfated fucans from Pelvetia canaliculata (Fucales brown alga). Oligofucans released by MfFcnA at different time points were characterized using mass spectrometry coupled with liquid chromatography and tandem mass spectrometry through Charge Transfer Dissociation. This approach highlights a large diversity in the structures released. In particular, the analyses show the presence of species with less than three sulfates per two fucose residues. They also reveal species with monosaccharides other than fucose and the occurrence of laterally branched residues. Precisely, the lateral branching is either in the form of a hexose accompanied by a trisulfated fucose nearby, or of a side chain of fucoses with a pentose as the branching point on the polymer. Overall, the results indicate that the structure of sulfated fucans from P. canaliculata is more complex than expected. They also reveal the interesting capacity of MfFcnA to accommodate different substrates, leading to structurally diverse oligofucan products that potentially could be screened for bioactivities.
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Dissertations / Theses on the topic "Fucose"

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Smelt, Kathryn Helena. "Synthesis of L-fucose analogues." Thesis, University of Oxford, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.362080.

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Yuan, Kun. "Effects of defucosylation on human breast cancer cells." Thesis, Birmingham, Ala. : University of Alabama at Birmingham, 2007. https://www.mhsl.uab.edu/dt/2010r/yuan.pdf.

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McCabe, N. R. "Training and fucose metabolism in chick brain." Thesis, Open University, 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.355645.

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Doknic, D. "SYNTHESIS OF FUCOSE-BASED LIGANDS FOR DC-SIGN." Doctoral thesis, Università degli Studi di Milano, 2012. http://hdl.handle.net/2434/203241.

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DC-SIGN is a C-type lectin that is expressed in dendritic cells and that is involved in a number of infection processes such as HIV or Ebola. Within the scope of this work a library of monovalent, fucose-based ligands was synthesised to block DC-SIGN. The structures originate from three scaffolds containing 2-aminocyclohexane carboxylic acid in different configurations. The compounds were tested by means of SPR competition assays and were found to be similar to the natural ligand Lewis X in terms of affinity for DC-SIGN. On the one hand, the most potent ligand, and on the other hand, the most accessible ligand were selected for further functionalisation and polyvalent presentation by the attachment to dendrimers. The increased valency resulted in an improved affinity by up to one order of magnitude in comparison with the monomeric structure. Moreover, the functionalised monomers were used for the fabrication of glycan arrays and were screened with several commercially available lectins. Strongest binding could be detected with the lectin from the bacterial phytopathogen Ralstonia solanacearum.
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Sanz, Sender Silvia. "Synthesis and biological function of fucose in Plasmodium falciparum." Doctoral thesis, Universitat de Barcelona, 2017. http://hdl.handle.net/10803/587108.

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Malaria is a parasitic disease caused by Plasmodium parasites and it is transmitted by female Anopheles mosquito. P. falciparum has a complex life cycle that includes important stages in two different hosts: a mosquito and a human. The transmission between the human and the mosquito host also involves the transition between asexual and sexual forms of the parasites. Glycobiology includes the study of carbohydrate metabolism and glycoconjugate (glycoprotein and glycolipid) structures. Protozoan parasites synthesize different glycoconjugates for protection and to respond to changes in the environment. Glycoconjugates coat the parasite surface with carbohydrates generally different from the host ones. They are crucial for parasite virulence and survival. Until very recently the only glycan structures described in P. falciparum were the GPI-anchors, however other glycan structures have been found in the past few years as the N-glycans or C-mannosylation. The glycome consists in the complete set of glycosylations that an organism or a cell produces at a certain time point, therefore the description of the parasite glycome may help to understand better the host- pathogen interactions in parasitic diseases. Sugar nucleotides are activated forms of monosaccharides that are the donors of glycosyltransferases to form glyconjugates. They can be synthesized by a de novo pathway that consists in the bioconversion of an existing sugar or sugar nucleotide; or by a salvage pathway that involves an activation and a further pyrophosphorylation. The identification and quantification of the sugar nucleotides present in malaria parasites may help to describe its glycosylation profile. The first paper presented in the thesis describes the identification and quantification of the sugar nucleotides present in the parasite, among which we found: UDP-Glc, UDP-Gal, UDP-GlcNAc, GDP-Man and GDP-Fuc. We also investigated the salvage pathways present in the parasite but we couldn’t elucidate the presence of a fucose salvage pathway. Plasmodium parasites conserve homolog genes for the de novo biosynthetic pathway of GDP-Fuc: GMD and FS. We were able to prove the in vitro activity of GMD and FS enzymes and to show that both enzymes are required for the synthesis of fucose. GMD and FS are expressed along the intraerythrocytic life cycle and both enzymes localize in the cytoplasm of the parasite, as well as other parasite enzymes related with carbohydrate metabolism. The expression of a putative O-fucosyltransferase (PoFUT2) present in the parasite genome, together with the uptake of GDP-Fuc by parasite extracts suggested the presence of a fucose containing glycan. In the second paper, we characterized the enzymes responsible for the synthesis of GDP-Fuc, GMD and FS. We disrupted both genes in the parasite and analyzed the sugar nucleotide content present in the parasite. After GMD and FS disruption, GDP-Fuc was still detected in the parasite and no evidence of salvage mechanism was found. We described indirect evidence of a fucose containing glycan that was abrogated after the disruption of GMD. The last work here presented (not yet published) tries to characterize the enzyme that is probably responsible for the transfer of fucose to the glycoconjugate. We disrupted, by double crossover recombination, PoFUT2 gene in the human and in the rodent malaria parasite. The disruption of PoFUT2 does not have any significant effect for the viability and growth of the parasite along the parasite cycle in the human and in the mosquito host. These works open the door to new research lines to find an alternative pathway for obtaining fucose or GDP-Fuc. Obtaining evidence of the glycosylation state of PoFUT2 mutants and the characterization of other possible glycosylation reaction present in the parasite are other research topics to investigate.
La malaria está causada por el parásito Plasmodium y se transmite mediante hembras del mosquito Anopheles. La glicobiología es el estudio de los procesos relacionados con los carbohidratos y las estructuras glicoconjugadas que forman. Los parásitos sintetizan glicoconjugados o proteínas de unión a glicanos, y muchas veces se encargan de mediar las interacciones huésped-patógeno. Los azúcares nucleótidos son formas activadas de monosacáridos que son usados por glicosiltransferasas para formar glicoconjugados. La identificación y cuantificación de estos azúcares nucleótidos en el parásito de la malaria puede contribuir a la definición de su perfil de glicosilación. El primer trabajo presentado en la tesis permitió identificar los azúcares nucleótidos presentes en el parásito, así como la posible presencia de un glicoconjugado que contenga fucosa, sintetizado a partir de la actividad O-fucosiltransferasa de una proteína homóloga anotada en el genoma del parásito, PoFUT2. El siguiente trabajo permitió caracterizar las enzimas implicadas en la síntesis de la GDP-fucosa, GMD y FS. Este artículo nos permitió mostrar evidencias indirectas de la presencia del glicococonjugado que contiene fucosa. A partir de la disrupción de los genes de biosíntesis descubrimos que el contenido de GDP-fucosa en parásitos mutantes no variaba con respecto a los parásitos salvajes. Sin embargo, la síntesis del gliconjugado sí que se reducía. El tercer trabajo (sin publicar) se centra en la caracterización de la enzima encargada de transferir la fucosa al glicoconjugado. La disrupción de PoFUT2 no parece tener ningún efecto en la viabilidad y crecimiento del parásito a lo largo del ciclo de éste en el humano y en el mosquito. Estos trabajos abren la puerta a nuevas investigaciones para descubrir una vía alternativa de obtención de GDP-Fucosa. La obtención de evidencias del estado de glicosilación de los mutantes de PoFUT2 y la caracterización de otras posibles glicosilaciones son otros temas a investigar.
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Bandini, Giulia. "Studies on fucosylation in Trypanosoma brucei." Thesis, University of Dundee, 2011. https://discovery.dundee.ac.uk/en/studentTheses/c74554c1-f4d3-4bb3-aa31-899fcf507e11.

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The biosynthesis of GDP-Fucose, the activated donor for fucose, has been recently shown to be essential in the parasite Trypanosoma brucei. Fucose is a common sugar modification on eukaryotic glycan structures, but it has not been well described in trypanosomatids. To elucidate the role of fucose in T. brucei we searched for putative fucosyltransferases in this parasite. A single putative T. brucei fucosyltransferase (TbFT) was identified and recombinantly expressed in Escherichia coli. The protein was active and structural characterization of its reaction product identified it as a GDP-Fuc: ß-D-galactose a-1,2-fucosyltransferase with preference for Galß1,3GlcNAc containing structures as glycan acceptors. A procyclic form conditional null mutant for TbFT was generated and this glycosyltransferase shown to be essential for parasite growth in vitro, with the mutant cells displaying a slightly abnormal morphology and an apparent reduction in the surface high molecular weight glycoconjugate complex. Here we also describe the various experimental approaches that were used to try to identify the fucosylated glycocojugates in T. brucei. Lastly, to better understand the biosynthesis of GDP-Mannose, the starting metabolite for the biosynthesis of GDP-Fuc, we biochemically characterized T. brucei phosphomannomutase (TbPMM). Here we show this enzyme could interconvert not only mannose-phosphates, but also glucose-phosphates.
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Muiry, Jennifer Anne Ross. "The bacterial transport systems for L-rhamnose and L-fucose." Thesis, University of Cambridge, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315190.

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Yao, David C. "Roles of O-fucose Molecules in Notch Signaling and Hematopoiesis." Case Western Reserve University School of Graduate Studies / OhioLINK, 2011. http://rave.ohiolink.edu/etdc/view?acc_num=case1311379342.

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Weidner, Stefan. "Enzymatische Synthese von GDP-[beta]-L-Fucose [GDP-beta-L-Fucose] ausgehend von D-Mannose Klonierung, Expression und Charakterisierung von Enzymen aus nicht-pathogenen Enterobacteriaceae /." [S.l. : s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=972659331.

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Staib, Lena [Verfasser], Thilo M. [Akademischer Betreuer] [Gutachter] Fuchs, and Hannelore [Gutachter] Daniel. "Investigation of propanediol and fucose degradation by Salmonella Typhimurium / Lena Staib ; Gutachter: Hannelore Daniel, Thilo M. Fuchs ; Betreuer: Thilo M. Fuchs." München : Universitätsbibliothek der TU München, 2016. http://d-nb.info/1121206808/34.

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Books on the topic "Fucose"

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Černoušková, Dagmar. Orbis pictus Bohuslava Fuchse: Orbis pictus von Bohuslav Fuchs = Orbis pictus de Bohuslav Fuchs = Orbis pictus of Bohuslav Fuchs. Brno: Muzeum města Brna, 2012.

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Pinelli, Dominique. U Fucone. La Tour d'Aigues: Editions de l'Aube, 1998.

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Luder, Gustav. Schlaue fuchse, stolze hahne: Fabelhaftes - kurzprosa. Hannover: Moorburg, 1986.

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Arbeitman, Yoël L., ed. Fucus. Amsterdam: John Benjamins Publishing Company, 1988. http://dx.doi.org/10.1075/cilt.58.

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Riedel, Michael S. Fuchs. London: Koenig Books, 2017.

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Heidenreich, Gert. Fuchse Jagen: Epilog auf das Jahr 1968. Munich: Piper, 1987.

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Kubinszky, Mihály. Bohuslav Fuchs. Budapest: Akadémiai Kiadó, 1985.

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Fuchs, Eckehard. Eckehard Fuchs. Edited by Schmidt Johannes 1969- and Roedel Anke. Dresden: Ed. Azur, 2009.

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Mihály, Kubinszky. Bohuslav Fuchs. Berlin: Henschelverlag Kunst und Gesellschaft, 1986.

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Goethe, Johann Wolfgang von. Reineke Fuchs. Köln: Anaconda, 2010.

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Book chapters on the topic "Fucose"

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Schomburg, Dietmar, and Dörte Stephan. "Fucose-1-phosphate guanylyltransferase." In Enzyme Handbook, 625–27. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59025-2_111.

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Renkonen, Risto. "Fucose-1-Phosphate Guanylyltransferase (FPGT)." In Handbook of Glycosyltransferases and Related Genes, 1631–35. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54240-7_112.

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Bakker, Hans, Angel Ashikov, Francoise H. Routier, and Rita Gerardy-Schahn. "GDP-Fucose Transporter 1 (SLC35C1)." In Handbook of Glycosyltransferases and Related Genes, 1403–11. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54240-7_38.

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Matsumoto, Kenjiroo, Akira Ishio, and Kenji Matsuno. "O-Fucose Glycan in Drosophila Notch Signaling." In Glycoscience: Biology and Medicine, 1–7. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54836-2_163-1.

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Matsumoto, Kenjiroo, Akira Ishio, and Kenji Matsuno. "O-Fucose Glycan in Drosophila Notch Signaling." In Glycoscience: Biology and Medicine, 841–47. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54841-6_163.

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Ogorek, Christiane, Ingo Jordan, Volker Sandig, and Hans Henning von Horsten. "Fucose-Targeted Glycoengineering of Pharmaceutical Cell Lines." In Antibody Engineering, 507–17. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-974-7_29.

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Kannagi, Reiji. "Fucosyltransferase 6. GDP-Fucose Lactosamine α3-Fucosyltransferase (FUT6)." In Handbook of Glycosyltransferases and Related Genes, 559–71. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54240-7_80.

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Kannagi, Reiji. "Fucosyltransferase 5. GDP-Fucose Lactosamine α3/4-Fucosyltransferase (FUT5)." In Handbook of Glycosyltransferases and Related Genes, 549–58. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54240-7_79.

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Ihara, Hideyuki, Hiroki Tsukamoto, Jianguo Gu, Eiji Miyoshi, Naoyuki Taniguchi, and Yoshitaka Ikeda. "Fucosyltransferase 8. GDP-Fucose N-Glycan Core α6-Fucosyltransferase (FUT8)." In Handbook of Glycosyltransferases and Related Genes, 581–96. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54240-7_59.

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Kudo, Takashi, and Hisashi Narimatsu. "Fucosyltransferase 4. GDP-Fucose Lactosamine α1,3-Fucosyltransferase. Myeloid Specific (FUT4)." In Handbook of Glycosyltransferases and Related Genes, 541–47. Tokyo: Springer Japan, 2014. http://dx.doi.org/10.1007/978-4-431-54240-7_95.

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Conference papers on the topic "Fucose"

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Al-Samarra, Esraa Ali Abdul Karim, and Rafah Razooq Hameed Al-Samarrai. "Evaluation of the correlation between D-dimer and total L-fucose, fucose binding protein and fucose binding lipids in type 2 diabetes patients infected with COVID-19." In International Conference of Chemistry and Petrochemical Techniques (ICCPT). AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0095332.

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Arzhanova, E. L. "L-FUCOSE EFFECT ON DISRUPTIONS IN MITOCHONDRIAL FUNCTION AND METABOLISM OF PERITONEAL MACROPHAGES OF MUC2–/–MICE." In X Международная конференция молодых ученых: биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-289.

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L-fucose is a monosaccharide present in various glycolipids and glycoproteins and may participate in signaling processes of both epithelial and immune cells, in particular macrophages. We studied the metabolic and functional differences of peritoneal macrophages derived from a model of IBD and control mice before and after L-fucose treatment in vitro.
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Singh, Sudhir, Kuntal Pal, Elliot Ensink, Jessica Yadav, Doron Kletter, Marshall Bern, Anand Mehta, Karsten Melcher, and Brian B. Haab. "Abstract B31: Development of fucose based pancreatic cancer biomarkers using modified lectins." In Abstracts: AACR Special Conference on Pancreatic Cancer: Innovations in Research and Treatment; May 18-21, 2014; New Orleans, LA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.panca2014-b31.

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Braster, Rens, Remco Visser, Gestur Vidarsson, and Marjolein van Egmond. "Abstract A02: The art of omission: Low fucose antibodies enhance tumor cell clearance in vivo." In Abstracts: AACR Special Conference: Tumor Immunology and Immunotherapy: A New Chapter; December 1-4, 2014; Orlando, FL. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/2326-6074.tumimm14-a02.

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Kato, Junji, Rishu Takimoto, Takahiro Osuga, Michihiro Ono, Masahiro Hirakawa, Makoto Yoshida, Yasushi Sato, and Fumito Tamura. "Abstract 4463: Targeting SN38 delivery to gastrointestinal cancer cells using a fucose-bound nanoparticle approach." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4463.

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Listinsky, JJ, GP Siegal, and CM Listinsky. "P5-07-04: Is a-L-Fucose Overexpressed on Cells of Aggressive Human Breast Cancers?" In Abstracts: Thirty-Fourth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 6‐10, 2011; San Antonio, TX. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/0008-5472.sabcs11-p5-07-04.

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Kerr, Sheena C., Stephen D. Carrington, Michaela Wimmerova, Iwona Bucior, Joanne N. Engel, and John V. Fahy. "Inhibiting Fucose Binding Lectins As An Anti-Adhesion And Anti-Infection Strategy For Pseudomonas Airway Infections." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a2468.

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Yang, Yurui, Hongbin Lan, Huawei Zhu, and Yiran Zhu. "The Investigation of P7 Peptide Delivery Targeting Cdc24 in Ras-driven Pancreatic Cancer by L-fucose-bound Liposome." In The International Conference on Biomedical Engineering and Bioinformatics. SCITEPRESS - Science and Technology Publications, 2022. http://dx.doi.org/10.5220/0011251700003443.

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Ibrahim, Waleed Satar, and Rafah Razooq Hameed Al-Samarrai. "Evaluation the correlation between serum fucose and lipid profile in sera of patients with dyslipidemia in Samarra city." In 1ST SAMARRA INTERNATIONAL CONFERENCE FOR PURE AND APPLIED SCIENCES (SICPS2021): SICPS2021. AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0121797.

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Listinsky, JJ, GP Siegal, and CM Listinsky. "P2-18-06: Conventional Trastuzumab Is an Antagonist of Natural Killer Cells: Making the Case for Fucose-Depleted Trastuzumab." In Abstracts: Thirty-Fourth Annual CTRC‐AACR San Antonio Breast Cancer Symposium‐‐ Dec 6‐10, 2011; San Antonio, TX. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/0008-5472.sabcs11-p2-18-06.

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Reports on the topic "Fucose"

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Spiegel, Yitzhak, Michael McClure, Itzhak Kahane, and B. M. Zuckerman. Characterization of the Phytophagous Nematode Surface Coat to Provide New Strategies for Biocontrol. United States Department of Agriculture, November 1995. http://dx.doi.org/10.32747/1995.7613015.bard.

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Chemical composition and biological role of the surface coat (SC) of the root-knot nematodes, Meloidogyne spp. are described. SC proteins of M. incognita race 3 infective juveniles (J2) were characterized by electrophoresis and western blotting of extracts from radioiodine and biotin-labelled nematodes. J2 labelled with radioiodine and biotin released 125I and biotin-labelled molecules into water after 20 hours incubation, indicating that SC proteins may be loosely attached to the nematode. Antiserum to the principal protein reacted with the surface of live J2 and with surface proteins previously separated by electrophoresis. Human red blood cells (HRBC) adhered to J2 of several tylenchid nematodes over the entire nematode body. HRBC adhered also to nylon fibers coated with SC extracted from M. javanica J2; binding was Ca++/Mg++ dependent, and decreased when the nylon fibers were coated with bovine serum albumin, or pre-incubated with fucose and mannose. These experiments support a working hypothesis that RBC adhesion involves carbohydrate moieties of HRBC and carbohydrate-recognition domain(s) (CRD) distributed on the nematode surface. To our knowledge, this is the first report of a surface CRD i the phylum Nematoda. Gold-conjugated lectins and neoglycoproteins combined with silver enhancement have been used for the detection of carbohydrates and CRD, respectively, on the SC of M. javanica J2. Biotin reagents were used to trace surface proteins, specifically, on live J2. The labile and transitory nature of the SC was demonstrated by the dynamics of HRBC adherence to detergent-treated J2, J2 at different ages or fresh-hatched J2 held at various temperatures. SC recovery was demonstrated also by a SDS-PAGE profile. Monoclonal antibodies developed to a cuticular protein of M. incognita J2 gave a slight, but significant reduction in attachment of Pasteuria penetrans spores. Spore attachment as affected by several enzymes was inconsistent: alcian blue, which specifically blocks sulfyl groups, had no afffect on spore attachment. Treatment with cationized ferritin alone or catonized ferritin following monoclonal antibody caused significant decreases in spore attachment. Those results suggest a role in attachment by negatively charged groups.
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Meade, Roger, and Linda Meade. Klaus Fuchs: The Second Confession. Office of Scientific and Technical Information (OSTI), October 2014. http://dx.doi.org/10.2172/1159562.

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Shay, H. Report on Simulations of the Royle-Sentoku-Fuchs Experiment. Office of Scientific and Technical Information (OSTI), February 2013. http://dx.doi.org/10.2172/1069000.

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Hamilton, T., T. Brown, A. Marchetti, R. Martinelli, and S. Kehl. Determination of Plutonium Activity Concentrations and 240Pu/239Pu Atom Ratios in Brown Algae (Fucus distichus) Collected from Amchitka Island, Alaska. Office of Scientific and Technical Information (OSTI), May 2005. http://dx.doi.org/10.2172/15016341.

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Edwards, Susan L., Marcus E. Berzofsky, and Paul P. Biemer. Addressing Nonresponse for Categorical Data Items Using Full Information Maximum Likelihood with Latent GOLD 5.0. RTI Press, September 2018. http://dx.doi.org/10.3768/rtipress.2018.mr.0038.1809.

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Full information maximum likelihood (FIML) is an important approach to compensating for nonresponse in data analysis. Unfortunately, only a few software packages implement FIML and even fewer have the capability to compensate for missing not at random (MNAR) nonresponse. One of these packages is Statistical Innovations’ Latent GOLD; however, the user documentation for Latent GOLD provides no mention of this capability. The purpose of this paper is to provide guidance for fitting MNAR FIML models for categorical data items using the Latent GOLD 5.0 software. By way of comparison, we also provide guidance on fitting FIML models for nonresponse missing at random (MAR) using the methods of Fuchs (1982) and Fay (1986), who incorporated item nonresponse indicators within a structural modeling framework. We compare both FIML for MAR and FIML for MNAR nonresponse models for independent and dependent variables. Also, we provide recommendations for future applications of FIML using Latent GOLD.
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Robinson, Dale. The distribution and morphology of Fucus distichus in an estuarine environment and the effect of selected ions on the uptake of inorganic carbon and nitrate. Portland State University Library, January 2000. http://dx.doi.org/10.15760/etd.3316.

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