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  • 1
    Online Resource
    Online Resource
    GM3 Signaling (2020)
    Singapore :Springer Nature Singapore :
    Details
    Keywords: Molecular genetics. ; Cancer. ; Genetics. ; Biochemistry. ; Biological transport. ; Cell membranes. ; Molecular Genetics. ; Cancer Biology. ; Genetics and Genomics. ; Biochemistry. ; Membrane Trafficking.
    Description / Table of Contents: 1. History of sialic acids, gangliosides and GM3 -- 2. Synthesis of GM3 -- 3. Molecular localization of GM3 in cells -- 4. Basic function of GM3 as an interacting molecule -- 5. GD3 mimetics with a neurite forming capacity -- 6. GM3 as a pathogenic infection receptor -- 7. GM3 and related gangliosides prevent inflammation and atherosclerosis -- 8. GM3 has an anti-tumor capacity -- 9. GM3 suppresses tumor angiogenesis -- 10. Interaction between EGFR and GM3 -- 11. Membrane ganglioside-specific neuraminidase 3 (NEU3) regulates GM3 signaling -- 12. Regulation of GM3-mediated EGFR signaling by NEU3 sialidase -- 13. VEGFR-GM3 interaction in angiogenesis -- 14. GM3, competing with GM1, interaction with urokinase plasminogen activator receptor (uPAR) in endothelial caveolar-lipid rafts inhibits angiogenesis -- 15. GM3 interacts with TGFβ Rs in the epithelial-mesenchymal transition (EMT) during posterior capsular opacification (PCO) formation -- 16. Galectin-1 promotes tumor growth and escapes immune surveillance -- 17. GM3-HGFR, FGFR and PDGFR cancer cell behavior, and IGF-1R in diabetic wound healing -- 18. GM3, caveolin-1 and insulin receptor in insulin resistance -- 19. GM3 suppresses arthritis -- 20. GM3 protects cochlear hair cells and hearing from corti degeneration -- 21. GM3 increases osteoclast differentiation via direct GM3 cooperation with RANKL and IGF-1 -- 22. GM3 in leukemic cells into terminal differentiation -- 23. α2,3-Sialyllactose (3SL) or α2,6-sialyllactose (6SL) of GM3 glycan in innate immunity. .
    Abstract: This book reviews recent progress in understanding of the signaling and biochemistry of GM3 ganglioside in eukaryotic cells. GM3 is the simplest of the gangliosides and the precursor of other gangliosides. It is expressed in the outer leaflet of plasma cell membranes and has roles in the recognition, interaction, binding, adhesion, and motility of cells. In addition, GM3 has been documented to have functional roles in cell migration, proliferation, senescence, and apoptosis. The full range of topics of interest are addressed in the book. The early chapters discuss the synthesis of GM3, its molecular localization in cells, and its basic function as an interacting molecule. The ways in which GM3 exerts its effects via various growth factor receptors are fully explored. Current knowledge of the part played by GM3 in health and disease is discussed in depth. For example, its roles in preventing inflammation, inhibiting tumor angiogenesis and tumor growth, and suppressing arthritis are highlighted, and attention drawn to the significance of GM3 as a driver of impaired wound healing in diabetics. The book will be of interest to all who want a comprehensive update on research in this field.
    Type of Medium: Online Resource
    Pages: VII, 138 p. 32 illus., 26 illus. in color. , online resource.
    Edition: 1st ed. 2020.
    ISBN: 9789811556524
    URL: https://doi.org/10.1007/978-981-15-5652-4
    DOI: 10.1007/978-981-15-5652-4
    DDC: 572.8
    Language: English
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  • 2
    Online Resource
    Online Resource
    Ganglioside Biochemistry (2020)
    Singapore :Springer Nature Singapore :
    Details
    Keywords: Molecular genetics. ; Cancer. ; Genetics. ; Biochemistry. ; Biological transport. ; Cell membranes. ; Molecular Genetics. ; Cancer Biology. ; Genetics and Genomics. ; Biochemistry. ; Membrane Trafficking.
    Description / Table of Contents: Preface: Carbohydrates- the third life chain -- 1. Glycosylation -- 2. N-Glycan and O-glycan glycosylation in eukaryotes -- 3. Sialyltransferase, sialylation and sulfoylation -- 4. Congenital disorders of glycosylation (CDG) of N-glycoprotein -- 5. Neuraminic acids/sialic acids (N-acetyl- and N-glycolylneuraminic acid) -- 6. Biosynthesis of sialic acid -- 7. Neu5Gc (N-glycolylneuraminic acid) -- 8. Gangliosides -- 9. Gangliosides and tumor-associated ganglioside (TAG) modulate receptor-tyrosine kinases (RTKs) -- 10. Sialic acids and TAGs of tumor cells to escape immunesurveillance and immuneediting -- 11. Tumor characteristics in tumor related carbohydrates.
    Abstract: This book presents the latest knowledge and the most recent research results in the field of ganglioside biochemistry. The early chapters cover all relevant background on sialic acids and their biosynthesis, on N-glycolylneuraminic acid (Neu5Gc), which cannot be synthesized by humans, and on general aspects of ganglioside research. Ganglioside adsorption, disorders of ganglioside degradation, and the regulation of gangliosides are thoroughly discussed. A major focus of the book is the role of gangliosides in cancer. Here, the discussion encompasses, for example, the biological importance, antigenicity, and immunological actions of tumor-associated gangliosides (TAGs), the significance of different glycolipids and gangliosides as TAGs, and emerging anti-cancer vaccine strategies. The ability of sialic acids and TAGs of tumor cells to escape immunosurveillance and immunoediting also receives detailed attention. The significance of sialic acids in regulation of the complement system is explained, and the closing chapter focuses especially on the role of sialyl T antigen in cancer. The book will be of value for all who are interested in functional glycobiology and glycomic studies.
    Type of Medium: Online Resource
    Pages: XVI, 214 p. 57 illus., 48 illus. in color. , online resource.
    Edition: 1st ed. 2020.
    ISBN: 9789811558153
    URL: https://doi.org/10.1007/978-981-15-5815-3
    DOI: 10.1007/978-981-15-5815-3
    DDC: 572.8
    Language: English
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  • 3
    Online Resource
    Online Resource
    Glycosphingolipids Signaling (2020)
    Singapore :Springer Nature Singapore :
    Details
    Keywords: Molecular genetics. ; Cancer. ; Genetics. ; Biochemistry. ; Biological transport. ; Cell membranes. ; Molecular Genetics. ; Cancer Biology. ; Genetics and Genomics. ; Biochemistry. ; Membrane Trafficking.
    Description / Table of Contents: 1. Glycosphingolipids (GSLs) -- 2. Mammal GSL synthesis via ER and Golgi network -- 3. The GSL dependent signaling -- 4. Viral protein interaction with host cells GSLs -- 5. Bacterial toxin protein interaction with host cells GSL -- 6. GSL signaling regulation.
    Abstract: This book presents the latest knowledge and the most recent research results on glycosphingolipid (GSL)-mediated signaling. GSLs are important constituents of the plasma membrane that exert their distinct functions through binding to certain functional proteins. They play a role in various human diseases and also function as human alloantigens. Cellular GSLs are associated with many biological functions such as cellular oncotransformation, phenotype change, neuronal or embryonic development, regulation of cell division, cell–cell interaction, cell attachment, adhesion, and motility, and intracellular signaling via protein–carbohydrate or carbohydrate–carbohydrate interactions. This book opens by providing the key background on GSL glycan–receptor interactions and mammalian GSL synthesis. Up-to-date information is then presented on all aspects of GSL-dependent signaling. Viral protein and bacterial toxin protein interactions with host cell GSLs are examined in depth, and the concluding chapter is devoted to signaling regulation. The book should assist in the further development of new strategies against emerging infectious agents and intractable diseases.
    Type of Medium: Online Resource
    Pages: XVII, 181 p. 30 illus., 25 illus. in color. , online resource.
    Edition: 1st ed. 2020.
    ISBN: 9789811558078
    URL: https://doi.org/10.1007/978-981-15-5807-8
    DOI: 10.1007/978-981-15-5807-8
    DDC: 572.8
    Language: English
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  • 4
    Online Resource
    Online Resource
    Glycobiology of Innate Immunology (2022)
    Singapore :Springer Nature Singapore :
    Details
    Keywords: Genetics. ; Medical genetics. ; Biology. ; Membranes (Biology). ; Biological transport. ; Cell membranes. ; Genetics and Genomics. ; Medical Genetics. ; Biological Sciences. ; Biological Membranes. ; Membrane Trafficking.
    Description / Table of Contents: Part 1. Glycans in innate immunity of dendritic cells -- Chapter 1) Historical expansion of defense system -- Chapter 2) Columbus era to modern revolution in immunological defense system -- Chapter 3) Historical profile of defense constituents and progress in innte immune repertoire -- Chapter 4) The outline of innate immunity -- Chapter 5) Autophagy from microbial invaders and self-associated molecular patterns (SAMPs) of innate immune cells -- Part 2. Dendritic cells (DCs) -- Chapter 6) General biology of DCs -- Chapter 7) Classification and different function of DCs -- Chapter 8) Glycan biosynthesis in eukaryotes -- Chapter 9) Glycans in cell recognition and evolutionary adaptation in organisms -- Chapter 10) Changes in glycan structure involve in co-regulated expression of glycan-binding lectin counterparts -- Chapter 11) Evolution of lectin: alternative splicing contributes to variation for glycan binding receptors -- Chapter 12) Glycan regulation of NK cell receptors -- Chapter 13) Carbohydrate recognition of target antigens by DCs during infection and inflammation -- Chapter 14) Glycan-specific trafficking receptors in DCs maturation -- Chapter 15) Glycan ligands in trafficking of DC migration -- Chapter 16) Chemokine receptors in DCs trafficking -- Chapter 17) Glycan structure-recognizing selectins in DC-endothelium interaction during infection and inflammation -- Chapter 18) Glycans activate the innate immune system -- Chapter 19) Innate immune lectin receptors of Siglec, DC-SIGN, Galectin and TLR in DCs -- Chapter 20) Galectins -- Chapter 21) DC-specific ICAM-3-grabbing non-integrin, DC-SIGNB (CD209) -- Chapter 22) Other DCs-derivd receptors -- Chapter 23) Toll-like receptors (TLRs) -- Chapter 24) CD33 and CD33-related Siglecs in pathogen recognition and endocytosis of DC in the innate immune system -- Chapter 25) Pathogenic suppression of the pathogen-specific host immune response -- Chapter 26) DCs tumor immunotherapy through sialyl binding of DCs to T cells.
    Abstract: This book presents the latest knowledge and the most recent research results on glycobiology of innate immunology. Innate immunity is the crucial part of the immunological defense system that exerts their distinct functions through binding to certain functional glycoproteins. They play a role in various human diseases and also function against microbial invaders and self-associated molecular patterns. Co-regulated expression of glycan-binding is associated with many biological components such as cellular oncotransformation, phenotype change, neuronal or embryonic development, regulation of cell division, cell–cell interaction, cell attachment, adhesion, and motility, and intracellular signaling via protein–carbohydrate or carbohydrate–carbohydrate interactions. This book opens by providing the key background on glycans in innate immunity and its mechanisms behind the Dendritic cell interactions during infection and inflammation are examined in depth, and the concluding chapter is devoted to signaling tumor immunotherapy. Up-to-date information is then presented on all aspects of glycan structure-recognizing signaling. The book should assist in the further development of new strategies against emerging infectious agents and intractable diseases.
    Type of Medium: Online Resource
    Pages: XIX, 656 p. 1 illus. , online resource.
    Edition: 1st ed. 2022.
    ISBN: 9789811690815
    URL: https://doi.org/10.1007/978-981-16-9081-5
    DOI: 10.1007/978-981-16-9081-5
    DDC: 576.5
    Language: English
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  • 5
    Electronic Resource
    Electronic Resource
    Purification and biochemical characterization of pullulanase type I from Thermus caldophilus GK-24 (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 138 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A thermostable pullulanase (pullulan 6-glucanohydrolase, EC 3.2.1.41) has been purified to homogeneity from Thermus caldophilus GK-24 by Chromatographic methods, including gel-filtration and ion-exchange chromatography. The specific activity of the enzyme was increased 431-fold with a recovery of 13.2%. The purified enzyme was a monomer, Mr= 65 kDa as estimated by SDS-PAGE and gel filtration. The pI was 6.1. The enzyme was most active at pH 5.5. The activity was maximal at 75 °C and stable up to 95 °C for 30 min at pH 5.5. The enzyme was stable to incubation from pH 3.5 to pH 8.0 at 4 °C for 24 h. The activity of the enzyme was stimulated by Mn2+ and Mg2+ ions. Ni2+, Ca2+, Co2+ ions and EDTA did not inhibit the enzyme activity. The enzyme hydrolyzed the α-1,6 linkages of amylopectin, glycogens, α,β-limited dextrin, and pullulan. The enzyme caused the complete hydrolysis of pullulan to maltotriose. The activity was inhibited by α-, β-, or γ-cyclodextrins. The N-terminal sequence [(Ala-Pro-Gln-(Asp or Tyr)-Asn-Leu-Leu-Xaa-ILe-Gly-Ala(Ser)] showed some similarity to those of bacterial pullulanases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08148.x
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  • 6
    Electronic Resource
    Electronic Resource
    Specific detection of pullulanase type I in polyacrylamide gels (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 116 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A specific detection of pullulanase type I which hydrolyzes the α-1,6-glycosidic linkages on pullulan and starch was developed using impregnation of gels with soluble starch and staining for amylose with iodine. It was a simple and highly sensitive zymogram method capable of detecting as little as 0.001 unit of pullulanase type I activity in polyacrylamide gels after electrophoresis. After fractionation of crude enzyme using DEAE ion exchange chromatography to avoid possible co-migration of amylolytic enzymes which disturb the interaction between amylose and iodine, the high and critical sensitivity of the detection was achieved. The specific detection is based on the fact that when pullulanase type I hydrolyzes the α-1,6-glycosidic bonds in soluble starch increased amounts of α-1,4-linked amylose is formed which yields more intensely blue colored conjugate with iodine. Thus, blue bands on the lighter background signal the presence of pullulanase type I. In contrast, amylolytic enzymes give ‘white’ bands on the lightly stained background because they remove amylose. This procedure is effective in enzyme screening to distinguish debranching enzyme (pullulanase type I) from other pullulan-degrading enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb06723.x
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  • 7
    Electronic Resource
    Electronic Resource
    Characterization of a DNA fragment carrying the raw starch-digesting α-amylase and salt-dependent α-amylase genes from Bacillus circulans F-2 (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 126 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A 5.4 kb HindIII DNA fragment carrying the gene encoding raw starch-digesting α-amylase (RSDA), has been previously cloned from Bacillus circulans F-2 and expressed in Escherichia coli [Kim et al. (1990) Biochim. Biophys. Acta 1048, 2233–2238]. Interestingly, when the cell extract of E. coli harboring a plasmid carrying this fragment was incubated with l M NaCl, it exhibited about 10 times higher enzyme activity than when assayed without NaCl. Differential zymograms showed two different amylase activities: one for RSDA and the other for a salt-dependent a-amylase (SDA). Even though RSDA activity was detected without NaCl, SDA activity was detected only in high concentrations of NaCl. SDA activity was fully detected at above l M NaCl. Results from subcloning of the genes, fractionation analysis of cell extracts, and immunological assays clearly suggested that the two amylases are genetically distinct and that genes for both enzymes are closely linked on the 5.4 kb DNA fragment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07406.x
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  • 8
    Electronic Resource
    Electronic Resource
    Purification and Characterization of β-amylase from Bacillus polymyxa No. 26-1 (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of food science 61 (1996), S. 0 
    Details
    ISSN: 1750-3841
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Process Engineering, Biotechnology, Nutrition Technology
    Notes: An extracellular β-amylase, which was easily adsorbable onto raw corn starch, was purified 22.5-fold from a new isolate of Bacillus polymyxa No 26–1 with a Mr of 53 kDa and pI of 9.1. The optimum temperature was 45°C and pH 5.5 for raw corn starch. Thermal stability at 40°C and pH stability at 5.0–8.5 were shown. The degradation ofraw starch by β-amylase was greatly stimulated by pullulanase addition. Scanning electron micrographs revealed that starch granule degradation by the enzyme alone occured at the equatorial grooves of lecticular granules. Corn starch granules hydrolyzed by β-amylase had large holes on granule surfaces.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2621.1996.tb14767.x
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  • 9
    Electronic Resource
    Electronic Resource
    Pullulanases of alkaline and broad pH range from a newly isolated alkalophilicBacillus sp. S-1 and aMicrococcus sp. Y-1 (1993)
    Springer
    Journal of industrial microbiology and biotechnology 12 (1993), S. 48-57 
    Details
    ISSN: 1476-5535
    Keywords: Alkalophilic bacteria ; Alkaline pullulanase ; Multifunctional pullulanase ; (Bacillus sp. S-1) ; (Micrococcus sp. Y-1)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Two highly alkalophilic bacteria, and potent producers of alkaline pullulanase, were isolated from Korean soils. The two isolates, identified asBacillus sp. S-1 andMicrococcus sp. Y-1, grow on starch under alkaline conditions and effectively secrete extracellular pullulanases. The two isolates were extremely alkalophilic since bacterial growth and enzyme production occurred at pH values ranging from pH 6.0 to 12.0 forMicrococcus sp. Y-1 and pH 6.0 to 10.0 forBacillus sp. S-1. Both strains secrete enzymes that possess amylolytic and pullulanolytic acitivities. Extracellular crude enzymes of both isolates gave maltotriose as the major product formed from soluble starch and pullulan hydrolysis. Compared to other alkalophilic microbes such asMicrococcus sp. (0.57 units ml−1),Bacillus sp. KSM-1876 (0.56 units ml−1) andBacillus No. 202-1 (1.89 units ml−1) these isolates secreted extremely high concentrations (7.0 units ml−1 forBacillus sp. S-1 and 7.6 units ml−1 forMicrococcus sp. Y-1) of pullulanases in batch culture. The pullulanase activities from both strains were mostly found in the culture medium (85–90%). The extracellular enzymes of both bacteria were alkalophilic and moderately thermoactive; optimal activity was detected at pH 8.0–10.0 and between 50 and 60°C. Even at pH 12.0, 65% of original Y-1 pullulanase activity and 10% of S-1 pullulanase activity remained. The two newly isolated strains had broad pH ranges and moderate thermostability for their enzyme activities. These result strongly indicate that these new bacterial isolates have potential as producers of pullulanases for use in the starch industry.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01570128
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  • 10
    Electronic Resource
    Electronic Resource
    Allelic divergence in the human insulin gene provides evidence for intragenic recombination events in the non-coding regions: evidence for existence of new alleles (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 146-151 
    Details
    ISSN: 1617-4623
    Keywords: Allelic divergence ; Human insulin gene ; Intragenic recombination ; Non-coding regions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Intragenic polymorphism of the human insulin gene (INS) was investigated in Korean subjects. The 1.9 kb INS sequence, including the 5′ to 3′ flanking regions, was amplified using the polymerase chain reaction (PCR), and analyzed by direct sequencing. All nucleotide sequences in the coding regions were the same as INS sequences previously reported, and four nucleotides, at positions +216, +1045, +1367, and +1380 in the non-coding regions, were found to be polymorphic. In addition to the previously identified polymorphic alleles αl (A-C-C-C) and β1 (T-G-T-A), new nucleotide arrangements were also identified and designated α4 (A-C-C-A), α5 (A-G-C-C), α6 (A-C-T-C), and β2 (T-C-C-C). It was concluded that the new alleles may originate by intragenic recombination within INS during chromosomal crossing-over between the α1 and β1 alleles. The allele α1 was the predominant form in our sample; the new variant alleles, as well as allele β1, appeared to be much less frequent in INSs genes of the Korean subjects studied. Furthermore, the new alleles were detected only in heterozygous form. These results suggest that intragenic recombination can account for allelic divergence in INS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00283261
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