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Artículos de revistas sobre el tema "Cholerae sialidase"

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Publicado: 4 de junio de 2021
Última modificación: 20 de febrero de 2023

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1

Jung, K., M. Pergande, and S. Klotzek. "Sialidase from different sources compared for electrophoretically separating serum alkaline phosphatase fractions from liver and bone." Clinical Chemistry 35, no. 9 (September 1, 1989): 1955–57. http://dx.doi.org/10.1093/clinchem/35.9.1955.

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Abstract We compared sialidase (neuraminidase; EC 3.2.1.18) from Vibrio cholerae, Clostridium perfringens, and Arthrobacter ureafaciens, seeking to improve the electrophoretic separation of the liver and bone isoenzymes of alkaline phosphatase (EC 3.1.3.1) on cellulose acetate membranes. Resolution is decisively determined by the type and activity of sialidase used in the preincubation of serum sample. Sialidase from Arthrobacter ureafaciens is not suited for this method. For optimal separation of the two isoenzymes we recommend the use of sialidase from Vibrio cholerae, determination of its a
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2

Khedri, Zahra, Yanhong Li, Hongzhi Cao, Jingyao Qu, Hai Yu, Musleh M. Muthana, and Xi Chen. "Synthesis of selective inhibitors against V. cholerae sialidase and human cytosolic sialidase NEU2." Organic & Biomolecular Chemistry 10, no. 30 (2012): 6112. http://dx.doi.org/10.1039/c2ob25335f.

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3

Dhanushkodi, Anandh, and Michael P. McDonald. "Intracranial V. cholerae Sialidase Protects against Excitotoxic Neurodegeneration." PLoS ONE 6, no. 12 (December 15, 2011): e29285. http://dx.doi.org/10.1371/journal.pone.0029285.

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4

Watson, Jacqueline N., Tara L. Knoll, Johnny H. Chen, Doug T. H. Chou, Thor J. Borgford та Andrew J. Bennet. "Use of conformationally restricted pyridinium α-D-N-acetylneuraminides to probe specificity in bacterial and viral sialidases". Biochemistry and Cell Biology 83, № 2 (1 квітня 2005): 115–22. http://dx.doi.org/10.1139/o04-126.

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Investigations into subtle changes in the catalytic activity of sialidases have been performed using enzymes from several different origins, and their results have been compared. This work highlights the potential pitfalls encountered when extending conclusions derived from mechanistic studies on a single enzyme even to those with high-sequence homology. Specifically, a panel of 5 pyridinium N-acetylneuraminides were used as substrates in a study that revealed subtle differences in the catalytic mechanisms used by 4 different sialidase enzymes. The lowest reactivity towards the artificial (pyr
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5

Chuenkova, M., and M. E. Pereira. "Trypanosoma cruzi trans-sialidase: enhancement of virulence in a murine model of Chagas' disease." Journal of Experimental Medicine 181, no. 5 (May 1, 1995): 1693–703. http://dx.doi.org/10.1084/jem.181.5.1693.

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Trypanosoma cruzi, the etiological agent of Chagas' disease, expresses a trans-sialidase at highest levels in infective trypomastigotes, where it attaches to the plasma membrane by a glycophosphoinositol linkage. Bound enzyme sheds into the extracellular milieu in a soluble form. Experiments performed in vitro suggest that the trans-sialidase participates in several parameters of T. cruzi-host interactions, like cell adhesion and complement resistance. However, the role that membrane-bound and soluble trans-sialidase plays in the infection of mammals is not understood. To begin to study the ro
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6

Slack, Teri J., Wanqing Li, Dashuang Shi, John B. McArthur, Gengxiang Zhao, Yanhong Li, An Xiao, et al. "Triazole-linked transition state analogs as selective inhibitors against V. cholerae sialidase." Bioorganic & Medicinal Chemistry 26, no. 21 (November 2018): 5751–57. http://dx.doi.org/10.1016/j.bmc.2018.10.028.

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7

Powell, L. D., S. W. Whiteheart, and G. W. Hart. "Cell surface sialic acid influences tumor cell recognition in the mixed lymphocyte reaction." Journal of Immunology 139, no. 1 (July 1, 1987): 262–70. http://dx.doi.org/10.4049/jimmunol.139.1.262.

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Abstract The Ia+ B cell lymphoma, AKTB-1b, fails to stimulate thymic lymphocytes in a one-way mixed lymphocyte reaction unless pretreated with sialidase or inhibitors of N-linked oligosaccharide processing. A comparison of different sialidases and sialyltransferases suggests that the removal of only a subset of total surface sialic acid, rather than net desialylation of the cell surface, is required. Three sialidases were compared, including Vibrio cholerae (VC) and Clostridium perfringens (CP), which will cleave alpha 2-3, alpha 2-6, and alpha 2-8, sialic acid linkages, and Newcastle Disease
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8

Mann, Maretta C., Robin J. Thomson, Jeffrey C. Dyason, Sarah McAtamney, and Mark von Itzstein. "Modelling, synthesis and biological evaluation of novel glucuronide-based probes of Vibrio cholerae sialidase." Bioorganic & Medicinal Chemistry 14, no. 5 (March 2006): 1518–37. http://dx.doi.org/10.1016/j.bmc.2005.10.004.

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9

Wilson, Jennifer C., Robin J. Thomson, Jeffrey C. Dyason, Pas Florio, Kaylene J. Quelch, Samia Abo, and Mark von Itzstein. "The design, synthesis and biological evaluation of neuraminic acid-based probes of Vibrio cholerae sialidase." Tetrahedron: Asymmetry 11, no. 1 (January 2000): 53–73. http://dx.doi.org/10.1016/s0957-4166(99)00552-2.

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10

Wallimann, Kurt, and Andrea Vasella. "Phosphonic-Acid Analogues of the N-Acetyl-2-deoxyneiiraniinic Acids: Synthesis and Inhibition ofVibrio cholerae Sialidase." Helvetica Chimica Acta 73, no. 5 (August 8, 1990): 1359–72. http://dx.doi.org/10.1002/hlca.19900730523.

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11

Mizan, Shaikh, Adam Henk, Amy Stallings, Marie Maier, and Margie D. Lee. "Cloning and Characterization of Sialidases with 2-6′ and 2-3′ Sialyl Lactose Specificity from Pasteurella multocida." Journal of Bacteriology 182, no. 24 (December 15, 2000): 6874–83. http://dx.doi.org/10.1128/jb.182.24.6874-6883.2000.

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ABSTRACT Pasteurella multocida is a mucosal pathogen that colonizes the respiratory system of susceptible hosts. Most isolates ofP. multocida produce sialidase activity, which may contribute to colonization of the respiratory tract or the production of lesions in an active infection. We have cloned and sequenced a sialidase gene, nanH, from a fowl cholera isolate ofP. multocida. Sequence analysis of NanH revealed that it exhibited significant amino acid sequence homology with many microbial sialidases. Insertional inactivation of nanH resulted in a mutant strain that was not deficient in siali
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12

Vasella, Andrea, and Ren� Wyler. "Synthesis of a Phosphonic Acid Analogue ofN-Acetyl-2,3-didehydro-2-deoxyneuraminic Acid, an Inhibitor ofVibrio cholerae Sialidase." Helvetica Chimica Acta 74, no. 2 (March 13, 1991): 451–63. http://dx.doi.org/10.1002/hlca.19910740223.

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13

WALLIMANN, K., and A. VASELLA. "ChemInform Abstract: C-Glycosides of N-Acetylneuraminic Acid. Synthesis and Investigation of Their Effect on Vibrio cholerae Sialidase." ChemInform 23, no. 3 (August 22, 2010): no. http://dx.doi.org/10.1002/chin.199203241.

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14

Schreiner, Erwin, Erich Zbiral, Reinhard G. Kleineidam, and Roland Schauer. "2,3-Didehydro-2-deoxysialic acids structurally varied at C-5 and their behaviour towards the sialidase from Vibrio cholerae." Carbohydrate Research 216 (September 1992): 61–66. http://dx.doi.org/10.1016/0008-6215(92)84150-q.

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15

VASELLA, A., and R. WYLER. "ChemInform Abstract: Synthesis of a Phosphonic Acid Analogue of N-Acetyl-2,3-didehydro-2- deoxyneuraminic Acid, an Inhibitor of Vibrio cholerae Sialidase." ChemInform 22, no. 21 (August 23, 2010): no. http://dx.doi.org/10.1002/chin.199121270.

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16

Haselhorst, Thomas, Jennifer C. Wilson, Robin J. Thomson, Sarah McAtamney, John G. Menting, Ross L. Coppel, and Mark von Itzstein. "Saturation transfer difference (STD) 1H-NMR experiments and in silico docking experiments to probe the binding of N-acetylneuraminic acid and derivatives to Vibrio cholerae sialidase." Proteins: Structure, Function, and Bioinformatics 56, no. 2 (April 28, 2004): 346–53. http://dx.doi.org/10.1002/prot.20143.

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17

Zbiral, Erich, Erwin Schreiner, Rudolf Christian, Reinhard G. Kleineidam, and Roland Schauer. "Structural Variations ofN-Acetylneuraminic Acid, 10. Synthesis of 2,7-, 2,8-, and 2,9-Dideoxy- and 2,4,7-Trideoxy-2,3-didehydro-N-acetylneuraminic Acids and Their Behavior Towards Sialidase fromVibrio cholerae." Liebigs Annalen der Chemie 1989, no. 2 (February 10, 1989): 159–65. http://dx.doi.org/10.1002/jlac.198919890131.

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18

Schreiner, Erwin, Erich Zbiral, Reinhard G. Kleineidam, and Roland Schauer. "Structural Variations on N-acetylneuraminic acid, 20. Synthesis of some 2,3-didehydro-2-deoxysialic Acids structurally varied at C-4 and their behavior towards Sialidase from Vibrio cholerae." Liebigs Annalen der Chemie 1991, no. 2 (February 12, 1991): 129–34. http://dx.doi.org/10.1002/jlac.199119910124.

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19

Maliakal, Mathew A., Mepur H. Ravindranath, Reiko F. Irie, and Donald L. Morton. "An improved method for the measurement of total lipid-bound sialic acids after cleavage of ?2,8 sialic acid linkage withVibrio cholerae sialidase in the presence of cholic acid, SDS and Ca2+." Glycoconjugate Journal 11, no. 2 (April 1994): 97–104. http://dx.doi.org/10.1007/bf00731149.

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20

SCHREINER, E., E. ZBIRAL, R. G. KLEINEIDAM, and R. SCHAUER. "ChemInform Abstract: Structural Variations on N-Acetylneuraminic Acid. Part 20. Synthesis of Some 2,3-Didehydro-2-deoxysialic Acids Structurally Varied at C-4 and Their Behavior Towards Sialidase from Vibrio cholerae." ChemInform 22, no. 17 (August 23, 2010): no. http://dx.doi.org/10.1002/chin.199117258.

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21

Lee, Youngjin, Young Bae Ryu, Hyung-Seop Youn, Jung Keun Cho, Young Min Kim, Ji-Young Park, Woo Song Lee, Ki Hun Park, and Soo Hyun Eom. "Structural basis of sialidase in complex with geranylated flavonoids as potent natural inhibitors." Acta Crystallographica Section D Biological Crystallography 70, no. 5 (April 30, 2014): 1357–65. http://dx.doi.org/10.1107/s1399004714002971.

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Sialidase catalyzes the removal of a terminal sialic acid from glycoconjugates and plays a pivotal role in nutrition, cellular interactions and pathogenesis mediating various infectious diseases including cholera, influenza and sepsis. An array of antiviral sialidase agents have been developed and are commercially available, such as zanamivir and oseltamivir for treating influenza. However, the development of bacterial sialidase inhibitors has been much less successful. Here, natural polyphenolic geranylated flavonoids which show significant inhibitory effects againstCp-NanI, a sialidase fromC
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22

Masserini, M., P. Palestini, B. Venerando, A. Fiorilli, D. Acquotti, and G. Tettamanti. "Interactions of proteins with ganglioside-enriched microdomains on the membrane: the lateral phase separation of molecular species of GD1a ganglioside, having homogeneous long-chain base composition, is recognized by Vibrio cholerae sialidase." Biochemistry 27, no. 20 (October 4, 1988): 7973–78. http://dx.doi.org/10.1021/bi00420a057.

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23

Zbiral, Erich, Hannelore H. Brandstetter, Rudolf Christian, and Roland Schauere. "Structural Variations ofN-Acetylneuraminic Acid, 7. Synthesis of the C-7-, C-8-, and C-7,8-Side Chain Epimers of 2-Deoxy-2,3-didehydro-N-acetylneuraminic Acid and Their Behaviour Towards Sialidase fromVibrio cholerae." Liebigs Annalen der Chemie 1987, no. 9 (September 14, 1987): 781–86. http://dx.doi.org/10.1002/jlac.198719870828.

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24

Spiegel, S., K. M. Yamada, B. E. Hom, J. Moss, and P. H. Fishman. "Fibrillar organization of fibronectin is expressed coordinately with cell surface gangliosides in a variant murine fibroblast." Journal of Cell Biology 102, no. 5 (May 1, 1986): 1898–906. http://dx.doi.org/10.1083/jcb.102.5.1898.

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NCTC 2071A cells, a line of transformed murine fibroblasts, grow in serum-free medium, are deficient in gangliosides, synthesize fibronectin, but do not retain and organize it on the cell surface. When the cells are exposed to exogenous gangliosides, fibrillar strands of fibronectin become attached to the cell surface. A morphologically distinct variant of NCTC 2071A cells was observed to both retain cell surface fibronectin and organize it into a fibrillar network when the cells were stained with anti-fibronectin antibodies and a fluorescent second antibody. A revertant cell type appeared to
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25

Zbiral, Erich, Erwin Schreiner, Mamikrao M. Salunkhe, Gerhard Schulz, Reinhard G. Kleineidam та Roland Schauer. "Structural Variations ofN-Acetylneuraminic Acid, 11, Synthesis of the 4-Methylumbelliferyl 2α-Glycosides of 7-Epi-, 8-Epi-, and 7,8-Bis(epi)-N-acetylneuraminic Acids, as well as of 7-Deoxy-, 8-Deoxy-, 9-Deoxy-, and 4,7-Dideoxy-N-acetylneuraminic Acids and Their Behaviour Towards Sialidase fromVibrio cholerae". Liebigs Annalen der Chemie 1989, № 6 (13 червня 1989): 519–26. http://dx.doi.org/10.1002/jlac.198919890192.

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26

Almeida, C. N., T. Q. Furian, K. A. Borges, G. Perdoncini, M. J. Mauel, S. L. S. Rocha, V. P. Nascimento, C. T. P. Salle, and H. L. S. Moraes. "Assessment of FTA card employment for Pasteurella multocida DNA transport and detection of virulence-associated genes in strains isolated from fowl cholera in the United States." Arquivo Brasileiro de Medicina Veterinária e Zootecnia 70, no. 6 (December 2018): 1855–61. http://dx.doi.org/10.1590/1678-4162-9821.

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ABSTRACT Fowl Cholera (FC) is a disease caused by Pasteurella multocida. The severity of this disease is partly caused by virulence factors. Genes encoding fimbriae, capsule, sialidases and proteins for iron metabolism may be related to P. multocida’s ability to infect the host. Besides to examining DNA for the presence of virulence genes, DNA is essential for the diagnostic and FTA cards are an alternative for genetic material transport. The study aims to evaluate the viability of P. multocida DNA transport using the cards and to detect 14 virulence genes in 27 strains isolated from FC cases
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27

Kaisar, M. Hasanul, Mohammed Saruar Bhuiyan, Aklima Akter, Danial Saleem, Anita S. Iyer, Pinki Dash, Al Hakim, et al. "Vibrio cholerae Sialidase-Specific Immune Responses Are Associated with Protection against Cholera." mSphere 6, no. 2 (April 28, 2021). http://dx.doi.org/10.1128/msphere.01232-20.

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ABSTRACT Cholera remains a major public health problem in resource-limited countries. Vaccination is an important strategy to prevent cholera, but currently available vaccines provide only 3 to 5 years of protection. Understanding immune responses to cholera antigens in naturally infected individuals may elucidate which of these are key to longer-term protection seen following infection. We recently identified Vibrio cholerae O1 sialidase, a neuraminidase that facilitates binding of cholera toxin to intestinal epithelial cells, as immunogenic following infection in two recent high-throughput s
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28

Chowdhury, Fahima, Afroza Akter, Taufiqur Rahman Bhuiyan, Rajib Biswas, Md Golam Firoj, Imam Tauheed, Jason B. Harris, et al. "Long-term sialidase-specific immune responses after natural infection with cholera: Findings from a longitudinal cohort study in Bangladesh." Frontiers in Immunology 13 (December 22, 2022). http://dx.doi.org/10.3389/fimmu.2022.1067737.

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BackgroundImmune responses that target sialidase occur following natural cholera and have been associated with protection against cholera. Sialidase is a neuraminidase that facilitates the binding of cholera toxin (CT) to intestinal epithelial cells. Despite this, little is known about age-related sialidase-specific immune responses and the impact of nutritional status and co-infection on sialidase-specific immunity.MethodsWe enrolled 50 culture-confirmed Vibrio cholerae O1 cholera cases presenting to the icddr,b Dhaka hospital with moderate to severe dehydration. We evaluated antibody respons
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29

Upadhyay, Ipshita, Siqi Li, Galen Ptacek, Hyesuk Seo, David A. Sack, and Weiping Zhang. "A polyvalent multiepitope protein cross-protects against Vibrio cholerae infection in rabbit colonization and passive protection models." Proceedings of the National Academy of Sciences 119, no. 50 (December 5, 2022). http://dx.doi.org/10.1073/pnas.2202938119.

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Using epitope- and structure-based multiepitope fusion antigen vaccinology platform, we constructed a polyvalent protein immunogen that presents antigenic domains (epitopes) of Vibrio cholerae toxin-coregulated pilus A, cholera toxin (CT), sialidase, hemolysin A, flagellins (B, C, and D), and peptides mimicking lipopolysaccharide O-antigen on a flagellin B backbone. Mice and rabbits immunized intramuscularly with this polyvalent protein immunogen developed antibodies to all of the virulence factors targeted by the immunogen except lipopolysaccharide. Mouse and rabbit antibodies exhibited funct
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30

Kauffman, Robert C., Taufiqur R. Bhuiyan, Rie Nakajima, Leslie M. Mayo-Smith, Rasheduzzaman Rashu, Mohammad Rubel Hoq, Fahima Chowdhury, et al. "Single-Cell Analysis of the Plasmablast Response to Vibrio cholerae Demonstrates Expansion of Cross-Reactive Memory B Cells." mBio 7, no. 6 (December 20, 2016). http://dx.doi.org/10.1128/mbio.02021-16.

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ABSTRACT We characterized the acute B cell response in adults with cholera by analyzing the repertoire, specificity, and functional characteristics of 138 monoclonal antibodies (MAbs) generated from single-cell-sorted plasmablasts. We found that the cholera-induced responses were characterized by high levels of somatic hypermutation and large clonal expansions. A majority of the expansions targeted cholera toxin (CT) or lipopolysaccharide (LPS). Using a novel proteomics approach, we were able to identify sialidase as another major antigen targeted by the antibody response to Vibrio cholerae in
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31

Asang, Gogula Selvi, Shadariah Mamat, Nadiawati Alias, and Asmad Kari. "Expression and characterization of family 40 Carbohydrate Binding Module (CBM) from Vibrio cholerae Non-O1 sialidase." Asia Pacific Journal of Molecular Biology and Biotechnology, October 29, 2020, 26–38. http://dx.doi.org/10.35118/apjmbb.2020.028.4.03.

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Carbohydrate Binding Module (CBM) is a non-catalytic protein domain found in carbohydrate-active enzyme (glycoside hydrolase) and its role is to bring carbohydrates in close proximity to the enzyme catalytic site for complete hydrolysis. The removal of this CBM from most protein domains often leads to reduced enzyme activity and efficiency. In this study, a gene encoding for family 40 CBM from Vibrio cholerae Non-O1 sialidase was cloned and successfully expressed in E. coli BL21 (DE3) strain. The CBM40 encoded 195 amino acids with 585 bp of nucleotide sequence. The protein was successfully exp
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32

WALLIMANN, K., and A. VASELLA. "ChemInform Abstract: Phosphonic-Acid Analogues of the N-Acetyl-2-deoxyneuraminic Acids: Synthesis and Inhibition of Vibrio cholerae Sialidase." ChemInform 21, no. 48 (November 27, 1990). http://dx.doi.org/10.1002/chin.199048271.

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33

ZBIRAL, E., E. SCHREINER, R. CHRISTIAN, R. G. KLEINEIDAM, and R. SCHAUER. "ChemInform Abstract: Structural Variations of N-Acetylneuraminic Acid. Part 10. Synthesis of 2,7-, 2,8-, and 2,9-Dideoxy- and 2,4,7-Trideoxy-2,3-didehydro-N-acetylneuraminic Acids and Their Behavior Toward Sialidase from Vibrio cholerae." ChemInform 20, no. 19 (May 9, 1989). http://dx.doi.org/10.1002/chin.198919288.

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ZBIRAL, E., H. H. BRANDSTETTER, R. CHRISTIAN, and R. SCHAUER. "ChemInform Abstract: Structural Variations of N-Acetylneuraminic Acid. Part 7. Synthesis of the C-7-, C-8-, and C-7,8 Side Chain Epimers of 2-Deoxy-2,3-didehydro-N-acetylneuraminic Acid and Their Behavior Towards Sialidase from Vibrio cholerae." ChemInform 18, no. 49 (December 8, 1987). http://dx.doi.org/10.1002/chin.198749326.

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