By Anatole A. Klyosov, Zbigniew J. Witczak, David Platt
ISBN-10: 0470373180
ISBN-13: 9780470373187
The great advisor to the present realizing of galectins and their promising strength in drug layout this is often the 1st publication targeting galectins. It used to be encouraged by means of themes mentioned on the symposium "Galectins: constructions, services, and healing goals" that used to be part of the 234th American Chemical Society assembly in 2007. to aid chemists, biochemists, and others comprehend the demanding situations inherent within the examine of galectins and construct on fresh advances within the box, the editors have compiled articles from best specialists on galectins and their biomedical purposes. Galectins contains: * an summary of early galectin examine * a proof of the character of galectins * A dialogue of the constitution and services of galectins, their ligand specificity and molecular mechanisms of motion, and the localization of galectins within the phone * An exploration of the jobs galectins play in tumor development and melanoma, fibrosis, irritation, and immunity * A dialogue of the impression of galectins on mobilephone migration, angiogenesis, and chemoresistance * An advent to new methods to designing galectin inhibitors this is often the most effective reference on galectins for natural, medicinal, carbohydrate, and pharmaceutical chemists, biochemists, molecular and telephone biologists, pharmacologists, melanoma researchers, and graduate-level scholars in those disciplines, in addition to clinicians and drug builders.
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Facy P, Seve AP, Hubert M, Monsigny M, Hubert J. Analysis of nuclear sugar-binding components in undifferentiated and in vitro differentiated human promyelocytic leukemia cells (HL60)Exp Cell Res 1990;190:151À160. REFERENCES 29 25. Felin M, Doyennette-Moyne MA, Hadj-Sahraoui Y, Aubery M, Hubert J, Seve AP. Identification of two nuclear N-acetylglucosamine-binding proteins. J Cell Biochem 1994;56:527À535. 26. Lefebvre T, Cieniewski C, Lemoine J, Guerardel Y, Leroy Y, Zanetta JP, Michalski JC. Identification of N-acetyl-D-glucosamine-specific lectins from rat liver cytosolic and nuclear compartments as heat-shock proteins.
If per residue free energies are summarily greater for one type of dimer, then that one will prevail in solution. In this regard, formation of dimer type (terminal, symmetric, and nonsymmetric) may be functionally important, because this may help differentiate how different galectins bind differently to complex glycans intra- or extracellularly on the surface of cells. These natural glycans are far more complex than simple disaccharides such as lactose that have been used to study galectin carbohydrate binding and function.
1) (30). The actual amino acid residues that interact with the b-galactoside disaccharide, for example, lactose, are highly conserved among all galectins, as is evident from the amino acid sequence comparison shown in Fig. 2 (residues highlighted in red). Even though the b-galactoside disaccharide is the carbohydrate recognition element for galectin, the actual glycans present on various biomolecules, for example, cell surface proteoglycans, to which galectins bind, are far more complicated in situ than the simple recognition disaccharide.
Galectins by Anatole A. Klyosov, Zbigniew J. Witczak, David Platt
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