Results 191 to 200 of about 26,625 (243)
Uncovering antimicrobial resistance structures in <i>Staphylococcus</i> spp. from companion animals: latent class analysis of isolates from dogs. [PDF]
Front Vet SciCastro A +6 more
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Comparative N-Glycoproteomics Reveals Subtype-Specific N-Glycosylation Signatures and Immune Associations in Cholangiocarcinoma. [PDF]
Mol Cell ProteomicsXia Z +18 more
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Glycoprotein-Notebook: A Pan-Cancer Glycoproteomic Database and Toolkit for Analysis of Protein Glycosylation Changes Associated With Cancer Phenotypes. [PDF]
Mol Cell ProteomicsZhang H, Hoang T, Hu Y.
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Current Medicinal Chemistry, 2001
Resistance to glycopeptides in enterococci, which first emerged in the late 1980's and is now widespread mainly in the United States, is posing a serious clinical problem due to the lack of alternative and efficacious therapeutic options, particularly against infections caused by VanA strains that are highly resistant to glycopeptides and almost all ...
A, Malabarba, R, Ciabatti
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Resistance to glycopeptides in enterococci, which first emerged in the late 1980's and is now widespread mainly in the United States, is posing a serious clinical problem due to the lack of alternative and efficacious therapeutic options, particularly against infections caused by VanA strains that are highly resistant to glycopeptides and almost all ...
A, Malabarba, R, Ciabatti
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Glycopeptides and nephrotoxicity
Intensive Care Medicine, 1994Infections due to Gram-positive bacteria have become an increasing problem in the ICU. Furthermore, multidrug resistance among Gram-positive pathogens is increasingly recognized. Empirical therapy with antibiotic regimens that are effective against Gram-positive pathogens is often required in the ICU.
A W, Chow, R M, Azar
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Mini-Reviews in Medicinal Chemistry, 2003
The presence of carbohydrate side-chains in native glycoproteins alters a number of biochemical properties of the peptide backbone. One of the most frequently studied questions is the conformation-modifying effect of sugar incorporation into asparagine, serine and threonine residues.
Laszlo, Otvos, Mare, Cudic
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The presence of carbohydrate side-chains in native glycoproteins alters a number of biochemical properties of the peptide backbone. One of the most frequently studied questions is the conformation-modifying effect of sugar incorporation into asparagine, serine and threonine residues.
Laszlo, Otvos, Mare, Cudic
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2010
Oligosaccharides in protein play important roles in several biological events. In order to investigate the functions of oligosaccharides of protein, glycoproteins having homogeneous oligosaccharides should be prepared. For this purpose, preparation methods of diverse complex-type oligosaccharides as well as synthetic methods of glycopeptides are ...
Yasuhiro, Kajihara +3 more
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Oligosaccharides in protein play important roles in several biological events. In order to investigate the functions of oligosaccharides of protein, glycoproteins having homogeneous oligosaccharides should be prepared. For this purpose, preparation methods of diverse complex-type oligosaccharides as well as synthetic methods of glycopeptides are ...
Yasuhiro, Kajihara +3 more
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Current Protocols in Molecular Biology, 1995
AbstractGeneration of glycopeptides from glycoproteins is frequently useful when analyzing a protein's oligosaccharide side chains. Freed from the bulk of the polypeptide backbone by proteolysis, glycopeptides can be characterized by a variety of techniques.
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AbstractGeneration of glycopeptides from glycoproteins is frequently useful when analyzing a protein's oligosaccharide side chains. Freed from the bulk of the polypeptide backbone by proteolysis, glycopeptides can be characterized by a variety of techniques.
openaire +2 more sources