(Q41629497)

English

Direct synthesis of glycosylated amino acids from carbohydrate peracetates and Fmoc amino acids: solid-phase synthesis of biomedicinally interesting glycopeptides

scientific article published on January 1997

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

1 reference

Europe PubMed Central

Direct synthesis of glycosylated amino acids from carbohydrate peracetates and Fmoc amino acids: solid-phase synthesis of biomedicinally interesting glycopeptides (English)

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

1 reference

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author name string

Kihlberg J

1

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

Elofsson M

2

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

Salvador LA

3

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

language of work or name

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publication date

1 January 1997

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

Methods in Enzymology

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Europe PubMed Central

PubMed publication ID

5 October 2017

289

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

221-245

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

Protein glycosylation. Structural and functional aspects

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Biological roles of oligosaccharides: all of the theories are correct

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Glycobiology: Toward Understanding the Function of Sugars

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New glycosylpeptides with high antinociceptive activity

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Glycosylated peptide hormones: pharmacological properties and conformational studies of analogues of [1-desamino,8-D-arginine]vasopressin

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Solid-phase synthesis of O-glycopeptides

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Solid-phase synthesis of O-mannosylated peptides: two strategies compared

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9-Fluorenylmethoxycarbonyl amino-protecting group

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Improved method for the synthesis of o-glycosylated fmoc amino acids to be used in solid-phase glycopeptide synthesis (Fmoc = fluoren-9-ylmethoxycarbonyl)

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Synthesis of O-glycosylated tuftsins by utilizing threonine derivatives containing an unprotected monosaccharide moiety

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Building blocks for glycopeptide synthesis: glycosylation of 3-mercaptopropionic acid and Fmoc amino acids with unprotected carboxyl groups

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Solid-phase synthesis and conformational studies of glycosylated derivatives of helper-T-cell immunogenic peptides from hen-egg lysozyme.

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Synthesis of a water-soluble serine-based neoglycolipid which can be covalently linked to solid phases

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PapG adhesin from E. coli J96 recognizes the same saccharide epitope when present on whole bacteria and as isolated protein.

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Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70

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Glycosylation in the nucleus and cytoplasm

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Synthesis of a chromogenic proline-containing glycopeptide

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Solid-phase synthesis and conformational studies of helper T cell immunogenic peptides that carry carbohydrate haptens linked to serine

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Recent studies of the anomeric effect

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Silyl protection in the solid-phase synthesis of N-linked glycopeptides. Preparation of glycosylated fluorogenic substrates for subtilisins

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Preparation and application of the 5-(4-(9-fluorenylmethyloxycarbonyl)aminomethyl-3,5-dimethoxyphenoxy)-valeric acid (PAL) handle for the solid-phase synthesis of C-terminal peptide amides under mild conditions

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Susceptibility of glycans to beta-elimination in Fmoc-based O-glycopeptide synthesis.

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Fmoc-protected, glycosylated asparagines potentially useful as reagents in the solid-phase synthesis of N-glycopeptides

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Synthesis of glycopeptides and neoglycoproteins containing the fucosylated linkage region of N-glycoproteins

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Removal of Acyl Protective Groups from Glycopeptides: Base Does Not Epimerize Peptide Stereocenters, and beta-Elimination Is Slow

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Side Reactions in Peptide Synthesis

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Identifiers

10.1016/S0076-6879(97)89050-7

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

5 October 2017

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