Glycoconjugate Journal Impact Factor & Information

Publisher: Springer Verlag

Journal description

Glycoconjugate Journal publishes articles and reviews on all areas concerned with the composition degradation function interactions structure and synthesis of glycoconjugates (glycoproteins glycolipids oligosaccharides polysaccharides proteoglycans) including those aspects that are related to disease processes (eg immunological inflammatory and arthritic diseases infections metabolic disorders malignancy neurological disorders). Articles will be published on the organic synthesis of glycoconjugates and the development of methodologies only if biologically relevant. Articles on glycosylation changes in disease must focus either on the discovery of a novel disease marker or the improved understanding of some basic pathological mechanism. Also acceptable are articles on the effects of toxicological agents (alcohol tobacco narcotics environmental agents) on glycosylation and on the use of glycotherapeutics. Glycoconjugate Journal is the official journal of the International Glycoconjugate Organization which is responsible for organizing the biennial International Symposia on Glycoconjugates.

Current impact factor: 2.52

Impact Factor Rankings

2015 Impact Factor Available summer 2016
2014 Impact Factor 2.52
2013 Impact Factor 1.948
2012 Impact Factor 1.882
2011 Impact Factor 2.117
2010 Impact Factor 2.7
2009 Impact Factor 2.5
2008 Impact Factor 1.743
2007 Impact Factor 1.602
2006 Impact Factor 7.446
2005 Impact Factor 3.612
2004 Impact Factor 0.737
2003 Impact Factor 0.728
2002 Impact Factor 1.669
2001 Impact Factor 1.585
2000 Impact Factor 1.757
1999 Impact Factor 1.867
1998 Impact Factor 2.246
1997 Impact Factor 1.786
1996 Impact Factor 2.386
1995 Impact Factor 2.065
1994 Impact Factor 2.682
1993 Impact Factor 2.139
1992 Impact Factor 2.986

Impact factor over time

Impact factor

Additional details

5-year impact 2.01
Cited half-life >10.0
Immediacy index 0.41
Eigenfactor 0.00
Article influence 0.63
Website Glycoconjugate Journal website
Other titles Glycoconjugate journal (Online)
ISSN 0282-0080
OCLC 37662370
Material type Document, Periodical, Internet resource
Document type Internet Resource, Computer File, Journal / Magazine / Newspaper

Publisher details

Springer Verlag

  • Pre-print
    • Author can archive a pre-print version
  • Post-print
    • Author can archive a post-print version
  • Conditions
    • Author's pre-print on pre-print servers such as
    • Author's post-print on author's personal website immediately
    • Author's post-print on any open access repository after 12 months after publication
    • Publisher's version/PDF cannot be used
    • Published source must be acknowledged
    • Must link to publisher version
    • Set phrase to accompany link to published version (see policy)
    • Articles in some journals can be made Open Access on payment of additional charge
  • Classification

Publications in this journal

  • [Show abstract] [Hide abstract]
    ABSTRACT: The primary goal of this study was to develop a method to study the N-glycosylation of IgG from swine in order to detect epitopes containing N-glycolylneuraminic acid (Neu5Gc) and/or terminal galactose residues linked in α1-3 susceptible to cause xenograft-related problems. Samples of immunoglobulin were isolated from porcine serum using protein-A affinity chromatography. The eluate was then separated on electrophoretic gel, and bands corresponding to the N-glycosylated heavy chains were cut off the gel and subjected to tryptic digestion. Peptides and glycopeptides were separated by reversed phase liquid chromatography and fractions were collected for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric (MALDI-TOF-MS) analysis. Overall no α1-3 galactose was detected, as demonstrated by complete susceptibility of terminal galactose residues to β-galactosidase digestion. Neu5Gc was detected on singly sialylated structures. Two major N-glycopeptides were found, EEQFNSTYR and EAQFNSTYR as determined by tandem MS (MS/MS), as previously reported by Butler et al. (Immunogenetics, 61, 2009, 209-230), who found 11 subclasses for porcine IgG. Out of the 11, ten include the sequence corresponding to EEQFNSTYR, and only one codes for EAQFNSTYR. In this study, glycosylation patterns associated with both chains were slightly different, in that EEQFNSTYR had a higher content of galactose. The last step of this study consisted of peptide-mapping the 11 reported porcine IgG sequences. Although there was considerable overlap, at least one unique tryptic peptide was found per IgG sequence. The workflow presented in this manuscript constitutes the first study to use MALDI-TOF-MS in the investigation of porcine IgG structural features.
    Glycoconjugate Journal 11/2015; DOI:10.1007/s10719-015-9637-z
  • [Show abstract] [Hide abstract]
    ABSTRACT: Blood group oligosaccharides are one of the most clinically important antigen families and they may also act as secondary ligands for bacterial toxins from Escherichia coli and Vibrio cholerae. Herein we report the synthesis of spacered (sp = CH2CH2CH2NH2) glycosides of A antigen {α-D-GalNAc-(l→3)-[α-L-Fuc-(l→2)]-β-D-Gal-}, B antigen{α-D-Gal-(l→3)-[α-L-Fuc-(l→2)]-β-D-Gal-}, LewisX{α-D-Gal-(l→4)-[α-L-Fuc-(l→3)]-β-D-GlcNAc-}, A type-II {α-D-GalNAc-(l→3)-[α-L-Fuc-(l→2)]-β-D-Gal-(1→4)-β-D-GlcNAc-}, B type-II {α-D-Gal-(l→3)-[α-L-Fuc-(l→2)]-β-D-Gal-(1→4)-β-D-GlcNAc-}, H type-II{α-L-Fuc-(l→2)-β-D-Gal-(1→4)-β-D-GlcNAc-}, xenoantigen {α-D-Gal-(l→3)-β-D-Gal-(1→4)-[α-L-Fuc-(l→2)]-β-D-GlcNAc-} and Linear B Type II {α-D-Gal-(l→3)-β-D-Gal-(1→4)-β-D-GlcNAc-} useful for a range of biochemical investigations. This linker was chosen so as to facilitate the future conjugation of the antigens to proteins or other molecules. We also measured the affinities of some synthesized oligosaccharides against El Tor CTB strain from V. cholera.
    Glycoconjugate Journal 11/2015; DOI:10.1007/s10719-015-9635-1

  • Glycoconjugate Journal 09/2015; 32(8). DOI:10.1007/s10719-015-9617-3

  • Glycoconjugate Journal 08/2015; 32(6). DOI:10.1007/s10719-015-9598-2

  • Glycoconjugate Journal 06/2015; 32(5):173-342.
  • [Show abstract] [Hide abstract]
    ABSTRACT: This multi-authored book presents in 14 chapters an overview of the occurrence of sialic acids as constituents of glycoconjugates and summarises many biological and chemical aspects of these compounds. Each chapter is extensively documented by references, allowing the reader to retrieve the background. This book is well suited for master and PhD students in (structural) biology and for scientists interested in sialic acids.Here a short characterization of each chapter is given.J. Tiralongo describes in a comprehensive introductory chapter the chemical structure of the various sialic acids and their natural occurrence. Some biological features are covered as well. Explicit attention is paid to sialic-acid-binding proteins. The different properties of these proteins are discussed. C. Sato gives a detailed, descriptive account of glycocojugates bearing di-, oligo- or poly-sialic acid. Oligo/polysialo-glycocopnjugates play essential roles in biological systems from bacteria to humans. They ...
    Glycoconjugate Journal 02/2015; 32(1-2):77-78. DOI:10.1007/s10719-015-9575-9
  • Source
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    ABSTRACT: The complicated delivery mechanism of group II membrane proteins makes it difficult to decide the fusion pattern of their extracellular domains (ECDs) with Fc moiety. In this study, we compared the expression of ECDs of three group II membrane proteins including CLEC-2, Dectin-1, and LOX-1 by fusion of Fc moiety. We found that the pattern of ECD-Fc fusion order produced the functionally active recombinant proteins while the pattern of Fc-ECD fusion order led to the altered glycosylation which abolished the binding of these proteins with their ligands. Meanwhile, our results indicated that the secretion of mouse Fc (mFc)-fused ECD of CLEC-2 was more efficient than that of rabbit Fc (rFc)-fused protein, while rFc moiety was more sensitive for detection compared with mFc moiety. Altogether, we provide a favorable fusion pattern of Fc moiety with the ECDs of group II transmembrane proteins.
    Glycoconjugate Journal 12/2014; 32(1-2). DOI:10.1007/s10719-014-9571-5
  • [Show abstract] [Hide abstract]
    ABSTRACT: We have demonstrated that Bifidobacterium animalis subsp. lactis LKM512 had some probiotic properties in vivo and in vitro. To further understand their mechanisms, the chemical structure of the extracellular polysaccharide that constructs the cell envelope was determined. The strain was anaerobically cultured in MRS broth at 37 °C for 20 h, then the bacterial cells were harvested by centrifugation and washed. The cell wall-associated polysaccharide (CPS) was prepared from the cell wall component digested by lysozyme. The results of anion exchange and gel filtration chromatography showed that the polysaccharide was negatively charged and had a high molecular mass. The CPS was found to compose of galactopyranosyl, galactofuranosyl, glucopyranosyl and rhamnopyranosyl residues in the molar ratio of 1:1:1:3 by using methylation analysis with GC-MS and HPLC profiling. From the results of the structural characterization by 1 dimensional and 2 dimensional NMR spectroscopy, the polysaccharide was established to be a hexasaccharide repeating unit with the following structure:
    Glycoconjugate Journal 07/2014; 31(8). DOI:10.1007/s10719-014-9534-x

  • Glycoconjugate Journal 07/2014; 31(5):339-40. DOI:10.1007/s10719-014-9531-0
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    ABSTRACT: Four types of neutral glycosphingolipids (LacCer, Gb3Cer, Gb4Cer, and IV3αGalNAc-Gb4Cer; 10 pmol each) were analyzed using high-performance liquid chromatography (HPLC)-electrospray ionization quadrupole ion trap time-of-flight (ESI-QIT-TOF) mass spectrometry (MS) with a repeated high-speed polarity and MSn switching system. This system can provide six types of mass spectra, including positive and negative ion MS, MS2, and MS3 spectra, within 1 s per cycle. Using HPLC with a normal-phase column, information on the molecular weights of major molecular species of four neutral glycosphingolipids was obtained by detecting [M+Na]+ in the positive ion mode mass spectra and [M−H]− in the negative ion mode mass spectra. Sequences of glycosphingolipid oligosaccharide were obtained in the negative ion MS2 spectra. In addition, information on the ceramide structures was clearly obtained in the negative ion MS3 mass spectra. GlcCer molecular species were analyzed by HPLC-ESI-QIT-TOF MS with a reversed-phase column using 1 pmole of GlcCer. The structures of the seven molecular species of GlcCer, namely, d18:1-C16:0, d18:1-C18:0, d18:1-C20:0, d18:1-C22:0, d18:1-C23:0, d18:1-C24:1, and d18:1-C24:0, were characterized using positive ion MS and negative ion MS, MS2, and MS3. The established HPLC-ESI-QIT-TOF MS with MSn switching and a normal phase column has been successfully applied to the structural characterization of LacCer and Gb4Cer in a crude mixture prepared from human erythrocytes.
    Glycoconjugate Journal 12/2013; 30(9). DOI:10.1007/s10719-013-9492-8