Special Issue "Glycosylation and Glycoproteins"

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A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry, Molecular Biology and Biophysics".

Deadline for manuscript submissions: closed (30 December 2013)

Special Issue Editors

Guest Editor
Prof. Dr. Patricia Berninsone
Department of Biology, University of Nevada Reno, Reno, Nevada, USA
Website: http://www.unr.edu/biology/people/patricia-berninsone
E-Mail: berninsone@unr.edu
Interests: protein glycosylation, regulation of glycosylation reactions, roles of glycosylation in development and disease.

Co-Guest Editor
Dr. Joe Tiralongo
Institute for Glycomics, Gold Coast Campus, Griffith University, Queensland 4222, Australia
Website: http://research-hub.griffith.edu.au/display/n1fa060133beb3d3fc2ab57b0020384a2
E-Mail: j.tiralongo@griffith.edu.au

Special Issue Information

Dear Colleagues,

Sugars, which represent one of the four fundamental building blocks of life, are the most abundant biological molecules on our planet. Sugars can be combined in a myriad number of ways to form complex carbohydrate structures (glycans). The glycan repertoire (glycome) of a given cell or organism is thus many orders of magnitude more complex than the genome or the proteome. However, only over the past two decades have we begun to truly appreciate the extent to which glycan function permeates biological systems, including human health and disease.
Glycosylation is the process by which a sugar is enzymatically attached to proteins, lipids, or other organic molecules. In particular, glycosylation increases protein diversity and structure, and as such significantly impacts on the function of the resulting glycoprotein.
As the roles of glycosylation in physiological and pathological processes are increasingly being recognized, the field of glycobiology is eliciting an unprecedented interest. However, the extreme complexity and structural diversity of glycans, combined with their “non-template”-driven synthesis, pose a significant technical challenge that has stimulated advances in the field.
This Special Issue will welcome contributions in all areas of glycobiology, including studies on the function of glycans in basic biological processes and human diseases, and the regulation of glycosylation reactions in vivo, as well as technical advances to analyze the complexities of the glycoproteome.

Prof. Dr. Patricia Berninsone
Dr. Joe Tiralongo
Guest Editors

Submission

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are refereed through a peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed Open Access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1600 CHF.

Keywords

  • glycosylation
  • carbohydrate
  • glycosyl donor
  • glycosyl acceptor
  • glycan
  • protein
  • lipid
  • co-translation
  • post-translation
  • glypiation
  • glycosidic bond
  • mannosylation
  • oligosaccharide chain
  • glycoprotein
  • protein
  • mucins
  • glycoprotein IIb/IIIa
  • zona pellucida
  • miraculin
  • transferrin
  • ceruloplasmin
  • immunoglobins
  • histocompatibility antigens
  • human chorionic gonadotropin (HCG)
  • thyroid-stimulating hormone (TSH)
  • patatin
  • lectin
  • selectin
  • calnexin
  • calreticulin

Published Papers (11 papers)

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Displaying article 1-11
p. 6356-6377
by , , ,  and
Int. J. Mol. Sci. 2014, 15(4), 6356-6377; doi:10.3390/ijms15046356
Received: 9 December 2013; in revised form: 25 February 2014 / Accepted: 4 April 2014 / Published: 15 April 2014
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
p. 4965-4976
by , , ,  and
Int. J. Mol. Sci. 2014, 15(3), 4965-4976; doi:10.3390/ijms15034965
Received: 7 February 2014; in revised form: 6 March 2014 / Accepted: 13 March 2014 / Published: 20 March 2014
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
p. 4492-4522
by , , , , ,  and
Int. J. Mol. Sci. 2014, 15(3), 4492-4522; doi:10.3390/ijms15034492
Received: 28 December 2013; in revised form: 7 February 2014 / Accepted: 21 February 2014 / Published: 14 March 2014
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
p. 3768-3783
by  and
Int. J. Mol. Sci. 2014, 15(3), 3768-3783; doi:10.3390/ijms15033768
Received: 26 December 2013; in revised form: 17 February 2014 / Accepted: 21 February 2014 / Published: 3 March 2014
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
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p. 2840-2857
by  and
Int. J. Mol. Sci. 2014, 15(2), 2840-2857; doi:10.3390/ijms15022840
Received: 4 January 2014; in revised form: 20 January 2014 / Accepted: 27 January 2014 / Published: 19 February 2014
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
p. 2305-2326
by , , , ,  and
Int. J. Mol. Sci. 2014, 15(2), 2305-2326; doi:10.3390/ijms15022305
Received: 25 November 2013; in revised form: 13 January 2014 / Accepted: 23 January 2014 / Published: 7 February 2014
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
p. 159-170
by , , , ,  and
Int. J. Mol. Sci. 2014, 15(1), 159-170; doi:10.3390/ijms15010159
Received: 23 November 2013; in revised form: 3 December 2013 / Accepted: 13 December 2013 / Published: 23 December 2013
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
p. 23188-23202
by , , , , , , , , , ,  and
Int. J. Mol. Sci. 2013, 14(11), 23188-23202; doi:10.3390/ijms141123188
Received: 18 September 2013; in revised form: 22 October 2013 / Accepted: 31 October 2013 / Published: 21 November 2013
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
p. 20890-20912
by ,  and
Int. J. Mol. Sci. 2013, 14(10), 20890-20912; doi:10.3390/ijms141020890
Received: 29 August 2013; in revised form: 20 September 2013 / Accepted: 8 October 2013 / Published: 17 October 2013
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
p. 20555-20563
by , , ,  and
Int. J. Mol. Sci. 2013, 14(10), 20555-20563; doi:10.3390/ijms141020555
Received: 28 August 2013; in revised form: 24 September 2013 / Accepted: 27 September 2013 / Published: 14 October 2013
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
p. 16986-16998
by , , , ,  and
Int. J. Mol. Sci. 2013, 14(8), 16986-16998; doi:10.3390/ijms140816986
Received: 2 July 2013; in revised form: 7 August 2013 / Accepted: 8 August 2013 / Published: 19 August 2013
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(This article belongs to the Special Issue Glycosylation and Glycoproteins)
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Last update: 19 August 2013

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert