Literature DB >> 19508859

Golgi linked protein glycosylation and associated diseases.

Daniel Ungar1.   

Abstract

One of the Golgi's main functions is the glycosylation of secreted proteins. A large variety of glycan chains can be synthesized in the Golgi, and it is increasingly clear that these are critical in basic cellular functions as well as the development of multicellular organisms. The structurally best-documented glycans are N-glycans, yet these are also the most enigmatic in their function. In contrast, O-glycan function is far better understood, but here the structures and biosynthetic pathways are very incomplete. The critical importance of glycans is highlighted by the broad spectrum of diseases they are associated with, such as a number of inherited diseases, but also cancers or diabetes. The molecular clues to these, however, are only just being elucidated. Although some glycan structures are known to be involved in signaling or adhesion to the extracellular matrix, for most the functions are not yet known. This review aims at summarizing current knowledge as much as to point out critical areas key for future progress.

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Year:  2009        PMID: 19508859     DOI: 10.1016/j.semcdb.2009.03.004

Source DB:  PubMed          Journal:  Semin Cell Dev Biol        ISSN: 1084-9521            Impact factor:   7.727


  29 in total

Review 1.  Retrograde vesicle transport in the Golgi.

Authors:  Nathanael P Cottam; Daniel Ungar
Journal:  Protoplasma       Date:  2011-12-12       Impact factor: 3.356

2.  Neurology of inherited glycosylation disorders.

Authors:  Hudson H Freeze; Erik A Eklund; Bobby G Ng; Marc C Patterson
Journal:  Lancet Neurol       Date:  2012-05       Impact factor: 44.182

3.  The susceptibility loci juvenile idiopathic arthritis shares with other autoimmune diseases extend to PTPN2, COG6, and ANGPT1.

Authors:  Susan D Thompson; Marc Sudman; Paula S Ramos; Miranda C Marion; Mary Ryan; Monica Tsoras; Tracey Weiler; Michael Wagner; Mehdi Keddache; J Peter Haas; Cornelia Mueller; Sampath Prahalad; John Bohnsack; Carol A Wise; Marilynn Punaro; Dongping Zhang; Carlos D Rosé; Mary E Comeau; Jasmin Divers; David N Glass; Carl D Langefeld
Journal:  Arthritis Rheum       Date:  2010-11

4.  Organizational interplay of Golgi N-glycosyltransferases involves organelle microenvironment-dependent transitions between enzyme homo- and heteromers.

Authors:  Antti Hassinen; Sakari Kellokumpu
Journal:  J Biol Chem       Date:  2014-08-18       Impact factor: 5.157

Review 5.  Golgi glycosylation and human inherited diseases.

Authors:  Hudson H Freeze; Bobby G Ng
Journal:  Cold Spring Harb Perspect Biol       Date:  2011-09-01       Impact factor: 10.005

Review 6.  Pharmacoperones as Novel Therapeutics for Diverse Protein Conformational Diseases.

Authors:  Ya-Xiong Tao; P Michael Conn
Journal:  Physiol Rev       Date:  2018-04-01       Impact factor: 37.312

7.  Characterization of glycosylation profiles of HIV-1 transmitted/founder envelopes by mass spectrometry.

Authors:  Eden P Go; Geetha Hewawasam; Hua-Xin Liao; Haiyan Chen; Li-Hua Ping; Jeffrey A Anderson; David C Hua; Barton F Haynes; Heather Desaire
Journal:  J Virol       Date:  2011-06-08       Impact factor: 5.103

Review 8.  Cell cycle regulation of Golgi membrane dynamics.

Authors:  Danming Tang; Yanzhuang Wang
Journal:  Trends Cell Biol       Date:  2013-02-28       Impact factor: 20.808

Review 9.  Glycosylation Quality Control by the Golgi Structure.

Authors:  Xiaoyan Zhang; Yanzhuang Wang
Journal:  J Mol Biol       Date:  2016-03-05       Impact factor: 5.469

10.  Changes in glycosylation of human blood plasma chitotriosidase in patients with type 2 diabetes.

Authors:  Ewa Żurawska-Płaksej; Ewa Maria Kratz; Mirosława Ferens-Sieczkowska; Maria Knapik-Kordecka; Agnieszka Piwowar
Journal:  Glycoconj J       Date:  2016-02       Impact factor: 2.916

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