Literature DB >> 8839979

Sialic acids structure-analysis-metabolism-occurrence-recognition.

G Reuter1, H J Gabius.   

Abstract

Sialic acids are commonly positioned at non-reducing termini of complex carbohydrates. Steady refinements of analytical techniques have enabled detailed mapping of the complexity of sialic acids, unravelling a number of possibilities for substitutions. These developments have aided the description of the required enzymatic activities. In view of the physiological significance of this intriguing extent of variability of one sugar unit, the assumption that distinct types of sialic acids can serve as ligands in recognitive interactions is gaining support. It is reinforced by the discovery of several classes of mammalian lectins that bind sialo-glycoconjugates. Notably, an often encountered modification of sialic acids, namely O-acetylation, can be considered as a modulatory signal in recognition, either serving as contact point or masking a ligand structure. The increased knowledge of the physiological roles of sialic acids, for example in selectin-mediated leukocyte recruitment to sites of inflammation or in influenza virus propagation, even points to clinical applications. This perspective has led the field from the inherently descriptive beginning to technically sophisticated attempts for deliberate drug design.

Entities:  

Mesh:

Substances:

Year:  1996        PMID: 8839979     DOI: 10.1515/bchm3.1996.377.6.325

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN: 0177-3593


  13 in total

Review 1.  Plant lectins: occurrence, biochemistry, functions and applications.

Authors:  H Rüdiger; H J Gabius
Journal:  Glycoconj J       Date:  2001-08       Impact factor: 2.916

2.  Postcolumn HPLC detection of mono- and oligosaccharides with a chemosensor.

Authors:  Kyu Kwang Kim; Jorge O Escobedo; Nadia N St Luce; Oleksandr Rusin; Douglas Wong; Robert M Strongin
Journal:  Org Lett       Date:  2003-12-25       Impact factor: 6.005

3.  Initial events in infectious salmon anemia virus infection: evidence for the requirement of a low-pH step.

Authors:  T M Eliassen; M K Frøystad; B H Dannevig; M Jankowska; A Brech; K Falk; K Romøren; T Gjøen
Journal:  J Virol       Date:  2000-01       Impact factor: 5.103

Review 4.  Lectins: a primer for histochemists and cell biologists.

Authors:  Joachim C Manning; Antonio Romero; Felix A Habermann; Gabriel García Caballero; Herbert Kaltner; Hans-Joachim Gabius
Journal:  Histochem Cell Biol       Date:  2016-12-24       Impact factor: 4.304

Review 5.  Lipid glycosylation: a primer for histochemists and cell biologists.

Authors:  Jürgen Kopitz
Journal:  Histochem Cell Biol       Date:  2016-12-20       Impact factor: 4.304

6.  Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A.

Authors:  A van der Spoel; E Bonten; A d'Azzo
Journal:  EMBO J       Date:  1998-03-16       Impact factor: 11.598

Review 7.  Sweet complementarity: the functional pairing of glycans with lectins.

Authors:  H-J Gabius; J C Manning; J Kopitz; S André; H Kaltner
Journal:  Cell Mol Life Sci       Date:  2016-03-08       Impact factor: 9.261

8.  Rapid analysis of O-acetylated neuraminic acids by matrix assisted laser desorption/ionization time-of-flight mass spectrometry.

Authors:  P Stehling; M Gohlke; R Fitzner; W Reutter
Journal:  Glycoconj J       Date:  1998-04       Impact factor: 2.916

9.  Hypomorphic sialidase expression decreases serum cholesterol by downregulation of VLDL production in mice.

Authors:  Abraham Yang; Gabriel Gyulay; Mark Mitchell; Elizabeth White; Bernardo L Trigatti; Suleiman A Igdoura
Journal:  J Lipid Res       Date:  2012-09-14       Impact factor: 5.922

10.  The proteomic profile of hereditary inclusion body myopathy.

Authors:  Ilan Sela; Irit Milman Krentsis; Zipora Shlomai; Menachem Sadeh; Ron Dabby; Zohar Argov; Hannah Ben-Bassat; Stella Mitrani-Rosenbaum
Journal:  PLoS One       Date:  2011-01-31       Impact factor: 3.240

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.