Literature DB >> 8282566

Cellular sialoglycoconjugates: a histochemical perspective.

J Roth1.   

Abstract

Sialic acids are found at the non-reducing terminus of oligosaccharide side-chains of most glycoproteins and glycolipids. Their expression is often developmentally regulated during organogenesis and in differentiating cells. Further, differential expression of various sialyltransferases results in organ- and cell-type specific expression of sialylated glycosylation sequences. The availability of highly specific lectins and of monoclonal antibodies has permitted histochemical investigations of the various cellular and subcellular aspects of the process of sialylation. This review provides a survey on the developmentally regulated and organ- as well as cell-type specific expression of various sialoglycoconjugates and their tumour-associated occurrence with special reference to intestine and kidney.

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Year:  1993        PMID: 8282566     DOI: 10.1007/BF00211765

Source DB:  PubMed          Journal:  Histochem J        ISSN: 0018-2214


  112 in total

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Journal:  Trends Biochem Sci       Date:  1989-07       Impact factor: 13.807

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Journal:  J Histochem Cytochem       Date:  1989-11       Impact factor: 2.479

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  17 in total

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

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Journal:  Org Lett       Date:  2003-12-25       Impact factor: 6.005

Review 2.  From glycophenotyping by (plant) lectin histochemistry to defining functionality of glycans by pairing with endogenous lectins.

Authors:  Herbert Kaltner; Gabriel García Caballero; Anna-Kristin Ludwig; Joachim C Manning; Hans-Joachim Gabius
Journal:  Histochem Cell Biol       Date:  2018-05-05       Impact factor: 4.304

3.  Combining results from lectin affinity chromatography and glycocapture approaches substantially improves the coverage of the glycoproteome.

Authors:  Claudia A McDonald; Jane Y Yang; Vinita Marathe; Ten-Yang Yen; Bruce A Macher
Journal:  Mol Cell Proteomics       Date:  2008-10-15       Impact factor: 5.911

Review 4.  Protein glycosylation in the endoplasmic reticulum and the Golgi apparatus and cell type-specificity of cell surface glycoconjugate expression: analysis by the protein A-gold and lectin-gold techniques.

Authors:  J Roth
Journal:  Histochem Cell Biol       Date:  1996-07       Impact factor: 4.304

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Journal:  J Anat       Date:  1996-06       Impact factor: 2.610

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Authors:  Christopher T Saeui; Esteban Urias; Lingshu Liu; Mohit P Mathew; Kevin J Yarema
Journal:  Glycoconj J       Date:  2015-05-01       Impact factor: 2.916

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8.  Progressive multifocal leukoencephalopathy (PML) development is associated with mutations in JC virus capsid protein VP1 that change its receptor specificity.

Authors:  Leonid Gorelik; Carl Reid; Manuela Testa; Margot Brickelmaier; Simona Bossolasco; Annamaria Pazzi; Arabella Bestetti; Paul Carmillo; Ewa Wilson; Michele McAuliffe; Christopher Tonkin; John P Carulli; Alexey Lugovskoy; Adriano Lazzarin; Shamil Sunyaev; Kenneth Simon; Paola Cinque
Journal:  J Infect Dis       Date:  2011-07-01       Impact factor: 5.226

Review 9.  Lipid glycosylation: a primer for histochemists and cell biologists.

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

10.  Poly (alpha 2,8-deaminoneuraminic acid) is expressed in lung on a single 150-kDa glycoprotein and is an oncodevelopmental antigen.

Authors:  B Qu; M Ziak; C Zuber; J Roth
Journal:  Proc Natl Acad Sci U S A       Date:  1996-08-20       Impact factor: 11.205

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