Literature DB >> 11350079

Identification of protein substrates for transglutaminase in Caenorhabditis elegans.

A Mádi1, Z Kele, T Janáky, M Punyiczki, L Fésüs.   

Abstract

Transglutaminase-dependent cross-linking of proteins leads to protein polymerisation that confers stability as well as resistance to mechanical disruption and chemical attack. Various transglutaminases have been implicated in a wide range of biological phenomena occurring in both extracellular and intracellular compartments, but further clarification of the physiological role of these enzymes requires identification of possible substrate molecules. Here we report the detection, purification, and identification of two proteins, enolase and ATP synthase alpha subunit as glutamine donor protein substrates for the transglutaminase of the nematode Caenorhabditis elegans. Copyright 2001 Academic Press.

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Year:  2001        PMID: 11350079     DOI: 10.1006/bbrc.2001.4872

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Analysis of transglutaminase protein substrates by functional proteomics.

Authors:  Margherita Ruoppolo; Stefania Orrù; Alfonsina D'Amato; Simona Francese; Paolo Rovero; Gennaro Marino; Carla Esposito
Journal:  Protein Sci       Date:  2003-06       Impact factor: 6.725

2.  Alpha-enolase involvement in intestinal and extraintestinal manifestations of celiac disease.

Authors:  Aaron Lerner; Polina Sobolevskaia; Leonid Churilov; Yehuda Shoenfeld
Journal:  J Transl Autoimmun       Date:  2021-06-16
  2 in total

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