Literature DB >> 8416819

VAT-1 from Torpedo is a membranous homologue of zeta crystallin.

M Linial1, O Levius.   

Abstract

VAT-1 is a major protein from Torpedo synaptic vesicles. A protein data-base search revealed a striking homology to zeta crystallin from guinea pig lens. The overall amino-acid identity is 27%, and 58% similarity is reached by including conserved substitutions. The highest similarity (60% to 85%) between the two proteins is observed in five discrete domains, which are also conserved in zinc-dependent dehydrogenases, particularly in the alcohol dehydrogenase family. The cofactor-binding domain of oxidoreductases is conserved in VAT-1 and in zeta crystallin. VAT-1 preferably binds NADPH in the presence of zinc. In contrast with its homologous proteins, VAT-1 is an integral membrane protein of synaptic vesicles.

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Year:  1993        PMID: 8416819     DOI: 10.1016/0014-5793(93)81140-u

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  4 in total

1.  Structural basis for interorganelle phospholipid transport mediated by VAT-1.

Authors:  Yasunori Watanabe; Yasushi Tamura; Chika Kakuta; Seiya Watanabe; Toshiya Endo
Journal:  J Biol Chem       Date:  2020-01-31       Impact factor: 5.157

2.  Novel roles of VAT1 expression in the immunosuppressive action of diffuse gliomas.

Authors:  Pei Yang; Kuanyu Wang; Chuanbao Zhang; Zhiliang Wang; Qi Liu; Jiangfei Wang; Tao Jiang; Xia Shan
Journal:  Cancer Immunol Immunother       Date:  2021-02-12       Impact factor: 6.968

3.  Highly immunoreactive IgG antibodies directed against a set of twenty human proteins in the sera of patients with amyotrophic lateral sclerosis identified by protein array.

Authors:  Caroline May; Eckhard Nordhoff; Swaantje Casjens; Michael Turewicz; Martin Eisenacher; Ralf Gold; Thomas Brüning; Beate Pesch; Christian Stephan; Dirk Woitalla; Botond Penke; Tamás Janáky; Dezső Virók; László Siklós; Jozsef I Engelhardt; Helmut E Meyer
Journal:  PLoS One       Date:  2014-02-26       Impact factor: 3.240

4.  Neocarzilin A Is a Potent Inhibitor of Cancer Cell Motility Targeting VAT-1 Controlled Pathways.

Authors:  Carolin M-L Gleissner; Carolin L Pyka; Wolfgang Heydenreuter; Thomas F Gronauer; Carina Atzberger; Vadim S Korotkov; Weiting Cheng; Stephan M Hacker; Angelika M Vollmar; Simone Braig; Stephan A Sieber
Journal:  ACS Cent Sci       Date:  2019-06-18       Impact factor: 14.553

  4 in total

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