Literature DB >> 8033259

Protein tyrosine sulfation, 1993--an update.

C Niehrs1, R Beisswanger, W B Huttner.   

Abstract

Sulfation is the most abundant post-translational modification of tyrosine residues and occurs in many soluble and membrane proteins passing through the secretory pathway of metazoan cells. The sulfation reaction is catalysed by tyrosylprotein sulfotransferase, a membrane-bound enzyme of the trans-Golgi-network. Tyrosylprotein sulfotransferase has been purified and its substrate specificity characterized. Tyrosine sulfation has been shown to be important for protein-protein interactions occurring during the intracellular transport of proteins and upon their secretion.

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Year:  1994        PMID: 8033259     DOI: 10.1016/0009-2797(94)90068-x

Source DB:  PubMed          Journal:  Chem Biol Interact        ISSN: 0009-2797            Impact factor:   5.192


  13 in total

1.  Sulfation, the up-and-coming post-translational modification: its role and mechanism in protein-protein interaction.

Authors:  Amina S Woods; Hay-Yan J Wang; Shelley N Jackson
Journal:  J Proteome Res       Date:  2007-01-26       Impact factor: 4.466

Review 2.  Updated perspectives on the cytosolic sulfotransferases (SULTs) and SULT-mediated sulfation.

Authors:  Masahito Suiko; Katsuhisa Kurogi; Takuyu Hashiguchi; Yoichi Sakakibara; Ming-Cheh Liu
Journal:  Biosci Biotechnol Biochem       Date:  2016-09-21       Impact factor: 2.043

3.  Prediction of tyrosine sulfation in seven-transmembrane peptide receptors.

Authors:  Kristine M Yu; Justin Liu; Ryan Moy; Henry C Lin; Hugh B Nicholas; Grace L Rosenquist
Journal:  Endocrine       Date:  2002-12       Impact factor: 3.633

4.  Existence of distinct tyrosylprotein sulfotransferase genes: molecular characterization of tyrosylprotein sulfotransferase-2.

Authors:  R Beisswanger; D Corbeil; C Vannier; C Thiele; U Dohrmann; R Kellner; K Ashman; C Niehrs; W B Huttner
Journal:  Proc Natl Acad Sci U S A       Date:  1998-09-15       Impact factor: 11.205

5.  Tyrosylprotein sulfotransferase: purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, a common posttranslational modification of eukaryotic proteins.

Authors:  Y b Ouyang; W S Lane; K L Moore
Journal:  Proc Natl Acad Sci U S A       Date:  1998-03-17       Impact factor: 11.205

6.  A target-specific approach for the identification of tyrosine-sulfated hemostatic proteins.

Authors:  Tzu-An Liu; Shin Yasuda; Frederick E Williams; Ming-Yih Liu; Masahito Suiko; Yoichi Sakakibara; Yuh-Shyong Yang; Ming-Cheh Liu
Journal:  Anal Biochem       Date:  2009-04-05       Impact factor: 3.365

7.  Ionic milieu controls the compartment-specific activation of pro-opiomelanocortin processing in AtT-20 cells.

Authors:  W K Schmidt; H P Moore
Journal:  Mol Biol Cell       Date:  1995-10       Impact factor: 4.138

8.  Tyrosine modification enhances metal-ion binding.

Authors:  Graham S Baldwin; Michael F Bailey; B Philip Shehan; Ioulia Sims; Raymond S Norton
Journal:  Biochem J       Date:  2008-11-15       Impact factor: 3.857

Review 9.  The multi-protein family of sulfotransferases in plants: composition, occurrence, substrate specificity, and functions.

Authors:  Felix Hirschmann; Florian Krause; Jutta Papenbrock
Journal:  Front Plant Sci       Date:  2014-10-16       Impact factor: 5.753

10.  Tyrosine O-sulfation promotes proteolytic processing of progastrin.

Authors:  J R Bundgaard; J Vuust; J F Rehfeld
Journal:  EMBO J       Date:  1995-07-03       Impact factor: 11.598

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