gopubmed logo
 
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Tyrosylprotein sulfotransferase 1

tyrosylprotein sulfotransferase, TPST-1, tyrosylprotein sulfotransferase-1
Top mentioned proteins: TPST2, ACID, CAN, fibrillin-1, CD45
Papers on tyrosylprotein sulfotransferase
Glycan modulation and sulfoengineering of anti-HIV-1 monoclonal antibody PG9 in plants.
New
Mach et al., Vienna, Austria. In Proc Natl Acad Sci U S A, Nov 2015
Both antibodies were efficiently sulfated in planta on coexpression of an engineered human tyrosylprotein sulfotransferase, resulting in antigen-binding and virus neutralization activities equivalent to PG9 synthesized by mammalian cells ((CHO)PG9).
Tyrosylprotein sulfotransferase 1 expression is negatively correlated with c‑Met and lymph node metastasis in human lung cancer.
New
Jin et al., Changsha, China. In Mol Med Report, Oct 2015
The present study aimed to test the expression of tyrosylprotein sulfotransferase 1 (TPST‑1) in human lung cancer and to analyze the correlation with clinicopathologic features and c‑Met expression levels.
Phytosulfokine peptide signalling.
Review
New
Sauter, Kiel, Germany. In J Exp Bot, Aug 2015
Processing of the preproprotein involves sulfonylation by a tyrosylprotein sulfotransferase in the trans-golgi and proteolytic cleavage in the apoplast.
An Arabidopsis thaliana copper-sensitive mutant suggests a role of phytosulfokine in ethylene production.
New
Fujiwara et al., Harbin, China. In J Exp Bot, Jul 2015
The positional cloning of tpst-2 revealed that this gene encodes a tyrosylprotein sulfotransferase (TPST).
Phytosulfokine peptide signaling controls pollen tube growth and funicular pollen tube guidance in Arabidopsis thaliana.
New
Sauter et al., Kiel, Germany. In Physiol Plant, Apr 2015
Phytosulfokine (PSK) is a peptide growth factor that requires tyrosine sulfation carried out by tyrosylprotein sulfotransferase (TPST) for its activity.
Heterodimers of tyrosylprotein sulfotransferases suggest existence of a higher organization level of transferases in the membrane of the trans-Golgi apparatus.
New
Bayer et al., Essen, Germany. In J Mol Biol, Apr 2015
The sole two human enzymes that transfer sulfate moieties from 3'-phospho-adenosine-5'-phospho-sulfate onto tyrosine residues, TPST1 and TPST2, are anchored to the membranes of the trans-Golgi compartment with the catalytic domain oriented to the lumen.
Genetic variation in microRNA-binding site and prognosis of patients with colorectal cancer.
Choi et al., Taegu, South Korea. In J Cancer Res Clin Oncol, 2015
In the validation cohort, two SNPs (TPST1 rs3757417T>G and PAUF rs12373A>C) were significantly associated with prognosis in the same direction as the discovery cohort when adjusted for age, preoperative carcinoembryonic antigen level, and pathologic stage (discovery + validation cohort; TPST1 rs3757417T>G, disease-free survival (DFS), p value = 0.0004, overall survival (OS), p value = 0.01 in recessive model; PAUF rs12373A>C, DFS, p value = <0.0001,
Tyrosine sulfation as a protein post-translational modification.
Review
Mao et al., Yü-ching, Taiwan. In Molecules, 2014
PTS is catalyzed by tyrosylprotein sulfotransferase (TPST) through transfer of an activated sulfate from 3'-phosphoadenosine-5'-phosphosulfate to tyrosine in a variety of proteins and peptides.
Fluorescent peptide sensors for tyrosylprotein sulfotransferase activity.
Geraghty et al., Minneapolis, United States. In Anal Biochem, 2014
Tyrosine sulfurylation is a post-translational modification important for protein-protein interactions in the extracellular space that are instrumental in cell adhesion, cell signaling, immune responses, and pathogen recognition of host cells.
Structural and energetic determinants of tyrosylprotein sulfotransferase sulfation specificity.
Ding et al., United States. In Bioinformatics, 2014
MOTIVATION: Tyrosine sulfation is a type of post-translational modification (PTM) catalyzed by tyrosylprotein sulfotransferases (TPST).
Suppression of Photosynthetic Gene Expression in Roots Is Required for Sustained Root Growth under Phosphate Deficiency.
Liu et al., Beijing, China. In Plant Physiol, 2014
HPS7 encodes a tyrosylprotein sulfotransferase.
Cerebral cortical hypoplasia with abnormal morphology of pyramidal neuron in growth-retarded mouse (grt/grt).
Sawada et al., Tsukuba, Japan. In Acta Neurobiol Exp (wars), 2013
The purpose of this study was to quantitatively characterize structural abnormalities of the cerebrum in a growth-retarded mouse (grt/grt) with a tyrosylprotein sulfotransferase 2 gene defect.
Identification of novel innate immune genes by transcriptional profiling of macrophages stimulated with TLR ligands.
GeneRIF
Pisetsky et al., Denver, United States. In Mol Immunol, 2011
two genes identified in this analysis, PLEC1 and TPST1, reduced IL-6 production by macrophages
Tyrosine sulfation of native mouse Psgl-1 is required for optimal leukocyte rolling on P-selectin in vivo.
GeneRIF
Moore et al., Oklahoma City, United States. In Plos One, 2010
Data show that Tpst1/Tpst2 DKO leukocytes bound less P-selectin than wild type leukocytes despite equivalent surface expression of Psgl-1.
Lack of protein-tyrosine sulfation disrupts photoreceptor outer segment morphogenesis, retinal function and retinal anatomy.
GeneRIF
Al-Ubaidi et al., Oklahoma City, United States. In Eur J Neurosci, 2010
These results indicate that protein-tyrosine sulfation by Tpst1/2 is essential for proper outer segment morphogenesis and synaptic function, but is not critical for overall retinal structure or synapse formation.
Tyrosine sulfation: an increasingly recognised post-translational modification of secreted proteins.
Review
Zhu et al., Australia. In N Biotechnol, 2009
Recent advances in our understanding of protein tyrosine sulfation have come about owing to the cloning of two human tyrosylprotein sulfotransferases (TPST-1 and TPST-2), the development of novel analytical and synthetic methodologies and detailed studies of proteins and peptides containing sulfotyrosine residues.
Mass spectrometric kinetic analysis of human tyrosylprotein sulfotransferase-1 and -2.
GeneRIF
Leary et al., Davis, United States. In J Am Soc Mass Spectrom, 2008
The kinetic parameters of tyrosylprotein sulfotransferase-1 and -2, catalyzing tyrosine sulfation of CCR8 peptides, were determined using liquid chromatography electrospray ionisation mass spectrometry.
Early postnatal pulmonary failure and primary hypothyroidism in mice with combined TPST-1 and TPST-2 deficiency.
GeneRIF
Moore et al., Oklahoma City, United States. In Gen Comp Endocrinol, 2008
Tpst1 and Tpst2 are the only Tpst genes in mice, tyrosine sulfation is required for normal pulmonary function at birth, and TPST-2 is required for normal thyroid gland function.
Protein tyrosine sulfation, 1993--an update.
Review
Huttner et al., Heidelberg, Germany. In Chem Biol Interact, 1994
The sulfation reaction is catalysed by tyrosylprotein sulfotransferase, a membrane-bound enzyme of the trans-Golgi-network.
Tyrosine sulfation and the secretory pathway.
Review
Huttner, Heidelberg, Germany. In Annu Rev Physiol, 1987
The sulfation reaction is catalyzed by tyrosylprotein sulfotransferase, an integral membrane protein that recognizes tyrosine residues in exposed protein domains containing acidic amino acids.
share on facebooktweetadd +1mail to friends