Catalytic mechanism of Golgi-resident human tyrosylprotein sulfotransferase-2: a mass spectrometry approach - Test2 - elhamkhani - TriplyDB

Catalytic mechanism of Golgi-resident human tyrosylprotein sulfotransferase-2: a mass spectrometry approach

Catalytic mechanism of Golgi-resident human tyrosylprotein sulfotransferase-2: a mass spectrometry approach

http://www.wikidata.org/entity/Q24599656

about

Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction Fluorescence assay for protein post-translational tyrosine sulfation Direct identification of tyrosine sulfation by using ultraviolet photodissociation mass spectrometry Simultaneous identification of tyrosine phosphorylation and sulfation sites utilizing tyrosine-specific bromination.Fragment-based optimization of small molecule CXCL12 inhibitors for antagonizing the CXCL12/CXCR4 interaction.Preparation and Analysis of N-Terminal Chemokine Receptor Sulfopeptides Using Tyrosylprotein Sulfotransferase Enzymes.LC-MS and LC-MS/MS studies of incorporation of 34SO3 into glycosaminoglycan chains by sulfotransferases.The structural role of receptor tyrosine sulfation in chemokine recognition.Tyrosine sulfation as a protein post-translational modification.New tools for evaluating protein tyrosine sulfation: tyrosylprotein sulfotransferases (TPSTs) are novel targets for RAF protein kinase inhibitors

P2860

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P2860

Catalytic mechanism of Golgi-resident human tyrosylprotein sulfotransferase-2: a mass spectrometry approach

http://www.wikidata.org/entity/Q24599656

description

2010 nî lūn-bûn

@nan

2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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prefLabel

Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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J.JASMS.2010.03.037

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Journal of the American Society for Mass Spectrometry

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Catalytic mechanism of Golgi-r ...... : a mass spectrometry approach

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Julie A Leary

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Kevin L Moore

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Lieza M Danan

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Peter J Ludden

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Weitao Jia

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Zhihao Yu

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P2860

Crystal structure of the human estrogen sulfotransferase-PAPS complex: evidence for catalytic role of Ser137 in the sulfuryl transfer reaction

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

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

(Glu62, Ala30, Tyr8)n serves as high-affinity substrate for tyrosylprotein sulfotransferase: a Golgi enzyme

Multiple sequence alignment with the Clustal series of programs

A structural and biochemical basis for PAPS-independent sulfuryl transfer by aryl sulfotransferase from uropathogenic Escherichia coli

Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate

The crystal structure of succinyl-CoA synthetase from Escherichia coli at 2.5-A resolution

Crystal structure of estrogen sulphotransferase

The sulfuryl transfer mechanism. Crystal structure of a vanadate complex of estrogen sulfotransferase and mutational analysis

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j.jasms.2010.03.037

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1633-42

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scholarly article

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10.1016/J.JASMS.2010.03.037

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9

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1040603570

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structural biology

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