Methods to Study Protein Tyrosine Phosphatases Acting on Yeast MAPKs.

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Methods to Study Protein Tyrosine Phosphatases Acting on Yeast MAPKs.

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2016 nî lūn-bûn

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2016年の論文

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年学术文章

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2016年學術文章

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2016年學術文章

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Methods to Study Protein Tyrosine Phosphatases Acting on Yeast MAPKs.

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Methods to Study Protein Tyrosine Phosphatases Acting on Yeast MAPKs.

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Methods to Study Protein Tyrosine Phosphatases Acting on Yeast MAPKs.

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Methods to Study Protein Tyrosine Phosphatases Acting on Yeast MAPKs.

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Methods to Study Protein Tyrosine Phosphatases Acting on Yeast MAPKs.

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Methods to Study Protein Tyrosine Phosphatases Acting on Yeast MAPKs.

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P1476

Methods to Study Protein Tyrosine Phosphatases Acting on Yeast MAPKs

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P2093

Almudena Sacristán-Reviriego

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María Molina

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P2860

Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.

The protein kinases of budding yeast: six score and more.

Regulation of the Saccharomyces cerevisiae HOG1 mitogen-activated protein kinase by the PTP2 and PTP3 protein tyrosine phosphatases.

Yeast RLM1 encodes a serum response factor-like protein that may function downstream of the Mpk1 (Slt2) mitogen-activated protein kinase pathway.

Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast

Signaling and circuitry of multiple MAPK pathways revealed by a matrix of global gene expression profiles

Combinatorial control of the specificity of protein tyrosine phosphatases.

Dual-specificity MAP kinase phosphatases (MKPs): shaping the outcome of MAP kinase signalling.

Substrate-trapping techniques in the identification of cellular PTP targets.

From form to function: signaling by protein tyrosine phosphatases.

P304

385-398

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P31

scholarly article

P356

10.1007/978-1-4939-3746-2_21

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P407

English

P478

1447

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P50

H Martín

P577

2016-01-01T00:00:00Z

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P698

27514817

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