Structural Basis for Substrate Preference of SMYD3, a SET Domain-containing Protein Lysine Methyltransferase.

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SET and MYND domain containing protein 3 in cancer.Therapeutical potential of deregulated lysine methyltransferase SMYD3 as a safe target for novel anticancer agents.ATM Signaling Pathway Is Implicated in the SMYD3-mediated Proliferation and Migration of Gastric Cancer Cells.

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P2860

Structural Basis for Substrate Preference of SMYD3, a SET Domain-containing Protein Lysine Methyltransferase.

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2016 nî lūn-bûn

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Structural Basis for Substrate ...... tein Lysine Methyltransferase.

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Structural Basis for Substrate ...... tein Lysine Methyltransferase.

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Structural Basis for Substrate ...... tein Lysine Methyltransferase.

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Structural Basis for Substrate ...... tein Lysine Methyltransferase.

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Bing Zhu

http://www.w3.org/2001/XMLSchema#string

Jinrong Min

http://www.w3.org/2001/XMLSchema#string

Mingzhu Wang

http://www.w3.org/2001/XMLSchema#string

Na Yang

http://www.w3.org/2001/XMLSchema#string

Nan Liu

http://www.w3.org/2001/XMLSchema#string

Qi Qiao

http://www.w3.org/2001/XMLSchema#string

Rui-Ming Xu

http://www.w3.org/2001/XMLSchema#string

Weiqi Fu

http://www.w3.org/2001/XMLSchema#string

P2860

Solution structure of the VEGF-binding domain of Flt-1: comparison of its free and bound states

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation.

Structural insights into the autoinhibition and posttranslational activation of histone methyltransferase SmyD3

Structural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA binding

Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3

Coot: model-building tools for molecular graphics

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Phasercrystallographic software

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9173-9180

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scholarly article

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10.1074/JBC.M115.709832

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English

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291

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2016-02-29T00:00:00Z

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4861483

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Structural Basis for Substrate Preference of SMYD3, a SET Domain-containing Protein Lysine Methyltransferase.

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P2860

P2860

Structural Basis for Substrate Preference of SMYD3, a SET Domain-containing Protein Lysine Methyltransferase.

description

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type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P698

P932