Bimolecular fluorescence complementation demonstrates that the c-Fes protein-tyrosine kinase forms constitutive oligomers in living cells.

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Small-Molecule Inhibitors of the c-Fes Protein-Tyrosine Kinase

P2860

Q27678635-8309CC74-4A06-4CAC-B6A8-C59BE3126B1F

P2860

Bimolecular fluorescence complementation demonstrates that the c-Fes protein-tyrosine kinase forms constitutive oligomers in living cells.

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http://www.wikidata.org/entity/Q35568709

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2009 nî lūn-bûn

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2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

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2009年論文

@zh-tw

2009年论文

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2009年论文

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2009年论文

@zh-cn

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Bimolecular fluorescence compl ...... ive oligomers in living cells.

@ast

Bimolecular fluorescence compl ...... ive oligomers in living cells.

@en

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Item

label

Bimolecular fluorescence compl ...... ive oligomers in living cells.

@ast

Bimolecular fluorescence compl ...... ive oligomers in living cells.

@en

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Bimolecular fluorescence compl ...... ive oligomers in living cells.

@ast

Bimolecular fluorescence compl ...... ive oligomers in living cells.

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P1476

Bimolecular fluorescence compl ...... ive oligomers in living cells.

@en

P2093

Jonathan M Shaffer

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

Sabine Hellwig

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

Thomas E Smithgall

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

P2860

A point mutation in the N-terminal coiled-coil domain releases c-Fes tyrosine kinase activity and survival signaling in myeloid leukemia cells

Closing in on the biological functions of Fps/Fes and Fer

The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly

Regulation of the human c-fes protein tyrosine kinase (p93c-fes) by its src homology 2 domain and major autophosphorylation site (Tyr-713)

Contributions of F-BAR and SH2 domains of Fes protein tyrosine kinase for coupling to the FcepsilonRI pathway in mast cells.

Co-expression with BCR induces activation of the FES tyrosine kinase and phosphorylation of specific N-terminal BCR tyrosine residues

K562 leukemia cells transfected with the human c-fes gene acquire the ability to undergo myeloid differentiation

Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation

Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations

Crystal structures of c-Src reveal features of its autoinhibitory mechanism

P304

4780-4788

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P31

scholarly article

P356

10.1021/BI900238F

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P407

English

P433

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P478

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

P577

2009-06-01T00:00:00Z

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

P5875

24344951

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P698

19382747

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

P932

3222594

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

Bimolecular fluorescence complementation demonstrates that the c-Fes protein-tyrosine kinase forms constitutive oligomers in living cells.

about

P2860

P2860

Bimolecular fluorescence complementation demonstrates that the c-Fes protein-tyrosine kinase forms constitutive oligomers in living cells.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P932