(Q44292880)

1 December 2017

Phosphorylation of Raf-1 by p21-activated kinase 1 and Src regulates Raf-1 autoinhibition (English)

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1 December 2017

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Nancy H Tran

1

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PubMed ID

12551923

1 December 2017

Jeffrey A Frost

series ordinal

2

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PubMed ID

12551923

1 December 2017

language of work or name

English

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publication date

27 January 2003

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Journal of Biological Chemistry

1 December 2017

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1 December 2017

278

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1 December 2017

11221-11226

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1 December 2017

13

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Organization and regulation of mitogen-activated protein kinase signaling pathways

1 December 2017

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https://api.crossref.org/works/10.1074%2FJBC.M210318200

Mitogen-activated protein (MAP) kinase pathways: regulation and physiological functions

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M210318200

Mammalian MAP kinase signalling cascades

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

The complexity of Raf-1 regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Isotype-specific functions of Raf kinases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Untying the regulation of the Raf-1 kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

14-3-3 antagonizes Ras-mediated Raf-1 recruitment to the plasma membrane to maintain signaling fidelity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Serine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Positive and negative regulation of Raf kinase activity and function by phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Autoregulation of the Raf-1 serine/threonine kinase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Actions of Rho family small G proteins and p21-activated protein kinases on mitogen-activated protein kinase family members

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Differential effects of PAK1-activating mutations reveal activity-dependent and -independent effects on cytoskeletal regulation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

A target for Src in mitosis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Associations of B- and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: preferential binding of Raf to artificial lipid rafts.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Phosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biological signaling

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Rac-PAK signaling stimulates extracellular signal-regulated kinase (ERK) activation by regulating formation of MEK1-ERK complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

PAK1 primes MEK1 for phosphorylation by Raf-1 kinase during cross-cascade activation of the ERK pathway.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Activation of B-Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

A conserved negative regulatory region in alphaPAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Conformational switch and role of phosphorylation in PAK activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Phosphorylation of 338SSYY341 regulates specific interaction between Raf-1 and MEK1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

How MAP kinases are regulated

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

Raf-1-associated Protein Phosphatase 2A as a Positive Regulator of Kinase Activation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M210318200

21 January 2018

Identifiers

DOI

10.1074/JBC.M210318200

1 reference

1 December 2017

1 reference

PubMed ID

12551923