Quantitative analysis of ERK2 interactions with substrate proteins: roles for kinase docking domains and activity in determining binding affinity (Q34509259)

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scientific article published on November 22, 2010

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English	Quantitative analysis of ERK2 interactions with substrate proteins: roles for kinase docking domains and activity in determining binding affinity	scientific article published on November 22, 2010

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scholarly article

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Europe PubMed Central

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2 August 2017

Quantitative analysis of ERK2 interactions with substrate proteins: roles for kinase docking domains and activity in determining binding affinity (English)

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2 August 2017

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Fengming Chen

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21098038

1 September 2024

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Paul Shapiro

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2 August 2017

Kimberly A. Burkhard

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1 September 2024

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22 November 2010

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2 August 2017

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http://www.jbc.org/article/S0021925820541197/pdf

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1 September 2024

http://intl.jbc.org/cgi/content/abstract/286/4/2477

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1 September 2024

https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21098038/pdf/?tool=EBI

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1 September 2024

https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21098038/?tool=EBI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21098038

1 September 2024

https://europepmc.org/articles/PMC3024742

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21098038

1 September 2024

https://europepmc.org/articles/PMC3024742?pdf=render

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21098038

1 September 2024

https://doi.org/10.1074/jbc.m110.177899

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1 September 2024

Journal of Biological Chemistry

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2 August 2017

286

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2 August 2017

4

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2 August 2017

2477-2485

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Europe PubMed Central

PubMed publication ID

2 August 2017

Noncatalytic function of ERK1/2 can promote Raf/MEK/ERK-mediated growth arrest signaling

1 reference

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7 July 2018

Effect of the DEF motif on phosphorylation of peptide substrates by ERK.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Targeting the Raf/MEK/ERK pathway with small-molecule inhibitors.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Substrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifs

1 reference

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7 July 2018

Advances in targeting the Ras/Raf/MEK/Erk mitogen-activated protein kinase cascade with MEK inhibitors for cancer therapy

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Unique MAP Kinase binding sites

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer

1 reference

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7 July 2018

Roles of the Raf/MEK/ERK pathway in cell growth, malignant transformation and drug resistance

1 reference

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7 July 2018

Mechanisms of MAPK signalling specificity

1 reference

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7 July 2018

The transcriptional ETS2 repressor factor associates with active and inactive Erks through distinct FXF motifs

1 reference

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7 July 2018

The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Quantifying ERK2-protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Coordinating ERK/MAPK signalling through scaffolds and inhibitors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Spatially separate docking sites on ERK2 regulate distinct signaling events in vivo

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Identification of a DEF-type docking domain for extracellular signal-regulated kinases 1/2 that directs phosphorylation and turnover of the BH3-only protein BimEL.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Protein-protein interactions in the regulation of the extracellular signal-regulated kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Phosphorylation-dependent changes in structure and dynamics in ERK2 detected by SDSL and EPR.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos by extracellular signal-regulated kinase mediates the transcriptional activation of AP-1 and cellular transformation induced by platelet-derived growth factor.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Assembly of Cell Regulatory Systems Through Protein Interaction Domains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Differential interaction of the tyrosine phosphatases PTP-SL, STEP and HePTP with the mitogen-activated protein kinases ERK1/2 and p38alpha is determined by a kinase specificity sequence and influenced by reducing agents

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Molecular interpretation of ERK signal duration by immediate early gene products

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Specificity determinants in MAPK signaling to transcription factors

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Expression and purification of recombinant human c-Fos/c-Jun that is highly active in DNA binding and transcriptional activation in vitro

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Multiple regions of MAP kinase phosphatase 3 are involved in its recognition and activation by ERK2.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Docking domains and substrate-specificity determination for MAP kinases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

ERK2 mitogen-activated protein kinase binding, phosphorylation, and regulation of the PDE4D cAMP-specific phosphodiesterases. The involvement of COOH-terminal docking sites and NH2-terminal UCR regions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

A conserved docking motif in MAP kinases common to substrates, activators and regulators

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Ribosomal S6 kinase 1 (RSK1) activation requires signals dependent on and independent of the MAP kinase ERK.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

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Extracellular signal-regulated kinase activates topoisomerase IIalpha through a mechanism independent of phosphorylation

1 reference

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7 July 2018

Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Identification of an extracellular signal-regulated kinase (ERK) docking site in ribosomal S6 kinase, a sequence critical for activation by ERK in vivo

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

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Activated raf induces the hyperphosphorylation of stathmin and the reorganization of the microtubule network.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

The Elk-1 ETS-domain transcription factor contains a mitogen-activated protein kinase targeting motif.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

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Kinetic analysis of biosensor data: elementary tests for self-consistency.

1 reference

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7 July 2018

Phosphorylation of c-Fos at the C-terminus enhances its transforming activity.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

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Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase

1 reference

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Molecular characterization of human stathmin expressed in Escherichia coli: site-directed mutagenesis of two phosphorylatable serines (Ser-25 and Ser-63)

1 reference

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The Mos/MAP kinase pathway stabilizes c-Fos by phosphorylation and augments its transforming activity in NIH 3T3 cells

1 reference

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7 July 2018

ERKs, extracellular signal-regulated MAP-2 kinases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3024742

7 July 2018

The docking interaction of caspase-9 with ERK2 provides a mechanism for the selective inhibitory phosphorylation of caspase-9 at threonine 125.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.177899

21 January 2018

PORE-ing over ERK substrates.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.177899

21 January 2018

Docking motif interactions in MAP kinases revealed by hydrogen exchange mass spectrometry

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.177899

21 January 2018

Docking sites on substrate proteins direct extracellular signal-regulated kinase to phosphorylate specific residues

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.177899

21 January 2018

A MAP kinase docking site is required for phosphorylation and activation of p90(rsk)/MAPKAP kinase-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.177899

21 January 2018

Detection of errors of interpretation in experiments in enzyme kinetics.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.177899

21 January 2018

The anti-apoptotic protein PEA-15 is a tight binding inhibitor of ERK1 and ERK2, which blocks docking interactions at the D-recruitment site.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.177899

21 January 2018

Calcium-mediated interactions regulate the subcellular localization of extracellular signal-regulated kinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.177899

21 January 2018

Dynamics of the Ras/ERK MAPK Cascade as Monitored by Fluorescent Probes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M110.177899

21 January 2018

Docking interactions induce exposure of activation loop in the MAP kinase ERK2

1 reference

https://pubmed.ncbi.nlm.nih.gov/21098038

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Selective targeting of MAPKs to the ETS domain transcription factor SAP-1

1 reference

https://pubmed.ncbi.nlm.nih.gov/21098038

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M110.177899

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

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