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The Akt-SRPK-SR Axis Constitutes a Major Pathway in Transducing EGF Signaling to Regulate Alternative Splicing in the Nucleus

Molecular cell, 2012-08, Vol.47 (3), p.422-433

2012

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Phosphorylation mechanism and structure of serine-arginine protein kinases

The FEBS journal, 2011-02, Vol.278 (4), p.587-597

2011

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Matrix Rigidity Controls Epithelial-Mesenchymal Plasticity and Tumor Metastasis via a Mechanoresponsive EPHA2/LYN Complex

Developmental cell, 2020-08, Vol.54 (3), p.302-316.e7

2020

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Release of SR Proteins from CLK1 by SRPK1: A Symbiotic Kinase System for Phosphorylation Control of Pre-mRNA Splicing

Molecular cell, 2016-07, Vol.63 (2), p.218-228

2016

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Kinetic and Catalytic Mechanisms of Protein Kinases

Chemical reviews, 2001-08, Vol.101 (8), p.2271-2290

Adams, Joseph A

2001

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Initiation of Parental Genome Reprogramming in Fertilized Oocyte by Splicing Kinase SRPK1-Catalyzed Protamine Phosphorylation

Cell, 2020-03, Vol.180 (6), p.1212-1227.e14

2020

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Molecular interactions connecting the function of the serine-arginine–rich protein SRSF1 to protein phosphatase 1

The Journal of biological chemistry, 2018-10, Vol.293 (43), p.16751-16760

2018

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Redirecting SR Protein Nuclear Trafficking through an Allosteric Platform

Journal of molecular biology, 2017-07, Vol.429 (14), p.2178-2191

2017

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Partitioning RS Domain Phosphorylation in an SR Protein through the CLK and SRPK Protein Kinases

Journal of molecular biology, 2013-08, Vol.425 (16), p.2894-2909

2013

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Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases

PLoS biology, 2016-11, Vol.14 (11), p.e2000127-e2000127

2016

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Structural Basis for the Regulation of Protein Kinase A by Activation Loop Phosphorylation

The Journal of biological chemistry, 2012-04, Vol.287 (18), p.14672-14680

2012

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Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function

Biochemical journal, 2015-03, Vol.466 (2), p.311-322

2015

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Directional Phosphorylation and Nuclear Transport of the Splicing Factor SRSF1 Is Regulated by an RNA Recognition Motif

Journal of molecular biology, 2016-06, Vol.428 (11), p.2430-2445

2016

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Nuclear protein kinase CLK1 uses a non-traditional docking mechanism to select physiological substrates

Biochemical journal, 2015-12, Vol.472 (3), p.329-338

2015

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N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation

Biochemical journal, 2014-08, Vol.462 (1), p.143-152

2014

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Ligand-induced global transitions in the catalytic domain of protein kinase A

Proceedings of the National Academy of Sciences - PNAS, 2009-03, Vol.106 (9), p.3023-3028

2009

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Designing bacterial signaling interactions with coevolutionary landscapes

PloS one, 2018-08, Vol.13 (8), p.e0201734-e0201734

2018

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Phosphorylation Reaction in cAPK Protein Kinase-Free Energy Quantum Mechanical/Molecular Mechanics Simulations

The journal of physical chemistry. B, 2007-11, Vol.111 (47), p.13455-13464

2007

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Interplay between SRPK and Clk/Sty Kinases in Phosphorylation of the Splicing Factor ASF/SF2 Is Regulated by a Docking Motif in ASF/SF2

Molecular cell, 2005-10, Vol.20 (1), p.77-89

2005

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A Sliding Docking Interaction Is Essential for Sequential and Processive Phosphorylation of an SR Protein by SRPK1

Molecular cell, 2008-03, Vol.29 (5), p.563-576

2008

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Mechanism of Dephosphorylation of the SR Protein ASF/SF2 by Protein Phosphatase 1

Journal of molecular biology, 2010-10, Vol.403 (3), p.386-404

2010

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Theoretical Insights Reveal Novel Motions in Csk's SH3 Domain That Control Kinase Activation

PloS one, 2015-06, Vol.10 (6), p.e0127724-e0127724

2015

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SRPK1 regulates RNA binding in a pre‐spliceosomal complex using a catalytic bypass mechanism

The FEBS journal, 2022-12, Vol.289 (23), p.7428-7445

2022

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A conserved sequence motif bridges two protein kinases for enhanced phosphorylation and nuclear function of a splicing factor

The FEBS journal, 2021-01, Vol.288 (2), p.566-581

2021

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Correction: Theoretical Insights Reveal Novel Motions in Csk's SH3 Domain That Control Kinase Activation

PloS one, 2015-07, Vol.10 (7), p.e0133801-e0133801

2015

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The Akt-SRPK-SR Axis Constitutes a Major Pathway in Transducing EGF Signaling to Regulate Alternative Splicing in the Nucleus

Phosphorylation mechanism and structure of serine-arginine protein kinases

Matrix Rigidity Controls Epithelial-Mesenchymal Plasticity and Tumor Metastasis via a Mechanoresponsive EPHA2/LYN Complex

Release of SR Proteins from CLK1 by SRPK1: A Symbiotic Kinase System for Phosphorylation Control of Pre-mRNA Splicing

Kinetic and Catalytic Mechanisms of Protein Kinases

Initiation of Parental Genome Reprogramming in Fertilized Oocyte by Splicing Kinase SRPK1-Catalyzed Protamine Phosphorylation

Molecular interactions connecting the function of the serine-arginine–rich protein SRSF1 to protein phosphatase 1

Redirecting SR Protein Nuclear Trafficking through an Allosteric Platform

Partitioning RS Domain Phosphorylation in an SR Protein through the CLK and SRPK Protein Kinases

Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases

Structural Basis for the Regulation of Protein Kinase A by Activation Loop Phosphorylation

Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function

Directional Phosphorylation and Nuclear Transport of the Splicing Factor SRSF1 Is Regulated by an RNA Recognition Motif

Nuclear protein kinase CLK1 uses a non-traditional docking mechanism to select physiological substrates

N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation

Ligand-induced global transitions in the catalytic domain of protein kinase A

Designing bacterial signaling interactions with coevolutionary landscapes

Phosphorylation Reaction in cAPK Protein Kinase-Free Energy Quantum Mechanical/Molecular Mechanics Simulations

Interplay between SRPK and Clk/Sty Kinases in Phosphorylation of the Splicing Factor ASF/SF2 Is Regulated by a Docking Motif in ASF/SF2

A Sliding Docking Interaction Is Essential for Sequential and Processive Phosphorylation of an SR Protein by SRPK1

Mechanism of Dephosphorylation of the SR Protein ASF/SF2 by Protein Phosphatase 1

Theoretical Insights Reveal Novel Motions in Csk's SH3 Domain That Control Kinase Activation

SRPK1 regulates RNA binding in a pre‐spliceosomal complex using a catalytic bypass mechanism

A conserved sequence motif bridges two protein kinases for enhanced phosphorylation and nuclear function of a splicing factor

Correction: Theoretical Insights Reveal Novel Motions in Csk's SH3 Domain That Control Kinase Activation

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