Predicting kinase-substrate interactions in the era of proteomics. Focus on “Identifying protein kinase target preferences using mass spectrometry”

Development of photo-crosslinking reagents for protein kinase-substrate interactions

FEBS Letters ◽

10.1016/s0014-5793(02)02778-3 ◽

2002 ◽

Vol 520 (1-3) ◽

pp. 156-160 ◽

Cited By ~ 28

Author(s):

Keykavous Parang ◽

Jeffrey A. Kohn ◽

S.Adrian Saldanha ◽

Philip A. Cole

Keyword(s):

Protein Kinase ◽

Substrate Interactions ◽

Use of synthetic peptide libraries and phosphopeptide-selective mass spectrometry to probe protein kinase substrate specificity.

10.1016/s0021-9258(17)37302-7 ◽

1994 ◽

Vol 269 (10) ◽

pp. 7423-7428

Author(s):

J.H. Till ◽

R.S. Annan ◽

S.A. Carr ◽

W.T. Miller

Keyword(s):

Mass Spectrometry ◽

Protein Kinase ◽

Substrate Specificity ◽

Synthetic Peptide ◽

Peptide Libraries ◽

Revisiting protein kinase–substrate interactions: Toward therapeutic development

Science Signaling ◽

10.1126/scisignal.aad4016 ◽

2016 ◽

Vol 9 (420) ◽

pp. re3-re3 ◽

Cited By ~ 33

Author(s):

Paulo Sérgio L. de Oliveira ◽

Felipe Augusto N. Ferraz ◽

Darlene A. Pena ◽

Dimitrius T. Pramio ◽

Felipe A. Morais ◽

...

Keyword(s):

Protein Kinase ◽

Substrate Interactions ◽

Kinase Substrate ◽

Therapeutic Development

rap1B, a cAMP-dependent protein kinase substrate, associates with the platelet cytoskeleton.

10.1016/s0021-9258(17)45385-3 ◽

1990 ◽

Vol 265 (32) ◽

pp. 19405-19408 ◽

Cited By ~ 1

Author(s):

T H Fischer ◽

M N Gatling ◽

J C Lacal ◽

G C White

Keyword(s):

Protein Kinase ◽

Kinase Substrate ◽

Camp Dependent Protein Kinase ◽

Dependent Protein

Purification and characterization of 240-kDa cGMP-dependent protein kinase substrate of vascular smooth muscle. Close resemblance to inositol 1,4,5-trisphosphate receptor

10.1016/s0021-9258(19)78173-3 ◽

1994 ◽

Vol 269 (15) ◽

pp. 11640-11647 ◽

Cited By ~ 1

Author(s):

T. Koga ◽

Y. Yoshida ◽

J.Q. Cai ◽

M.O. Islam ◽

S. Imai

Keyword(s):

Smooth Muscle ◽

Protein Kinase ◽

Purification And Characterization ◽

Kinase Substrate ◽

Cgmp Dependent Protein Kinase ◽

Inositol 1,4,5 Trisphosphate ◽

Dependent Protein ◽

Trisphosphate Receptor

Identification of a Ras-related protein in murine erythroleukemia cells that is a cAMP-dependent protein kinase substrate and is phosphorylated during chemically induced differentiation.

10.1016/s0021-9258(19)80661-0 ◽

2000 ◽

Vol 275 (19) ◽

pp. 14777

Author(s):

Jurgen S. Scheele ◽

Renate B. Pilz ◽

Lawrence A. Quilliam ◽

Gerry R. Boss

Keyword(s):

Protein Kinase ◽

Related Protein ◽

Induced Differentiation ◽

Kinase Substrate ◽

Erythroleukemia Cells ◽

Chemically Induced ◽

Dependent Protein ◽

Murine Erythroleukemia ◽

Murine Erythroleukemia Cells

2020 IEEE 20th International Conference on Bioinformatics and Bioengineering (BIBE) ◽

Predicting Kinase-Substrate Interactions in Medulloblastoma Subtypes

10.1109/bibe50027.2020.00128 ◽

2020 ◽

Author(s):

Aparna Krishnan ◽

Kristin Leskoske ◽

Krystine Garcia-Mansfield ◽

Ritin Sharma ◽

Jessica Rusert ◽

...

Keyword(s):

Substrate Interactions ◽

Protein kinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein.

10.1016/s0021-9258(17)37116-8 ◽

1994 ◽

Vol 269 (12) ◽

pp. 9361-9367

Author(s):

G.M. Verghese ◽

J.D. Johnson ◽

C. Vasulka ◽

D.M. Haupt ◽

D.J. Stumpo ◽

...

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Related Protein ◽

Kinase Substrate ◽

Calmodulin Binding ◽

Kinase C

Taming platelets with cyclic nucleotides11Abbreviations: ABP, actin binding protein; AC, adenylyl cyclase; cAMP, cyclic AMP; cAMP-PK, cAMP-dependent protein kinase; cGMP, cyclic GMP; cGMP-PK, cGMP-dependent protein kinase; DAG, 1,2-diacylglycerol; EDRF, endothelium-derived relaxing factor; GC, guanylyl cyclase; GP, glycoprotein; Hsp27, heat shock protein 27; IP3, inositol 1,4,5- trisphosphate; IRAG, IP3 receptor-associated cGMP-PK substrate; MAPK, mitogen-activated protein kinase; MAPKAPK-2, MAPK-activated protein kinase-2; MARCKS, myristoylated alanine-rich C kinase substrate; MLC, myosin light chain; MLCK, myosin light chain kinase; PDE, phosphodiesterase; PG-E1, prostaglandin E1; PG-I2, prostacyclin; PIP2, phosphatidylinositol 4,5-bisphosphate; PKC, protein kinase C; PLC, phospholipase C; TxA2, thromboxane A2, and VASP, vasodilator-stimulated phosphoprotein.

Biochemical Pharmacology ◽

10.1016/s0006-2952(01)00760-2 ◽

2001 ◽

Vol 62 (9) ◽

pp. 1153-1161 ◽

Cited By ~ 230

Author(s):

Ulrike R. Schwarz ◽

Ulrich Walter ◽

Martin Eigenthaler

Keyword(s):

Protein Kinase ◽

Light Chain ◽

Myosin Light Chain ◽

Mitogen Activated Protein Kinase ◽

Actin Binding ◽

Ip3 Receptor ◽

Kinase Substrate ◽

Mitogen Activated Protein ◽

Dependent Protein

Thrombin and histamine rapidly stimulate the phosphorylation of the myristoylated alanine-rich C-kinase substrate in human umbilical vein endothelial cells: Evidence for distinct patterns of protein kinase activation

Journal of Cellular Physiology ◽

10.1002/jcp.1041520121 ◽

1992 ◽

Vol 152 (1) ◽

pp. 166-176 ◽

Cited By ~ 10

Author(s):

Brian C. Jacobson ◽

Jordan S. Pober ◽

John W. Fenton ◽

Bruce M. Ewenstein

Keyword(s):

Endothelial Cells ◽

Protein Kinase ◽

Umbilical Vein ◽

Kinase Activation ◽

Human Umbilical Vein ◽

Kinase Substrate ◽

Protein Kinase Activation ◽

Umbilical Vein Endothelial Cells