BindingDB Entry 50038281: Discovery of kinase inhibitors by high-throughput docking and scoring based on a transferable linear interaction energy model.

Name: BindingDB Entry 50038281: Discovery of kinase inhibitors by high-throughput docking and scoring based on a transferable linear interaction energy model.
Creator: BindingDB
Keywords: Cyclin-Dependent Kinase 1 (CDK1), Cyclin-dependent kinase 1, Cyclin-dependent kinase 2, Ephrin type-B receptor 4 (EphB4), Epidermal growth factor receptor, Mitogen-activated protein kinase 14, and SRC, University of Zurich, Affinity

Research datakeyboard_double_arrow_right Dataset 01 Jan 2012 English Publisher:BindingDB

Authors: BindingDB;

doi: 10.7270/q29z95rd

BindingDB Entry 50038281: Discovery of kinase inhibitors by high-throughput docking and scoring based on a transferable linear interaction energy model.

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Abstract

Small molecule binding data for protein Cyclin-Dependent Kinase 1 (CDK1), Cyclin-dependent kinase 1, Cyclin-dependent kinase 2, Ephrin type-B receptor 4 (EphB4), Epidermal growth factor receptor, Mitogen-activated protein kinase 14, and SRC, Uniprot P00533, P06239, P06493, P14635, P24941, P54760, Q16539, and Q541P7

Keywords

Cyclin-Dependent Kinase 1 (CDK1), Cyclin-dependent kinase 1, Cyclin-dependent kinase 2, Ephrin type-B receptor 4 (EphB4), Epidermal growth factor receptor, Mitogen-activated protein kinase 14, and SRC, University of Zurich, Affinity

7 Research products, page 1 of 1

BindingDB Entry 50032427: Inhibitors of the tyrosine kinase EphB4. Part 3: identification of non-benzodioxole-based kinase inhibitors.
2011IsAmongTopNSimilarDocuments
BindingDB Entry 2846: Inhibitors of the tyrosine kinase EphB4. Part 1: Structure-based design and optimization of a series of 2,4-bis-anilinopyrimidines.
2008IsAmongTopNSimilarDocuments
BindingDB Entry 50047215: Three stories on Eph kinase inhibitors: From in silico discovery to in vivo validation.
2017IsAmongTopNSimilarDocuments
BindingDB Entry 50040352: Discovery of a novel chemotype of tyrosine kinase inhibitors by fragment-based docking and molecular dynamics.
2013IsAmongTopNSimilarDocuments
Discovery of Kinase Inhibitors by High-Throughput Docking and Scoring Based on a Transferable Linear Interaction Energy Model
2008IsDerivedFrom
BindingDB Entry 50045057: Structural Analysis of the Binding of Type I, I1/2, and II Inhibitors to Eph Tyrosine Kinases.
2016IsAmongTopNSimilarDocuments
BindingDB Entry 50045809: Current kinase inhibitors cover a tiny fraction of fragment space.
2016IsAmongTopNSimilarDocuments

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BindingDB Entry 50038281: Discovery of kinase inhibitors by high-throughput docking and scoring based on a transferable linear interaction energy model.

BindingDB Entry 50038281: Discovery of kinase inhibitors by high-throughput docking and scoring based on a transferable linear interaction energy model.

7 Research products, page 1 of 1

BindingDB Entry 50032427: Inhibitors of the tyrosine kinase EphB4. Part 3: identification of non-benzodioxole-based kinase inhibitors.

BindingDB Entry 2846: Inhibitors of the tyrosine kinase EphB4. Part 1: Structure-based design and optimization of a series of 2,4-bis-anilinopyrimidines.

BindingDB Entry 50047215: Three stories on Eph kinase inhibitors: From in silico discovery to in vivo validation.

BindingDB Entry 50040352: Discovery of a novel chemotype of tyrosine kinase inhibitors by fragment-based docking and molecular dynamics.

Discovery of Kinase Inhibitors by High-Throughput Docking and Scoring Based on a Transferable Linear Interaction Energy Model

BindingDB Entry 50045057: Structural Analysis of the Binding of Type I, I1/2, and II Inhibitors to Eph Tyrosine Kinases.

BindingDB Entry 50045809: Current kinase inhibitors cover a tiny fraction of fragment space.