Explaining why Gleevec is a specific and potent inhibitor of Abl kinase. - Wikidata - awgldk - TriplyDB

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

http://www.wikidata.org/entity/Q36582978

about

c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease Neuroprotective and Therapeutic Strategies against Parkinson's Disease: Recent Perspectives Computational modeling of membrane proteins Structure of the Human Protein Kinase ZAK in Complex with Vemurafenib P-loop conformation governed crizotinib resistance in G2032R-mutated ROS1 tyrosine kinase: clues from free energy landscape Uncovering Molecular Bases Underlying Bone Morphogenetic Protein Receptor Inhibitor Selectivity Molecular Determinants Underlying Binding Specificities of the ABL Kinase Inhibitors: Combining Alanine Scanning of Binding Hot Spots with Network Analysis of Residue Interactions and Coevolution Towards a Molecular Understanding of the Link between Imatinib Resistance and Kinase Conformational Dynamics Predictions of Ligand Selectivity from Absolute Binding Free Energy Calculations Imatinib binding to human c-Src is coupled to inter-domain allostery and suggests a novel kinase inhibition strategy Beyond Membrane Protein Structure: Drug Discovery, Dynamics and Difficulties.Computational analysis of the binding specificity of Gleevec to Abl, c-Kit, Lck, and c-Src tyrosine kinases.Measurement of small molecule binding kinetics on a protein microarray by plasmonic-based electrochemical impedance imaging.Computational study of Gleevec and G6G reveals molecular determinants of kinase inhibitor selectivity.Energetic dissection of Gleevec's selectivity toward human tyrosine kinases.Computational study of the "DFG-flip" conformational transition in c-Abl and c-Src tyrosine kinases.Conformational analysis of the DFG-out kinase motif and biochemical profiling of structurally validated type II inhibitors.Kinase dynamics. Using ancient protein kinases to unravel a modern cancer drug's mechanism Activation pathway of Src kinase reveals intermediate states as targets for drug design Ensembler: Enabling High-Throughput Molecular Simulations at the Superfamily Scale Modeling molecular kinetics with tICA and the kernel trick Dasatinib inhibits TGFβ-induced myofibroblast differentiation through Src-SRF Pathway.Conformational Selection and Induced Fit Mechanisms in the Binding of an Anticancer Drug to the c-Src Kinase Calculating the sensitivity and robustness of binding free energy calculations to force field parameters.Canonical and new generation anticancer drugs also target energy metabolism.Remodeling of the fibroblast cytoskeletal architecture during the replication cycle of Ectromelia virus: A morphological in vitro study in a murine cell line.Advanced molecular dynamics simulation methods for kinase drug discovery.Molecular modeling study of the induced-fit effect on kinase inhibition: the case of fibroblast growth factor receptor 3 (FGFR3).Rate Constants and Mechanisms of Protein-Ligand Binding.Small-world networks of residue interactions in the Abl kinase complexes with cancer drugs: topology of allosteric communication pathways can determine drug resistance effects.Structural propensities of kinase family proteins from a Potts model of residue co-variation.Novel Pieces for the Emerging Picture of Sulfoximines in Drug Discovery: Synthesis and Evaluation of Sulfoximine Analogues of Marketed Drugs and Advanced Clinical Candidates.Conformation-selective inhibitors reveal differences in the activation and phosphate-binding loops of the tyrosine kinases Abl and Src.Dynamic Equilibrium of the Aurora A Kinase Activation Loop Revealed by Single-Molecule Spectroscopy.The Endocytic Fate of the Transferrin Receptor Is Regulated by c-Abl Kinase.Mechanistic insights into Pin1 peptidyl-prolyl cis-trans isomerization from umbrella sampling simulations.Can Relative Binding Free Energy Predict Selectivity of Reversible Covalent Inhibitors?Coevolutionary Landscape of Kinase Family Proteins: Sequence Probabilities and Functional Motifs.Proton-Coupled Conformational Allostery Modulates the Inhibitor Selectivity for β-Secretase.The binding mechanism of a novel nicotinamide isostere inhibiting with TNKSs: a molecular dynamic simulation and binding free energy calculation.

P2860

Q24318974-DDDD761F-D805-472F-9B0A-92B892924860 Q26747508-B1F1B35C-2CB5-48D7-BE95-A83551E93557 Q26995693-C6FA9A7E-F5DB-4403-8D69-75380FD80BF7 Q27704282-064D58C5-7BC6-4CF1-937E-53B78B3789E8 Q28540825-7468891D-CBCA-4185-A4C5-429203B2358C Q28546110-1FBCF823-D010-4ED8-9567-C8356B9F32CA Q28548366-45842924-865E-4E91-A906-58284AE9B6AB Q28551159-AB4ABEBB-4526-43F0-A073-D9BB0B9858A2 Q28818600-4454813A-EE54-4908-9830-472EE2174350 Q30008882-BAA3E9E1-9BB9-4DD2-B9DC-9E95039DA480 Q30392142-3A9E2176-DCC2-41CD-AD48-907DCAE1B5AC Q33631185-DEBCD200-D24D-439F-8E65-B5ED8BA790CA Q34300380-6AE83968-6C1B-4689-A569-03B51CF99616 Q34408156-056FAF53-3355-4C75-A2A7-39F6F8DE1A35 Q34703677-A97991C1-F16D-435C-8EF6-8B64EE86DABA Q35043382-D46D1FE0-7138-46A9-B56A-0E45E3E6767C Q35493874-E6C135D1-74E5-4594-BC20-A2521B6E75CD Q35509663-B6F4B97A-74E9-49AD-9044-5BCABF261163 Q35738216-B2375513-F05C-48B7-A8F3-04155C2D41DF Q36060332-7951DD7E-CB8B-4A56-AC8D-41C8A3DE7191 Q36175542-A09249E7-DB56-4ED2-8165-82951B9F2B1B Q36373463-9A20C719-BBC1-434F-A4BB-DD3BA51EF557 Q36806236-F71633DE-B18C-472F-80F7-AC832FB3FDA6 Q37149321-CCBD1DD3-6BCA-4BC4-839E-76D10C20114C Q38208982-F7699E12-DB33-4AED-A137-DDA889488C04 Q38771653-68F53C30-419D-4DBD-ABBD-7E9B3FD60026 Q38800768-52A87571-8D71-40AD-9041-636D84BC548E Q39025426-19E5E2D7-9429-4AEF-9BF8-2F4512C87595 Q39219062-A63790C7-7174-4187-9238-069BBBAF3C6E Q39277365-ED19ACB6-E745-489D-9EB1-3B3607CF0BD1 Q39724623-5923EFD7-4B6C-4073-976F-AB2923C76A52 Q41039819-60A00B25-3427-4971-83BE-19BE0AD725DA Q41850714-DE93B012-7148-4C70-89DB-4C1162BE985C Q42359642-22E19042-FE41-4E06-A9C4-AF8EBB4285E6 Q42380149-857140B8-BD33-4BB1-93D4-3FAE593CC1B7 Q45846360-61F4FAFF-B281-40B9-924F-48933BE995A6 Q45934140-66FF6C01-6D0D-4D69-9455-5482B2934BC4 Q47213672-68D6B5E2-46A3-4446-BD2F-3927967051F4 Q48053583-2F171F49-E329-4732-896F-072FB5F34415 Q50921784-D3BC83E4-E375-4DDE-AF48-48AE33C4E7B2

P2860

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

http://www.wikidata.org/entity/Q36582978

description

2013 nî lūn-bûn

@nan

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

@ast

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

@en

type

label

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

@ast

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

@en

prefLabel

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

@ast

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

@en

P1433

Q36582978-3B9C8F99-D52A-45F9-AFAD-EB6CAE6789C5

P1476

Q36582978-18C261B6-1599-4683-87C6-F3457F003627

P2093

Q36582978-50E38373-38FD-448B-B9CC-9A3F12CCFBF9

Q36582978-6498661D-B0A4-41F7-96BF-A94DA6C1F7EF

Q36582978-C0608CA7-1DE2-4050-9493-55EC163767CC

Q36582978-D37B6D9C-FECC-4299-9169-92493BC2443F

P2860

Q36582978-00441F47-65CD-4179-B741-F987E57393F8

Q36582978-04D9CC07-63A3-4AFF-9556-F8098ECD9050

Q36582978-064247DA-67EF-4790-AFE8-1AECEAC76DEC

Q36582978-0908397C-9933-461D-900C-F191AD8C97DE

Q36582978-0BCEE406-0F46-49D1-B8FD-9CE0FE5FCE00

Q36582978-0FE41017-AD6D-4F94-9D03-22A3DE5739D1

Q36582978-1180DE78-5BC4-43B7-ADE8-595D6D004022

Q36582978-19053284-333F-4596-B9FB-F55D29FA4E72

Q36582978-2073BFD4-14DD-44C2-B2F6-069080C9F694

Q36582978-21701D06-2710-4DB8-8D9B-FD41A5C37DF3

P304

Q36582978-379CB42E-5A55-44F5-890D-E6B4ADEB912F

P31

Q36582978-0983C97C-F3FC-400F-AB6B-7A15A56DE30B

P356

Q36582978-0C991F2A-FC4A-4A16-A010-1309F7CCBE0C

P407

Q36582978-94E84807-16BD-43DB-B7B0-61DD639D2B87

P433

Q36582978-1D3C3C0B-3748-4D3D-9090-BD167B817935

P478

Q36582978-0590CCB6-6DB0-4B88-85D2-5D1A2457DCFF

P577

Q36582978-B075A883-6FDB-4FAA-A309-3F51BBC9CD92

P5875

Q36582978-97CE39F8-9FB2-4068-8A55-ADF103DDFF37

P698

Q36582978-0E701454-A200-4700-9D72-7C2AE0276287

P932

Q36582978-6E66CF2F-3D83-4C1A-80FD-6E74402664BC

P356

PNAS.1214330110

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Explaining why Gleevec is a specific and potent inhibitor of Abl kinase.

@en

P2093

Benoît Roux

http://www.w3.org/2001/XMLSchema#string

Wei Jiang

http://www.w3.org/2001/XMLSchema#string

Yen-Lin Lin

http://www.w3.org/2001/XMLSchema#string

Yilin Meng

http://www.w3.org/2001/XMLSchema#string

P2860

QMEAN server for protein model quality estimation

A conserved protonation-dependent switch controls drug binding in the Abl kinase

Structural mechanism for STI-571 inhibition of abelson tyrosine kinase

Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)

c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty

Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: structure of lck/imatinib complex

Small Molecule Recognition of c-Src via the Imatinib-Binding Conformation

Equally Potent Inhibition of c-Src and Abl by Compounds that Recognize Inactive Kinase Conformations

Analysis of imatinib and sorafenib binding to p38alpha compared with c-Abl and b-Raf provides structural insights for understanding the selectivity of inhibitors targeting the DFG-out form of protein kinases

All-atom empirical potential for molecular modeling and dynamics studies of proteins

P304

1664-1669

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.1214330110

http://www.w3.org/2001/XMLSchema#string

P407

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

110

http://www.w3.org/2001/XMLSchema#string

P577

2013-01-14T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

234134580

http://www.w3.org/2001/XMLSchema#string

P698

23319661

http://www.w3.org/2001/XMLSchema#string

P932

3562763

http://www.w3.org/2001/XMLSchema#string