Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia - Wikidata - awgldk - TriplyDB

Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia

Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia

http://www.wikidata.org/entity/Q27640723

about

Q27643286 Q28315773

sameAs

The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation Flexible ligand docking to multiple receptor conformations: a practical alternative Developing irreversible inhibitors of the protein kinase cysteinome The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2)Discovery of a Potential Allosteric Ligand Binding Site in CDK2 A Novel Approach to the Discovery of Small-Molecule Ligands of CDK2 X-ray structure of p38α bound to TAK-715: comparison with three classic inhibitors Structural Mechanisms Determining Inhibition of the Collagen Receptor DDR1 by Selective and Multi-Targeted Type II Kinase Inhibitors Mechanisms of drug resistance in kinases.Steered molecular dynamics simulations reveal the likelier dissociation pathway of imatinib from its targeting kinases c-Kit and Abl Insight on Mutation-Induced Resistance from Molecular Dynamics Simulations of the Native and Mutated CSF-1R and KIT Harnessing Fluorine-Sulfur Contacts and Multipolar Interactions for the Design of p53 Mutant Y220C Rescue Drugs Comparing pharmacophore models derived from crystal structures and from molecular dynamics simulations Computational insights for the discovery of non-ATP competitive inhibitors of MAP kinases From protein sequences to 3D-structures and beyond: the example of the UniProt knowledgebase.Oncogenic JAK1 and JAK2-activating mutations resistant to ATP-competitive inhibitors.Kinase domain point mutations in Philadelphia chromosome-positive acute lymphoblastic leukemia emerge after therapy with BCR-ABL kinase inhibitors.Computational study of Gleevec and G6G reveals molecular determinants of kinase inhibitor selectivity.Binding free energy calculation with QM/MM hybrid methods for Abl-Kinase inhibitor Rational, biologically based treatment of EGFR-mutant non-small-cell lung cancer.Protein kinase-inhibitor database: structural variability of and inhibitor interactions with the protein kinase P-loop.Identification of binding sites and favorable ligand binding moieties by virtual screening and self-organizing map analysis.Three-way complex variant translocation involving short arm chromosome (1;9;22)(p36;q34;q11) in a chronic myeloid leukemia patient.Targeting Filarial Abl-like Kinases: Orally Available, Food and Drug Administration-Approved Tyrosine Kinase Inhibitors Are Microfilaricidal and Macrofilaricidal.Bioinformatics and variability in drug response: a protein structural perspective.Ensembler: Enabling High-Throughput Molecular Simulations at the Superfamily Scale Classifying kinase conformations using a machine learning approach.The ins and outs of bcr-abl inhibition.An Allosteric Cross-Talk Between the Activation Loop and the ATP Binding Site Regulates the Activation of Src Kinase.Constructing and Validating High-Performance MIEC-SVM Models in Virtual Screening for Kinases: A Better Way for Actives Discovery.Treatment for chronic myelogenous leukemia: the long road to imatinib A Novel Four-Way Complex Variant Translocation Involving Chromosome 46,XY,t(4;9;19;22)(q25:q34;p13.3;q11.2) in a Chronic Myeloid Leukemia Patient Antileukemic effects of the novel, mutant FLT3 inhibitor NVP-AST487: effects on PKC412-sensitive and -resistant FLT3-expressing cells Strategies for overcoming imatinib resistance in chronic myeloid leukemia.Type-II kinase inhibitor docking, screening, and profiling using modified structures of active kinase states Mutations of FLT3/ITD confer resistance to multiple tyrosine kinase inhibitors.Structure-Based Design of Tetrahydroisoquinoline-7-carboxamides as Selective Discoidin Domain Receptor 1 (DDR1) Inhibitors.Biochemical mechanisms of resistance to small-molecule protein kinase inhibitors.A medicinal chemist's guide to molecular interactions Small-molecule inhibitors binding to protein kinase. Part II: the novel pharmacophore approach of type II and type III inhibition.

P2860

Q24323313-237E8C93-B1E6-48DC-9040-7A9BBDE5404B Q24650066-EB95CCF2-8C9B-45E9-B776-4B9075ABD588 Q27027983-679312F8-6643-4FCE-AFCF-478A152FC992 Q27653890-3919AE74-304D-4407-8DD2-53BB8CBAF843 Q27666837-A5E1F3A5-6921-46A3-86C2-99382009DCE2 Q27671549-0478BE9A-0898-428F-BE47-4AFB0BD0FE36 Q27681911-81114C46-864B-4808-BA45-8B92279C6875 Q27683558-6B966D0D-BD53-4C9E-AEEC-55B52346F1F9 Q27692567-DCB46DEE-28D4-4BA2-B777-FCF11802B129 Q28472368-37286EF5-14AA-4CF0-96CC-01B7C5B28673 Q28553167-10BFE7A3-A29D-4D38-96A1-95CA332FCBD3 Q28829378-0C692A06-49BF-4F0A-86A0-0E8224CC6FFE Q30386769-7031E110-6F92-42B3-BD10-A660D7A65AAC Q33593739-DC0C0C0A-E1B5-4A60-A8B1-8F95F2554974 Q33716007-7CA68943-F46C-4235-8102-746CF7067BB3 Q33843072-0A9FEACE-EBC8-409A-B206-22147D726AE2 Q34378360-C4F73A87-F61F-4B82-BB5E-8BC063CBE77B Q34408156-544BDFAB-6E84-44B0-8C4D-7A66D2AC347F Q34427031-1026FE6D-EF49-4261-BAE1-9BCC22DF9DD4 Q34773458-8150422D-6851-4A8F-A2E5-E55A2779AD20 Q35606325-CAC0C3BD-C61E-4735-883E-2E9773C9B40D Q35608172-F71771F0-64CC-4F4E-A1D3-FF4390FAF216 Q35944604-568BAE97-810B-40E7-8EAC-951DD9A7928B Q35965183-35C6D35E-0E5C-4A66-94E1-2E353D1CC16B Q36009999-035E4936-85E6-4BC6-9E14-6410574F61ED Q36060332-92B6C46E-921E-4AAE-889B-454DF3075349 Q36268137-A2841AAF-81B1-4C06-9AB8-1CA26FDA379C Q36443401-90D8FEE1-27D4-46DA-96A7-57974173B73F Q36785393-0CF4C09F-E522-4391-831B-CA03E2DC01C7 Q36824248-866E2051-D493-47A5-BD7F-4D8ECF2F2260 Q36900105-BE1E0DAC-9E4D-49BD-AB42-CFECB03E25E0 Q36947496-A407DF4A-BC41-47D5-98A4-741EEF99A0E6 Q37003553-CD7EFE7B-45BB-4C6B-A0C2-AE68DBFF1544 Q37027402-020E2D8A-9EDD-4E8B-9B8E-56B5B72D37E8 Q37160025-B86342F1-55E8-498E-83B7-6FADDD471C7F Q37294768-2F348770-88B8-4E43-B861-ACF0EC87AD98 Q37317054-1365F868-8D0C-4B3F-8040-7CE9962D85A2 Q37665845-2D57511D-6017-4368-9FF8-1E2EC84F678A Q37719514-B542C7F5-63A5-41A4-ABAD-430FE820C324 Q38090664-B1B61CD0-8FD5-4B3A-8A72-5F5B0984E5B5

P2860

Structural biology contributions to the discovery of drugs to treat chronic myelogenous leukaemia

http://www.wikidata.org/entity/Q27640723

description

2006 nî lūn-bûn

@nan

2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

Structural biology contributio ...... chronic myelogenous leukaemia

@ast

Structural biology contributio ...... chronic myelogenous leukaemia

@en

Structural biology contributio ...... chronic myelogenous leukaemia

@nl

type

label

Structural biology contributio ...... chronic myelogenous leukaemia

@ast

Structural biology contributio ...... chronic myelogenous leukaemia

@en

Structural biology contributio ...... chronic myelogenous leukaemia

@nl

prefLabel

Structural biology contributio ...... chronic myelogenous leukaemia

@ast

Structural biology contributio ...... chronic myelogenous leukaemia

@en

Structural biology contributio ...... chronic myelogenous leukaemia

@nl

P1433

Q27640723-73C6B307-165B-45A0-B4ED-77E1F15F1335

P1476

Q27640723-73A6EFBD-207C-484F-BD7A-33C3FAAD41BA

P2093

Q27640723-11A690D4-B04D-4CB5-9573-6BCEFA4936E2

Q27640723-13143CCA-E3D9-4F70-B78F-C3FD3F1F771F

Q27640723-2BFD0F83-543B-4A98-B46B-CF9EC5876EA7

Q27640723-34AF7208-6DE6-4F26-BE45-4B44B961CF82

Q27640723-4A40DE3C-03D5-4188-81BB-6D96965098C3

Q27640723-692F6819-99ED-4EC9-B8B3-C19D6D6EE7B3

Q27640723-6FB6EE85-8082-42A9-B9A0-BA3647961970

Q27640723-92B898A2-4482-424B-B567-91AE2493A3DE

Q27640723-9FE33735-5BBD-4805-9A68-5181C156AEE0

Q27640723-E26A0B9B-F30B-4043-B431-C0890A1CAA42

P2860

Q27640723-067C248B-E73A-4D05-A126-38A4935404B2

Q27640723-078F552D-C575-4749-AA8D-75EE827D2DDB

Q27640723-086F2FC5-6EAB-4416-9D45-4E78988FA5BB

Q27640723-0C439399-6ACE-4DF2-BC06-8345013121CB

Q27640723-1B88D686-786B-4EB2-87D5-E49FE56FC4CB

Q27640723-1C58FE16-5B9C-4A8F-9E17-F7521134F13D

Q27640723-23B24671-51E9-4497-ABCB-567B264324B8

Q27640723-2A602D5A-8780-4B2F-B8BA-5675F1267514

Q27640723-2E876D02-D890-4241-B301-4B89370C193A

Q27640723-311A49C2-FAFE-428E-B36F-200999BE2BAB

P304

Q27640723-C3416CC5-E7DD-489C-89EC-AE7888C8AB19

P31

Q27640723-AACD81D1-EE2D-4B82-9233-8CE118B2E9A7

P3181

Q27640723-E224004A-FD85-4C7F-9760-9EC94D09A365

P356

Q27640723-CE5C124C-96DD-4714-90E3-09934FB25399

P433

Q27640723-2D4628EC-A8CC-4BA0-834C-7B063F8F567E

Q27640723-4908741D-0649-4BCB-B015-93FA721DA609

P478

Q27640723-3D00EC6A-011B-43E9-B9C8-51A34BB7F6F4

P577

Q27640723-56821687-BBBE-40AB-96D8-30450798A431

Q27640723-66510781-3603-45A2-987F-0A80DE596CC4

P5875

Q27640723-9EC1B3BD-D079-4550-9174-DFB1DA526BAC

P698

Q27640723-F775E266-4B7A-4191-AB8A-481FEE405786

P921

Q27640723-6903F24C-CBA1-4B70-AD32-55736B2260D3

Q27640723-C417BA55-7788-47F5-AEED-8ABBCFEFB6AB

P932

Q27640723-11E5B5A7-8005-4C94-A0DD-BF1D15DE4D4A

P3181

P356

S0907444906047287

P1433

Acta Crystallographica Section D: Biological Crystallography

P1476

Structural biology contributio ...... chronic myelogenous leukaemia

@en

P2093

Andreas Floersheimer

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

Doriano Fabbro

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

Gabriele Fendrich

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

Gabriele Rummel

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

Janis Liebetanz

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

Mario Centeleghe

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

Pascal Furet

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

Paul Rheinberger

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

Paul W Manley

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

Paul W. Manley

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

P2860

AMN107 (nilotinib): a novel and selective inhibitor of BCR-ABL

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystal structures of c-Src reveal features of its autoinhibitory mechanism

Structural mechanism for STI-571 inhibition of abelson tyrosine kinase

Crystal structure of bisphosphorylated IGF-1 receptor kinase: insight into domain movements upon kinase activation

Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site

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

Structural basis for the autoinhibition of c-Abl tyrosine kinase

The structural basis for autoinhibition of FLT3 by the juxtamembrane domain

Crystal structure of the tyrosine kinase domain of the human insulin receptor

P304

80-93

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

P31

scholarly article

P3181

546902

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

P356

10.1107/S0907444906047287

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

P433

1

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

Pt 1

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

P478

63

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

P577

2006-12-13T00:00:00Z

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

2007-01-01T00:00:00Z

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

P5875

6634473

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

P698

17164530

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

P921

structural biology

P932

2483489

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