Comparative analysis of two clinically active BCR-ABL kinase inhibitors reveals the role of conformation-specific binding in resistance.
about
The proximal signaling network of the BCR-ABL1 oncogene shows a modular organizationAP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistanceSequential ABL kinase inhibitor therapy selects for compound drug-resistant BCR-ABL mutations with altered oncogenic potencyThe growing arsenal of ATP-competitive and allosteric inhibitors of BCR-ABLEqually Potent Inhibition of c-Src and Abl by Compounds that Recognize Inactive Kinase ConformationsMechanisms of drug resistance in kinases.Characteristics and outcome of chronic myeloid leukemia patients with F317L BCR-ABL kinase domain mutation after therapy with tyrosine kinase inhibitors.Overcoming mutation-based resistance to antiandrogens with rational drug designA synergistic small-molecule combination directly eradicates diverse prion strain structuresComputational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.Emerging drugs for chronic myeloid leukemia.Early prediction of success or failure of treatment with second-generation tyrosine kinase inhibitors in patients with chronic myeloid leukemiaA TCR-mimic antibody to WT1 bypasses tyrosine kinase inhibitor resistance in human BCR-ABL+ leukemiasGlobal phosphoproteomics reveals crosstalk between Bcr-Abl and negative feedback mechanisms controlling Src signaling.Predictive factors for outcome and response in patients treated with second-generation tyrosine kinase inhibitors for chronic myeloid leukemia in chronic phase after imatinib failure.Drug resistance in cancer: principles of emergence and prevention.Inhibition of drug-resistant mutants of ABL, KIT, and EGF receptor kinasesAssociation between imatinib-resistant BCR-ABL mutation-negative leukemia and persistent activation of LYN kinase.Long-term outcome of patients with chronic myeloid leukemia treated with second-generation tyrosine kinase inhibitors after imatinib failure is predicted by the in vitro sensitivity of BCR-ABL kinase domain mutations.Dasatinib inhibits the growth of molecularly heterogeneous myeloid leukemias.Kinase domain point mutations in Philadelphia chromosome-positive acute lymphoblastic leukemia emerge after therapy with BCR-ABL kinase inhibitors.Targeted inhibition of kinases in cancer therapyActivity of dual SRC-ABL inhibitors highlights the role of BCR/ABL kinase dynamics in drug resistance.Philadelphia-positive acute lymphoblastic leukemia patients already harbor BCR-ABL kinase domain mutations at low levels at the time of diagnosisPhosphorylation of the ATP-binding loop directs oncogenicity of drug-resistant BCR-ABL mutantsReal-time analysis of imatinib- and dasatinib-induced effects on chronic myelogenous leukemia cell interaction with fibronectin.Oncogenes come of age.Beneficial effects of combining nilotinib and imatinib in preclinical models of BCR-ABL+ leukemias.Identification of an orally available compound with potent and broad FLT3 inhibition activityMEK1/2 inhibitors sensitize Bcr/Abl+ human leukemia cells to the dual Abl/Src inhibitor BMS-354/825Acquired resistance to drugs targeting receptor tyrosine kinasesAdaphostin-induced oxidative stress overcomes BCR/ABL mutation-dependent and -independent imatinib resistance.Characterizing and Overriding the Structural Mechanism of the Quizartinib-Resistant FLT3 "Gatekeeper" F691L Mutation with PLX3397Dual tyrosine kinase inhibitors in chronic myeloid leukemia.Converting cancer therapies into cures: lessons from infectious diseasesWhy do chronic myelogenous leukemia stem cells survive allogeneic stem cell transplantation or imatinib: does it really matter?Aurora A and B kinases as targets for cancer: will they be selective for tumors?BECLIN 1-VPS34 COMPLEX ARCHITECTURE: UNDERSTANDING THE NUTS AND BOLTS OF THERAPEUTIC TARGETS.Anticipating clinical resistance to target-directed agents : the BCR-ABL paradigm.SGX393 inhibits the CML mutant Bcr-AblT315I and preempts in vitro resistance when combined with nilotinib or dasatinib.
P2860
2e1687ca70f766141811a3442553f0a858b0f12a2f56fff3ddd49e3a3a0f847fb6295af99b4f938741e0a0bf28a18554cf3ebd6ce69e1beb65f75fc860fede498674508cff14727eefdcb4d3418cbf58797fcc6b3709f9271affdf6cae6c7fa8adb5b616a3be940217400f7a5cce4ac281fbdffe6fe8e70aa9b840bf86f97cb595ff2f39c86bdb942a3249d6aef33193134818a4f942423350eef27f1ee172b0c788603e8d52d0389761853ff8fbd3a7482010c5ea959b98585f6dcb42b92e66a01bce63235f5de3f6fe4f01dc34a0eb2d85e573dbbed848f455a5d1
P248
Q24294830-83BCE57A-B954-4733-99E9-ED5516C77D93Q24648017-B4585F13-13C0-4CC9-90CC-BD324827891DQ24681743-5E6F1621-D0D3-4FF5-A922-75EC92AB12CCQ26866312-7E1D9092-09B0-4EC6-B459-5694BCBB0D2EQ27654059-DFF26607-0E2D-44B8-8E91-15988F265E7BQ27692567-C9196059-ACCB-4642-BA66-2417EAFFCAD8Q27851450-B5598F1C-BFF8-41FF-B6AF-8D856EB092A5Q28044590-722C8048-1918-4082-9B0A-5955993139E9Q30885765-4E587D12-EC4C-4500-B7F6-E1E1B621BFD7Q31036423-5269B04C-B885-4E87-9470-48D3AD2FA835Q33536762-A6BFFD24-4301-4C71-9BCA-7EF9F9AFABF4Q33632220-A09EFAA2-FFEC-43E7-AB67-5B7F594671F1Q33714727-0585AD70-00E1-42B5-9883-0DF97251CF24Q33753325-AAAB10FA-94E6-4144-AE5A-FC19227409C5Q33843731-42FBE481-FA31-452D-9270-5E73B3173BC2Q33892278-BE07AC92-7EF5-4B2C-9DD3-72CA6CF1A36BQ33906140-9FF5CF13-401C-4F77-951E-97ECCBBD18A4Q33988398-F14490DE-20F8-4242-953D-A845DDA38C63Q34293384-902FC9E9-75F4-41AB-8701-071DCD462B4CQ34335004-9CEBF4E7-0742-40CF-9AE6-991F55FFB893Q34378360-C99E65D4-D9C4-46FA-9240-976B25E8BC02Q34683348-45E4B4F5-8DC4-42B9-9B0F-6F6DA0D40B99Q34695008-CFA17452-6021-4C52-AFB3-8CF7829F5B3FQ34750545-03A38DAE-68CE-4F35-89E0-7E9CFBB58D09Q35221149-92228514-5647-4E92-80E7-7B8CA1911810Q35242120-96DF319D-A337-4822-BD1E-A15D330BFC6DQ35623817-6393C2CD-B1BD-4D19-A23F-9F8B35E00FF0Q35642790-411C0BA2-E193-4C52-92E3-40A07143EDDCQ35789739-57689956-9DAE-43BB-A1BC-6232704E59DBQ35804449-7B8B5DA1-4348-4263-8309-FD15FEDC2F1BQ35823437-61E46C78-06F0-4EB3-B774-0BD4285C7273Q35849543-C9375704-C7D2-4909-895B-DE83768B4EAEQ35909096-72009FB8-420E-4BF9-878C-7128097F03E0Q36265601-0B7CC5AE-9795-452E-B4BD-8C9B26E90662Q36301709-7A48DB47-A3A2-46EC-87C6-2D555EB7EC8BQ36328410-F23A1DC8-5E01-4962-8FEC-7788F11E4979Q36352091-4FAA1CBD-37A8-4ED9-A68F-06F63C3329CEQ36379709-6661B63F-5638-4A33-B3B5-1F30AC558CD4Q36466443-FB51361A-F115-4A6E-9608-7968D1E85258Q36535476-8AE818F0-90D1-4ADD-8C17-4BB966B7051E
P2860
Comparative analysis of two clinically active BCR-ABL kinase inhibitors reveals the role of conformation-specific binding in resistance.
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Comparative analysis of two cl ...... pecific binding in resistance.
@ast
Comparative analysis of two cl ...... pecific binding in resistance.
@en
type
label
Comparative analysis of two cl ...... pecific binding in resistance.
@ast
Comparative analysis of two cl ...... pecific binding in resistance.
@en
prefLabel
Comparative analysis of two cl ...... pecific binding in resistance.
@ast
Comparative analysis of two cl ...... pecific binding in resistance.
@en
P2093
P2860
P356
P1476
Comparative analysis of two cl ...... pecific binding in resistance.
@en
P2093
Brian J Skaggs
Charles L Sawyers
Francis Y Lee
Michael R Burgess
Neil P Shah
P2860
P304
P356
10.1073/PNAS.0409770102
P407
P577
2005-02-10T00:00:00Z