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Phosphorylation of the ATP-binding loop directs oncogenicity of drug-resistant BCR-ABL mutants

Phosphorylation of the ATP-binding loop directs oncogenicity of drug-resistant BCR-ABL mutants

http://www.wikidata.org/entity/Q35221149

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The proximal signaling network of the BCR-ABL1 oncogene shows a modular organization ABL tyrosine kinases: evolution of function, regulation, and specificity The chemical biology of protein phosphorylation Chemotherapeutic agents circumvent emergence of dasatinib-resistant BCR-ABL kinase mutations in a precise mouse model of Philadelphia chromosome-positive acute lymphoblastic leukemia Sequential ABL kinase inhibitor therapy selects for compound drug-resistant BCR-ABL mutations with altered oncogenic potency Acute myeloid leukaemia: a paradigm for the clonal evolution of cancer?Development of new mouse lung tumor models expressing EGFR T790M mutants associated with clinical resistance to kinase inhibitors Activation of tyrosine kinases by mutation of the gatekeeper threonine Mechanisms of drug resistance in kinases.Fitness conferred by BCR-ABL kinase domain mutations determines the risk of pre-existing resistance in chronic myeloid leukemia Dynamics of resistance development to imatinib under increasing selection pressure: a combination of mathematical models and in vitro data ABL fusion oncogene transformation and inhibitor sensitivity are mediated by the cellular regulator RIN1.BCR-ABL SH3-SH2 domain mutations in chronic myeloid leukemia patients on imatinib.Enhancement of ABL kinase catalytic efficiency by a direct binding regulator is independent of other regulatory mechanisms.Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer.Conformational disturbance in Abl kinase upon mutation and deregulation.Survey of phosphorylation near drug binding sites in the Protein Data Bank (PDB) and their effects.Global phosphoproteomics reveals crosstalk between Bcr-Abl and negative feedback mechanisms controlling Src signaling.Evolution of acquired resistance to anti-cancer therapy.Maximal entropy inference of oncogenicity from phosphorylation signaling.A robust error model for iTRAQ quantification reveals divergent signaling between oncogenic FLT3 mutants in acute myeloid leukemia.Oncogenic activity of epidermal growth factor receptor kinase mutant alleles is enhanced by the T790M drug resistance mutation Structural basis of protein kinase C isoform function Mechanisms of primary and secondary resistance to imatinib in chronic myeloid leukemia.Peptide reporters of kinase activity in whole cell lysates.Janus kinase inhibition by ruxolitinib extends dasatinib- and dexamethasone-induced remissions in a mouse model of Ph+ ALL.The C2 Domain and Altered ATP-Binding Loop Phosphorylation at Ser³⁵⁹ Mediate the Redox-Dependent Increase in Protein Kinase C-δ Activity Oncogene-specific activation of tyrosine kinase networks during prostate cancer progression.Design of substrate-based BCR-ABL kinase inhibitors using the cyclotide scaffold.Glucose deprivation activates a metabolic and signaling amplification loop leading to cell death Converting cancer therapies into cures: lessons from infectious diseases BCR-ABL1 compound mutations in tyrosine kinase inhibitor-resistant CML: frequency and clonal relationships Cancer as a moving target: understanding the composition and rebound growth kinetics of recurrent tumors.Therapeutic options for chronic myeloid leukemia: focus on imatinib (Glivec, Gleevectrade mark).Future options for imatinib mesilate-resistant tumors.Eph receptor signaling and ephrins Mutated BCR-ABL generates immunogenic T-cell epitopes in CML patients Concurrent molecular alterations in tumors with germ line epidermal growth factor receptor T790M mutations.The BCR-ABLT315I mutation compromises survival in chronic phase chronic myelogenous leukemia patients resistant to tyrosine kinase inhibitors, in a matched pair analysis JUN dependency in distinct early and late BRAF inhibition adaptation states of melanoma

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Phosphorylation of the ATP-binding loop directs oncogenicity of drug-resistant BCR-ABL mutants

http://www.wikidata.org/entity/Q35221149

description

2006 nî lūn-bûn

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2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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Phosphorylation of the ATP-bin ...... drug-resistant BCR-ABL mutants

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Phosphorylation of the ATP-bin ...... drug-resistant BCR-ABL mutants

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Phosphorylation of the ATP-bin ...... drug-resistant BCR-ABL mutants

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Phosphorylation of the ATP-bin ...... drug-resistant BCR-ABL mutants

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Phosphorylation of the ATP-bin ...... drug-resistant BCR-ABL mutants

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Phosphorylation of the ATP-bin ...... drug-resistant BCR-ABL mutants

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

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Phosphorylation of the ATP-bin ...... drug-resistant BCR-ABL mutants

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Ann Ryvkin

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Brian J Skaggs

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Charles L Sawyers

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Elliot M Landaw

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Evangelia Komisopoulou

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Joseph A Loo

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Lauren M Brown

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Mercedes E Gorre

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Michael R Burgess

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Yongming Xie

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P2860

Immunoaffinity profiling of tyrosine phosphorylation in cancer cells

The direct recruitment of BLNK to immunoglobulin alpha couples the B-cell antigen receptor to distal signaling pathways

Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain

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)

EGFR mutation and resistance of non-small-cell lung cancer to gefitinib.

Dasatinib in imatinib-resistant Philadelphia chromosome-positive leukemias

Complementation of the mitotic activator, p80cdc25, by a human protein-tyrosine phosphatase

Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia

Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

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10.1073/PNAS.0609239103

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51

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103

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2006-12-12T00:00:00Z

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6636174

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phosphorylation

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