Intrinsic differences between the catalytic properties of the oncogenic NUP214-ABL1 and BCR-ABL1 fusion protein kinases (Q46375245)

21 December 2017

title

Intrinsic differences between the catalytic properties of the oncogenic NUP214-ABL1 and BCR-ABL1 fusion protein kinases (English)

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21 December 2017

author

Kim De Keersmaecker

1

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21 December 2017

Jan Cools

3

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21 December 2017

Giulio Superti-Furga

4

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21 December 2017

Oliver Hantschel

5

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21 December 2017

author name string

M Versele

2

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21 December 2017

publication date

11 September 2008

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21 December 2017

published in

Leukemia

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21 December 2017

volume

22

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21 December 2017

issue

12

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21 December 2017

page(s)

2208-2216

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21 December 2017

https://scigraph.springernature.com/pub.10.1038/leu.2008.242

exact match

0 references

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Regulation of the c-Abl and Bcr-Abl tyrosine kinases

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The P190, P210, and P230 forms of the BCR/ABL oncogene induce a similar chronic myeloid leukemia-like syndrome in mice but have different lymphoid leukemogenic activity

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Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute lymphoblastic leukemia

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Kinase activation and transformation by NUP214-ABL1 is dependent on the context of the nuclear pore

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Structural Basis for the Cytoskeletal Association of Bcr-Abl/c-Abl

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A coiled-coil tetramerization domain of BCR-ABL is essential for the interactions of SH2-containing signal transduction molecules

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Activity of tyrosine kinase inhibitors against human NUP214-ABL1-positive T cell malignancies

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

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A common phosphotyrosine signature for the Bcr-Abl kinase

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Phosphotyrosine mapping in Bcr/Abl oncoprotein using phosphotyrosine-specific immonium ion scanning

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Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry

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c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines

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Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase.

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The structure of Dasatinib (BMS-354825) bound to activated ABL kinase domain elucidates its inhibitory activity against imatinib-resistant ABL mutants

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Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib

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The Src tyrosine kinase Hck is required for Tel-Abl- but not for Tel-Jak2-induced cell transformation.

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The Btk tyrosine kinase is a major target of the Bcr-Abl inhibitor dasatinib

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7 January 2021

Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib, and dasatinib reveal novel kinase and nonkinase targets

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7 January 2021

Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors

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7 January 2021

Use of an oriented peptide library to determine the optimal substrates of protein kinases

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7 January 2021

Recognition and specificity in protein tyrosine kinase-mediated signalling

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7 January 2021

Catalytic domains of tyrosine kinases determine the phosphorylation sites within c-Cbl

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7 January 2021

Identifiers

DOI

10.1038/LEU.2008.242

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21 December 2017

PubMed ID

18784740

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21 December 2017