DNA recognition by the RUNX1 transcription factor is mediated by an allosteric transition in the RUNT domain and by DNA bending (Q27639779)

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13 December 2019

title

DNA recognition by the RUNX1 transcription factor is mediated by an allosteric transition in the RUNT domain and by DNA bending (English)

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13 December 2019

2

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13 December 2019

author name string

Deborah Bartfeld

1

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13 December 2019

Graeme C Couture

3

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13 December 2019

Dov Rabinovich

4

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13 December 2019

Felix Frolow

5

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13 December 2019

Ditsa Levanon

6

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13 December 2019

Yoram Groner

7

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13 December 2019

Zippora Shakked

8

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13 December 2019

publication date

1 October 2002

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13 December 2019

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13 December 2019

volume

10

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13 December 2019

issue

10

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13 December 2019

page(s)

1395-1407

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The AML1-ETO chimaeric transcription factor in acute myeloid leukaemia: biology and clinical significance

13 December 2019

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AML1, AML2, and AML3, the human members of the runt domain gene-family: cDNA structure, expression, and chromosomal localization

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The RUNX3 gene--sequence, structure and regulated expression

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Architecture and anatomy of the genomic locus encoding the human leukemia-associated transcription factor RUNX1/AML1

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Spatial and temporal expression pattern of Runx3 (Aml2) and Runx1 (Aml1) indicates non-redundant functions during mouse embryogenesis

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Expression of the human acute myeloid leukemia gene AML1 is regulated by two promoter regions

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Transcription-coupled translation control of AML1/RUNX1 is mediated by cap- and internal ribosome entry site-dependent mechanisms.

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The Runx3 transcription factor regulates development and survival of TrkC dorsal root ganglia neurons

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The Ig fold of the core binding factor alpha Runt domain is a member of a family of structurally and functionally related Ig-fold DNA-binding domains

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Structural basis for the heterodimeric interaction between the acute leukaemia-associated transcription factors AML1 and CBFbeta

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7 January 2021

The leukemia-associated AML1 (Runx1)--CBF beta complex functions as a DNA-induced molecular clamp

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