Biophysical studies of the interaction between calmodulin and the R287-T311 region of human estrogen receptor α reveals an atypical binding process
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Identification of polyproline II regions derived from the proline-rich nuclear receptor coactivators PNRC and PNRC2: new insights for ERα coactivator interactions.Calmodulin Lobes Facilitate Dimerization and Activation of Estrogen Receptor-α.Discovery at the interface: Toward novel anti-proliferative agents targeting human estrogen receptor/S100 interactions.Concentration-dependent and surface-assisted self-assembly properties of a bioactive estrogen receptor α-derived peptide
P2860
Biophysical studies of the interaction between calmodulin and the R287-T311 region of human estrogen receptor α reveals an atypical binding process
description
im März 2012 veröffentlichter wissenschaftlicher Artikel
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wetenschappelijk artikel
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наукова стаття, опублікована в березні 2012
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name
Biophysical studies of the int ...... ls an atypical binding process
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Biophysical studies of the int ...... ls an atypical binding process
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type
label
Biophysical studies of the int ...... ls an atypical binding process
@en
Biophysical studies of the int ...... ls an atypical binding process
@nl
prefLabel
Biophysical studies of the int ...... ls an atypical binding process
@en
Biophysical studies of the int ...... ls an atypical binding process
@nl
P2093
P50
P1476
Biophysical studies of the int ...... ls an atypical binding process
@en
P2093
Cillian Byrne
Guy Leclercq
Jean-Claude Tabet
Magali Nicaise
Michel Desmadril
Sandrine Bourgoin-Voillard
P304
P356
10.1016/J.BBRC.2012.02.028
P407
P577
2012-03-01T00:00:00Z