Conformational changes of the glucocorticoid receptor ligand binding domain induced by ligand and cofactor binding, and the location of cofactor binding sites determined by hydrogen/deuterium exchange mass spectrometry (Q36458264)

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Language	Label	Description	Also known as
English	Conformational changes of the glucocorticoid receptor ligand binding domain induced by ligand and cofactor binding, and the location of cofactor binding sites determined by hydrogen/deuterium exchange mass spectrometry	scientific article

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scholarly article

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Europe PubMed Central

PMC publication ID

14 August 2017

Conformational changes of the glucocorticoid receptor ligand binding domain induced by ligand and cofactor binding, and the location of cofactor binding sites determined by hydrogen/deuterium exchange mass spectrometry (English)

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

1 reference

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author name string

Lee Frego

1

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Europe PubMed Central

PMC publication ID

14 August 2017

Walter Davidson

2

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Europe PubMed Central

PMC publication ID

14 August 2017

publication date

1 April 2006

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Europe PubMed Central

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14 August 2017

Protein Science

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Europe PubMed Central

PMC publication ID

14 August 2017

15

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Europe PubMed Central

PMC publication ID

14 August 2017

4

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

722-730

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Europe PubMed Central

PMC publication ID

14 August 2017

Discovery and characterization of a substrate selective p38alpha inhibitor

1 reference

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The three-dimensional structures of antagonistic and agonistic forms of the glucocorticoid receptor ligand-binding domain: RU-486 induces a transconformation that leads to active antagonism

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Mechanisms involved in the side effects of glucocorticoids

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Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition

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RU486-induced glucocorticoid receptor agonism is controlled by the receptor N terminus and by corepressor binding

1 reference

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Cooperativity of glucocorticoid response elements located far upstream of the tyrosine aminotransferase gene

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Dynamics and ligand-induced solvent accessibility changes in human retinoid X receptor homodimer determined by hydrogen deuterium exchange and mass spectrometry

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12 December 2020

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Amide hydrogen exchange determined by mass spectrometry: application to rabbit muscle aldolase

1 reference

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12 December 2020

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Deuterium exchange mass spectrometry as a probe of protein kinase activation. Analysis of wild-type and constitutively active mutants of MAP kinase kinase-1

1 reference

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Fourier transform ion cyclotron resonance mass spectrometric detection of small Ca(2+)-induced conformational changes in the regulatory domain of human cardiac troponin C

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Identifiers

10.1110/PS.051781406

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 August 2017

ResearchGate publication ID

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