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Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms

Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_c95928c8f6c04cf69fb1889c1608aeab

Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms

About this item

Full title

Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2020-04, Vol.11 (1), p.1621-1621, Article 1621

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Activin receptor-like kinase 1 (ALK1)-mediated endothelial cell signalling in response to bone morphogenetic protein 9 (BMP9) and BMP10 is of significant importance in cardiovascular disease and cancer. However, detailed molecular mechanisms of ALK1-mediated signalling remain unclear. Here, we report crystal structures of the BMP10:ALK1 complex at...

Alternative Titles

Full title

Molecular basis of ALK1-mediated signalling by BMP9/BMP10 and their prodomain-bound forms

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_c95928c8f6c04cf69fb1889c1608aeab

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_c95928c8f6c04cf69fb1889c1608aeab

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-020-15425-3

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