Log in to save to my catalogue

Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin

Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1083899

Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin

About this item

Full title

Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin

Publisher

Chichester, UK: John Wiley & Sons, Ltd

Journal title

EMBO reports, 2001-06, Vol.2 (6), p.505-510

Language

English

Formats

Publication information

Publisher

Chichester, UK: John Wiley & Sons, Ltd

More information

Scope and Contents

Contents

Protein phosphorylation represents a ubiquitous control mechanism in living cells. The structural prerequisites and consequences of this important post‐translational modification, however, are poorly understood. Oncoprotein 18/stathmin (Op18) is a globally disordered phosphoprotein that is involved in the regulation of the microtubule (MT) filament...

Alternative Titles

Full title

Phosphorylation disrupts the central helix in Op18/stathmin and suppresses binding to tubulin

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1083899

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1083899

Other Identifiers

ISSN

1469-221X

E-ISSN

1469-3178

DOI

10.1093/embo-reports/kve105

How to access this item