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PTPIP51 in Protein Interactions: Regulation and In Situ Interacting Partners

PTPIP51 in Protein Interactions: Regulation and In Situ Interacting Partners

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1019867420

PTPIP51 in Protein Interactions: Regulation and In Situ Interacting Partners

About this item

Full title

PTPIP51 in Protein Interactions: Regulation and In Situ Interacting Partners

Publisher

New York: Springer-Verlag

Journal title

Cell biochemistry and biophysics, 2012-07, Vol.63 (3), p.211-222

Language

English

Formats

Publication information

Publisher

New York: Springer-Verlag

More information

Scope and Contents

Contents

This study investigated the regulation of 14-3-3β binding to PTPIP51 by the tyrosine phosphorylation status of PTPIP51. The tyrosine 176 residue is phosphorylated by c-Src. Up to now, nothing is known about the impact of such well-established phosphorylation events on the interaction profile of PTPIP51 with its partners of the mitogen-activated pro...

Alternative Titles

Full title

PTPIP51 in Protein Interactions: Regulation and In Situ Interacting Partners

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_journals_1019867420

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1019867420

Other Identifiers

ISSN

1085-9195

E-ISSN

1559-0283

DOI

10.1007/s12013-012-9357-y

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