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Peter Hornbeck

Researcher at Cell Signaling Technology

Publications -  73
Citations -  7669

Peter Hornbeck is an academic researcher from Cell Signaling Technology. The author has contributed to research in topics: Phosphorylation & Antibody. The author has an hindex of 25, co-authored 71 publications receiving 6395 citations. Previous affiliations of Peter Hornbeck include University of California, San Francisco & National Institutes of Health.

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PhosphoSitePlus, 2014: mutations, PTMs and recalibrations

TL;DR: The ‘PTMVar’ dataset, an intersect of missense mutations and PTMs from PSP, identifies over 25 000 PTMVars (PTMs Impacted by Variants) that can rewire signaling pathways.
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PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse

TL;DR: PhosphoSitePlus as discussed by the authors is an open, comprehensive, manually curated and interactive resource for studying experimentally observed post-translational modifications, primarily of human and mouse proteins.
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The BioPAX community standard for pathway data sharing

Emek Demir, +94 more
- 01 Sep 2010 - 
TL;DR: Thousands of interactions, organized into thousands of pathways, from many organisms are available from a growing number of databases, and this large amount of pathway data in a computable form will support visualization, analysis and biological discovery.
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PhosphoSite: A bioinformatics resource dedicated to physiological protein phosphorylation.

TL;DR: As it develops into a comprehensive resource of known in vivo phosphorylation sites, it is expected that PhosphoSite will be a valuable tool for researchers seeking to understand the role of intracellular signaling pathways in a wide variety of biological processes.
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Akt–RSK–S6 Kinase Signaling Networks Activated by Oncogenic Receptor Tyrosine Kinases

TL;DR: A phosphoproteomic approach to identify targets of three core signaling pathways—all of which involve activation of AGC family kinases—downstream of oncogenic RTKs is developed, revealing previously unidentified Akt–RSK–S6 kinase substrates that merit further consideration as targets for combination therapy with RTKIs.