Reactome: A Curated Pathway Database
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Query author contributions in Reactome

Reactome depends on collaboration between our curation team and outside experts to assemble and peer-review its pathway modules. The integration of ORCID within Reactome enables us to meet a key challenge with authoring, curating and reviewing biological information by incentivizing and crediting the external experts that contribute their expertise and time to the Reactome curation process. More information is available at ORCID and Reactome.

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Details on Person Lees-Miller, SP

Class:IdPerson:69538
_displayNameLees-Miller, SP
_timestamp0000-00-00 00:00:00
initialSP
surnameLees-Miller
(author)[LiteratureReference:69530] ATM associates with and phosphorylates p53: mapping the region of interaction.
[LiteratureReference:76285] Conversion of phosphoglycolate to phosphate termini on 3' overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1.
[LiteratureReference:76305] Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair.
[LiteratureReference:76313] Protein phosphatases regulate DNA-dependent protein kinase activity.
[LiteratureReference:76318] Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNA-dependent protein kinase.
[LiteratureReference:76319] The DNA-dependent protein kinase interacts with DNA to form a protein-DNA complex that is disrupted by phosphorylation.
[LiteratureReference:76321] The DNA-dependent protein kinase is inactivated by autophosphorylation of the catalytic subunit.
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No pathways have been reviewed or authored by Lees-Miller, SP (69538)