Reactome: A Curated Pathway Database

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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Name Email address

Pathways authored by Bambara, Robert A (68357)

DB_ID Name
69190 DNA strand elongation
69306 DNA Replication

Details on Person Bambara, Robert A

_displayNameBambara, Robert A
_timestamp2017-08-22 20:36:36
affiliation[Affiliation:73874] University of Rochester School of Medicine and Dentistry
firstnameRobert A
modified[InstanceEdit:73875] 2007-08-03 22:57:00
[InstanceEdit:1243087] D'Eustachio, P, 2011-03-31
[InstanceEdit:8932050] D'Eustachio, Peter, 2016-07-20
(author)[LiteratureReference:68353] Cleavage specificity of Saccharomyces cerevisiae flap endonuclease 1 suggests a double-flap structure as the cellular substrate.
[LiteratureReference:69121] Enzymes and reactions at the eucaryotic DNA replication fork.
[LiteratureReference:69154] CalfRTH-1 nuclease can remove the initiator RNAs of Okazaki fragments by endonuclease activity.
[LiteratureReference:69175] Completion of mammalian lagging strand DNA replication using purified proteins.
[LiteratureReference:111254] AP endonuclease 1 coordinates flap endonuclease 1 and DNA ligase I activity in long patch base excision repair.
[LiteratureReference:176142] The human Rad9-Rad1-Hus1 checkpoint complex stimulates flap endonuclease 1
[LiteratureReference:176251] Evidence that DNA damage detection machinery participates in DNA repair
[LiteratureReference:182817] Processing of an HIV replication intermediate by the human DNA replication enzyme FEN1
[LiteratureReference:182868] The sequential mechanism of HIV reverse transcriptase RNase H
[LiteratureReference:182873] Unique progressive cleavage mechanism of HIV reverse transcriptase RNase H
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