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dc.contributor.authorRamakrishna Suresh-
dc.date.accessioned2019-11-26T04:07:59Z-
dc.date.available2019-11-26T04:07:59Z-
dc.date.issued2017-06-
dc.identifier.citationOPEN BIOLOGY, v. 7, no. 6, Article no. 170016en_US
dc.identifier.issn2046-2441-
dc.identifier.urihttps://royalsocietypublishing.org/doi/10.1098/rsob.170016-
dc.identifier.urihttps://repository.hanyang.ac.kr/handle/20.500.11754/114507-
dc.description.abstractDeubiquitylating enzymes (DUBs) reverse the ubiquitylation of target proteins, thereby regulating diverse cellular functions. In contrast to the plethora of research being conducted on the ability of DUBs to counter the degradation of cellular proteins or auto-ubiquitylated E3 ligases, very little is known about the mechanisms of DUB regulation. In this review paper, we summarize a novel possible mechanism of DUB deubiquitylation by other DUBs. The available data suggest the need for further experiments to validate and characterize this notion of 'Dubbing DUBs'. The current studies indicate that the idea of deubiquitylation of DUBs by other DUBs is still in its infancy. Nevertheless, future research holds the promise of validation of this concept.en_US
dc.description.sponsorshipThis study was supported by a grant of the National Research Foundation of Korea (2015R1C1A1A01054482).en_US
dc.language.isoen_USen_US
dc.publisherROYAL SOCen_US
dc.subjectauto-regulationen_US
dc.subjectdeubiquitylating DUBsen_US
dc.subjectproteasome degradationen_US
dc.subjectself-deubiquitylationen_US
dc.subjectubiquitylationen_US
dc.titleDeubiquitylation of deubiquitylasesen_US
dc.typeArticleen_US
dc.relation.no6-
dc.relation.volume7-
dc.identifier.doi10.1098/rsob.170016-
dc.relation.page1-11-
dc.relation.journalOPEN BIOLOGY-
dc.contributor.googleauthorHaq, Saba-
dc.contributor.googleauthorRamakrishna, Suresh-
dc.relation.code2017008374-
dc.sector.campusS-
dc.sector.daehakGRADUATE SCHOOL OF BIOMEDICAL SCIENCE AND ENGINEERING[S]-
dc.identifier.pidsuri28-
dc.identifier.orcidhttp://orcid.org/0000-0002-4038-1085-


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