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ScharerDavid Orlando

Scharer, Orlando D.
Schärer Lab.
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dc.citation.endPage 186 -
dc.citation.number 2 -
dc.citation.startPage 184 -
dc.citation.title MOLECULAR CELL -
dc.citation.volume 28 -
dc.contributor.author Schaerer, Orlando D. -
dc.date.accessioned 2023-12-22T09:09:05Z -
dc.date.available 2023-12-22T09:09:05Z -
dc.date.created 2017-01-26 -
dc.date.issued 2007-10 -
dc.description.abstract The structure of the Rad4/Rad23 protein, shown in a recent issue of Nature (Min and Pavletich, 2007), reveals how structurally diverse lesions are recognized in eukaryotic nucleotide excision repair: by probing for accessible nondarnaged DNA opposite the lesion. -
dc.identifier.bibliographicCitation MOLECULAR CELL, v.28, no.2, pp.184 - 186 -
dc.identifier.doi 10.1016/j.molcel.2007.10.006 -
dc.identifier.issn 1097-2765 -
dc.identifier.scopusid 2-s2.0-35348954826 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/21276 -
dc.identifier.url http://www.sciencedirect.com/science/article/pii/S1097276507006685 -
dc.identifier.wosid 000250739800004 -
dc.language 영어 -
dc.publisher CELL PRESS -
dc.title Achieving broad substrate specificity in damage recognition by binding accessible nondamaged DNA -
dc.type Article -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus NUCLEOTIDE EXCISION-REPAIR -

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