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- Publisher Website: 10.1016/j.cclet.2018.05.017
- Scopus: eid_2-s2.0-85046859714
- WOS: WOS:000438004700009
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Article: Peptide-based Approaches To Identify And Characterize Proteins That Recognize Histone Post-translational Modifications
Title | Peptide-based Approaches To Identify And Characterize Proteins That Recognize Histone Post-translational Modifications |
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Authors | |
Keywords | Crosslinkers Histone PTMs Peptide libraries Peptide microarrays Peptide pull-down |
Issue Date | 2018 |
Publisher | Elsevier Ltd for Chinese Chemical Society. The Journal's web site is located at http://www.chinchemlett.com.cn |
Citation | Chinese Chemical Letters, 2018, v. 29, p. 1051-1057 How to Cite? |
Abstract | Increasing amount of evidence suggests that post-translational modifications (PTMs) on histones are involved in regulating DNA-associated processes such as gene expression and DNA-damage repair. To identify and characterize proteins that recognize histone PTMs, tools relying on synthetic peptides have been constructed and widely used in recent years. In this review, we first summarize the development and applications of these tools, which includes peptide-based pull-down assay and peptide-array-based high-throughput screening. The limitation of peptide-based approaches is then discussed, followed by a brief description on recent development of nucleosome-based tools. |
Persistent Identifier | http://hdl.handle.net/10722/269417 |
ISSN | 2023 Impact Factor: 9.4 2023 SCImago Journal Rankings: 1.662 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | LIN, J | - |
dc.contributor.author | Li, XD | - |
dc.date.accessioned | 2019-04-24T08:07:17Z | - |
dc.date.available | 2019-04-24T08:07:17Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | Chinese Chemical Letters, 2018, v. 29, p. 1051-1057 | - |
dc.identifier.issn | 1001-8417 | - |
dc.identifier.uri | http://hdl.handle.net/10722/269417 | - |
dc.description.abstract | Increasing amount of evidence suggests that post-translational modifications (PTMs) on histones are involved in regulating DNA-associated processes such as gene expression and DNA-damage repair. To identify and characterize proteins that recognize histone PTMs, tools relying on synthetic peptides have been constructed and widely used in recent years. In this review, we first summarize the development and applications of these tools, which includes peptide-based pull-down assay and peptide-array-based high-throughput screening. The limitation of peptide-based approaches is then discussed, followed by a brief description on recent development of nucleosome-based tools. | - |
dc.language | eng | - |
dc.publisher | Elsevier Ltd for Chinese Chemical Society. The Journal's web site is located at http://www.chinchemlett.com.cn | - |
dc.relation.ispartof | Chinese Chemical Letters | - |
dc.subject | Crosslinkers | - |
dc.subject | Histone PTMs | - |
dc.subject | Peptide libraries | - |
dc.subject | Peptide microarrays | - |
dc.subject | Peptide pull-down | - |
dc.title | Peptide-based Approaches To Identify And Characterize Proteins That Recognize Histone Post-translational Modifications | - |
dc.type | Article | - |
dc.identifier.email | Li, XD: xiangli@hku.hk | - |
dc.identifier.authority | Li, XD=rp01562 | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.cclet.2018.05.017 | - |
dc.identifier.scopus | eid_2-s2.0-85046859714 | - |
dc.identifier.hkuros | 297531 | - |
dc.identifier.volume | 29 | - |
dc.identifier.spage | 1051 | - |
dc.identifier.epage | 1057 | - |
dc.identifier.isi | WOS:000438004700009 | - |
dc.publisher.place | China | - |
dc.identifier.issnl | 1001-8417 | - |