Full metadata record
DC Field | Value | Language |
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dc.contributor.author | Murale, Dhiraj P. | - |
dc.contributor.author | Hong, Seong Cheol | - |
dc.contributor.author | Jang, Se-young | - |
dc.contributor.author | Lee, Jun-Seok | - |
dc.date.accessioned | 2024-01-19T21:03:55Z | - |
dc.date.available | 2024-01-19T21:03:55Z | - |
dc.date.created | 2021-09-04 | - |
dc.date.issued | 2018-12-18 | - |
dc.identifier.issn | 1439-4227 | - |
dc.identifier.uri | https://pubs.kist.re.kr/handle/201004/120564 | - |
dc.description.abstract | Many intracellular proteins are metabolically unstable, and their half-life was known to be controlled by the "N-end rule," that is, the N-terminal residue controlled protein stability. To visualize or measure the cellular stability of a protein, depending on the N-terminal residues, attention is being paid to the development of selective labeling methods for individual N-terminal amino acids. However, there are only a limited number of functional groups available for specific N-terminal amino acid labeling in a biological environment. Herein, we report a re-examination of salicylaldehyde ester for selective N-terminal residue tagging. Salicylaldehyde ester has been used for chemical ligation to N-terminal serine or threonine under pyridine/acetic acid conditions. Inspired by previous selective serine/threonine labeling, N-terminal labeling of salicylaldehyde ester in aqueous buffer has been examined by using boron-dipyrromethene (BODIPY), rhodamine, and coumarin probes. Surprisingly, the selectivity not only significantly differed, depending on the fluorophore incorporated in salicylaldehyde, but was also perturbed by the addition of a small fraction of phosphate-buffered saline. In particular, the coumarin-based salicylaldehyde ester probe showed notable selectivity against N-terminal cysteine under aqueous buffer conditions. This result reveals the serendipitous discovery of a new N-terminal cysteine labeling strategy. | - |
dc.language | English | - |
dc.publisher | WILEY-V C H VERLAG GMBH | - |
dc.subject | END RULE | - |
dc.subject | PROTEIN | - |
dc.subject | SERINE | - |
dc.subject | BIOCONJUGATION | - |
dc.subject | THREONINE | - |
dc.subject | PEPTIDES | - |
dc.subject | LIGATION | - |
dc.title | Reinvestigation of an O-Salicylaldehyde Ester Functional Group in Aqueous Buffer and Discovery of a Coumarin Scaffold Probe for Selective N-Terminal Cysteine Labeling | - |
dc.type | Article | - |
dc.identifier.doi | 10.1002/cbic.201800565 | - |
dc.description.journalClass | 1 | - |
dc.identifier.bibliographicCitation | CHEMBIOCHEM, v.19, no.24, pp.2545 - 2549 | - |
dc.citation.title | CHEMBIOCHEM | - |
dc.citation.volume | 19 | - |
dc.citation.number | 24 | - |
dc.citation.startPage | 2545 | - |
dc.citation.endPage | 2549 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.identifier.wosid | 000453835200004 | - |
dc.identifier.scopusid | 2-s2.0-85056416110 | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Medicinal | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Pharmacology & Pharmacy | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | END RULE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | SERINE | - |
dc.subject.keywordPlus | BIOCONJUGATION | - |
dc.subject.keywordPlus | THREONINE | - |
dc.subject.keywordPlus | PEPTIDES | - |
dc.subject.keywordPlus | LIGATION | - |
dc.subject.keywordAuthor | amino acids | - |
dc.subject.keywordAuthor | fluorescence | - |
dc.subject.keywordAuthor | labeling agents | - |
dc.subject.keywordAuthor | peptides | - |
dc.subject.keywordAuthor | salicylaldehyde ester | - |
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