|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0007987,
umls-concept:C0014898,
umls-concept:C0017953,
umls-concept:C0023690,
umls-concept:C0039808,
umls-concept:C0076506,
umls-concept:C0205345,
umls-concept:C0205360,
umls-concept:C0439849,
umls-concept:C0445223,
umls-concept:C0679199,
umls-concept:C1552599,
umls-concept:C1704787,
umls-concept:C1707271,
umls-concept:C2603343
|
|
pubmed:issue |
23
|
|
pubmed:dateCreated |
2006-6-7
|
|
pubmed:abstractText |
A pathway has been devised, wherein a phenolic ester of a C-terminal peptide is ligated with an N-terminal peptide through two consecutive acyl migrations. In the first transacylation, the C-terminus is transferred from a phenol to a newly liberated ortho-thiol function. Subsequently, the acyl group is transported to a proximal benzylamine through a six-membered transition state.
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pubmed:grant |
|
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pubmed:language |
eng
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|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jun
|
|
pubmed:issn |
0002-7863
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
14
|
|
pubmed:volume |
128
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
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pubmed:pagination |
7460-2
|
|
pubmed:dateRevised |
2008-1-17
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|
pubmed:meshHeading |
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
Studies related to the relative thermodynamic stability of C-terminal peptidyl esters of O-hydroxy thiophenol: emergence of a doable strategy for non-cysteine ligation applicable to the chemical synthesis of glycopeptides.
|
|
pubmed:affiliation |
Laboratory for Bioorganic Chemistry, Sloan-Kettering Institute for Cancer Research, New York, New York 10021, USA.
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|
pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
|
