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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2008-3-17
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pubmed:abstractText |
To compare backbone-induced susceptibilities with affinity changes that are caused by side-chain modifications in the respective positions, structure activity relationship studies on a series of NT(8-13) analogues were performed providing valuable insights into the major requirement for neurotensin receptor recognition and activation. The data led us to highly potent NTR1 ligands and the generation of a pharmacophore model that will be helpful for the discovery of therapeutically relevant non-peptidic NTR1 agonists.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1464-3405
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2013-8
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pubmed:meshHeading |
pubmed-meshheading:18276136-Animals,
pubmed-meshheading:18276136-Calcium,
pubmed-meshheading:18276136-Molecular Structure,
pubmed-meshheading:18276136-Mutagenesis, Site-Directed,
pubmed-meshheading:18276136-Mutation,
pubmed-meshheading:18276136-Neurotensin,
pubmed-meshheading:18276136-Palladium,
pubmed-meshheading:18276136-Peptide Fragments,
pubmed-meshheading:18276136-Protein Binding,
pubmed-meshheading:18276136-RNA, Messenger,
pubmed-meshheading:18276136-Receptors, Neurotensin,
pubmed-meshheading:18276136-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:18276136-Structure-Activity Relationship,
pubmed-meshheading:18276136-Swine
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pubmed:year |
2008
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pubmed:articleTitle |
Peptide backbone modifications on the C-terminal hexapeptide of neurotensin.
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pubmed:affiliation |
Department of Chemistry and Pharmacy, Emil Fischer Center, Friedrich Alexander University, D-91052 Erlangen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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