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Title:

Tailoring of integrin ligands: probing the charge capability of the metal ion-dependent adhesion site.

Document type:
Journal Article
Author(s):
Bollinger, M; Manzenrieder, F; Kolb, R; Bochen, A; Neubauer, S; Marinelli, L; Limongelli, V; Novellino, E; Moessmer, G; Pell, R; Lindner, W; Fanous, J; Hoffman, A; Kessler, H
Abstract:
Intervention in integrin-mediated cell adhesion and integrin signaling pathways is an ongoing area of research in medicinal chemistry and drug development. One key element in integrin-ligand interaction is the coordination of the bivalent cation at the metal ion-dependent adhesion site (MIDAS) by a carboxylic acid function, a consistent feature of all integrin ligands. With the exception of the recently discovered hydroxamic acids, all bioisosteric attempts to replace the carboxylic acid of inte...     »
Journal title abbreviation:
J Med Chem
Year:
2012
Journal volume:
55
Journal issue:
2
Pages contribution:
871-82
Language:
eng
Fulltext / DOI:
doi:10.1021/jm2013826
Pubmed ID:
http://view.ncbi.nlm.nih.gov/pubmed/22185640
Print-ISSN:
0022-2623
TUM Institution:
Institut für Klinische Chemie und Pathobiochemie
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