001     97339
005     20250731113521.0
024 7 _ |a pmid:20965620
|2 pmid
024 7 _ |a 10.1016/j.ejmech.2010.09.057
|2 doi
024 7 _ |a 1768-3254
|2 ISSN
024 7 _ |a 0223-5234
|2 ISSN
024 7 _ |a WOS:000285485000044
|2 WOS
024 7 _ |a openalex:W2060859685
|2 openalex
037 _ _ |a PHPPUBDB-20356
041 _ _ |a eng
082 _ _ |a 610
100 1 _ |a Attolino, E.
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a Structure-based approach to nanomolar, water soluble matrix metalloproteinases inhibitors (MMPIs).
260 _ _ |a Amsterdam [u.a.]
|b Elsevier Science
|c 2010
300 _ _ |a 5919-5925
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a article
|2 DRIVER
336 7 _ |a Journal Article
|m journal
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
440 _ 0 |a Eur. J. Med. Chem.
|v 45
|y 12
|x 0223-5234
|0 PERI:(DE-600)2005170-0
500 _ _ |3 Converted on 2013-05-30 15:49
500 _ _ |3 Converted on 2013-06-21 19:21
520 _ _ |a N-arylsulfonyl-based MMPs inhibitors (MMPIs) are among the most prominent inhibitors possessing nanomolar affinity. However, their poor bioavailability remains critical for the drug development of this family of molecules. The structural analysis of the complex of NNGH (the most representative member of the family) with MMP-12 provided us with the basis to effectively design simple NNGH analogues with enhanced solubility in water. Following this approach, the sec-butyl residue, not directly involved in the binding with MMP, has been replaced with hydrophilic residues thus yielding new potent inhibitors soluble in water.
536 _ _ |0 G:(DE-H253)POF2-No-Ref-20130405
|f POF II
|x 0
|c POF2-544
|a FS Beamline without reference (POF2-544)
588 _ _ |a Dataset connected to Pubmed
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Matrix Metalloproteinase Inhibitors
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Molecular Structure
650 _ 2 |2 MeSH
|a Nanostructures: chemistry
650 _ 2 |2 MeSH
|a Protease Inhibitors: chemical synthesis
650 _ 2 |2 MeSH
|a Protease Inhibitors: chemistry
650 _ 2 |2 MeSH
|a Protease Inhibitors: pharmacology
650 _ 2 |2 MeSH
|a Solubility
650 _ 2 |2 MeSH
|a Stereoisomerism
650 _ 2 |2 MeSH
|a Structure-Activity Relationship
650 _ 2 |2 MeSH
|a Sulfones: chemical synthesis
650 _ 2 |2 MeSH
|a Sulfones: chemistry
650 _ 2 |2 MeSH
|a Sulfones: pharmacology
650 _ 2 |2 MeSH
|a Water: chemistry
650 _ 7 |0 0
|2 NLM Chemicals
|a Matrix Metalloproteinase Inhibitors
650 _ 7 |0 0
|2 NLM Chemicals
|a Protease Inhibitors
650 _ 7 |0 0
|2 NLM Chemicals
|a Sulfones
650 _ 7 |0 7732-18-5
|2 NLM Chemicals
|a Water
693 _ _ |0 EXP:(DE-H253)Unknown-BL-20150101
|f Unknown DESY Beamline
|x 0
|6 EXP:(DE-H253)Unknown-BL-20150101
700 1 _ |a Calderone, V.
700 1 _ |a Dragoni, E.
700 1 _ |a Fragai, M.
700 1 _ |a Richichi, B.
700 1 _ |a Luchinat, C.
700 1 _ |a Nativi, C.
773 _ _ |0 PERI:(DE-600)2005170-0
|a 10.1016/j.ejmech.2010.09.057
|g Vol. 45, p. 5919-5925
|p 5919-5925
|q 45<5919-5925
|t European journal of medicinal chemistry
|v 45
|x 0223-5234
|y 2010
856 4 0 |u http://www.ncbi.nlm.nih.gov/pubmed/20965620
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914 1 _ |y 2010
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980 _ _ |a ConvertedRecord


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