9871551

Source:http://linkedlifedata.com/resource/pubmed/id/9871551

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0020314, umls-concept:C0205549, umls-concept:C0220781, umls-concept:C0243077, umls-concept:C0623362, umls-concept:C1257890, umls-concept:C1707689, umls-concept:C1883254
pubmed:issue	7
pubmed:dateCreated	1999-1-27
pubmed:abstractText	Examination of the S1 area of the active site of pro-stromelysin has led us to the design of novel and potent inhibitors of matrix metalloproteinases containing constrained quaternary-hydroxy group at P1. The synthesis and biological activity of these compounds with variations at P1', P2', and P3' will be described.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9107377
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Collagenases, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors, http://linkedlifedata.com/resource/pubmed/chemical/Hydroxamic Acids, http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents, http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 1, http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinase 3, http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/prostromelysin
pubmed:status	MEDLINE
pubmed:month	Apr
pubmed:issn	0960-894X
pubmed:author	pubmed-author:ArnerE CEC, pubmed-author:CopelandR ARA, pubmed-author:CovingtonM BMB, pubmed-author:DeciccoC PCP, pubmed-author:HardmanK DKD, pubmed-author:JacobsonI CIC, pubmed-author:MagoldaR LRL, pubmed-author:ReddyP GPG, pubmed-author:WassermanZ RZR
pubmed:issnType	Print
pubmed:day	7
pubmed:volume	8
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	837-42
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:9871551-Catalytic Domain, pubmed-meshheading:9871551-Collagenases, pubmed-meshheading:9871551-Computer Simulation, pubmed-meshheading:9871551-Drug Design, pubmed-meshheading:9871551-Enzyme Precursors, pubmed-meshheading:9871551-Hydrogen Bonding, pubmed-meshheading:9871551-Hydroxamic Acids, pubmed-meshheading:9871551-Indicators and Reagents, pubmed-meshheading:9871551-Matrix Metalloproteinase 1, pubmed-meshheading:9871551-Matrix Metalloproteinase 3, pubmed-meshheading:9871551-Metalloendopeptidases, pubmed-meshheading:9871551-Models, Molecular, pubmed-meshheading:9871551-Molecular Conformation, pubmed-meshheading:9871551-Molecular Structure, pubmed-meshheading:9871551-Protease Inhibitors, pubmed-meshheading:9871551-Protein Conformation, pubmed-meshheading:9871551-Structure-Activity Relationship
pubmed:year	1998
pubmed:articleTitle	Structure-based design and synthesis of a series of hydroxamic acids with a quaternary-hydroxy group in P1 as inhibitors of matrix metalloproteinases.
pubmed:affiliation	DuPont Merck Pharmaceutical Company, Department of Physical and Chemical Science, Wilmington, Delaware, USA.
pubmed:publicationType	Journal Article