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rdf:type |
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lifeskim:mentions |
umls-concept:C0001721,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0025543,
umls-concept:C0205314,
umls-concept:C0242957,
umls-concept:C0444669,
umls-concept:C0623362,
umls-concept:C0679622,
umls-concept:C0919336,
umls-concept:C1167622,
umls-concept:C1551022,
umls-concept:C1707689,
umls-concept:C1961136,
umls-concept:C1979963,
umls-concept:C2003903
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pubmed:issue |
13
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pubmed:dateCreated |
2009-6-9
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pubmed:abstractText |
A serendipitous discovery that the metalloprotease binding profile of a novel class of 2-carboxamide-3-hydroxamic acid piperidines could be significantly attenuated by the modification of the unexplored P1 substituent enabled the design and synthesis of a novel 2-carboxamide-1-hydroxamic acid cyclohexyl scaffold core that exhibited excellent HER-2 potency and unprecedented MMP-selectivity that we believe would not have been possible via conventional P1' perturbations.
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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 |
Jul
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pubmed:issn |
1464-3405
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pubmed:author |
pubmed-author:BurnsDavid MDM,
pubmed-author:CovingtonMaryanne BMB,
pubmed-author:FridmanJordan SJS,
pubmed-author:FriedmanSteveS,
pubmed-author:HeChunhongC,
pubmed-author:KatiyarKamnaK,
pubmed-author:LiYanlongY,
pubmed-author:LiYun-LongYL,
pubmed-author:MarandoCindy ACA,
pubmed-author:MetcalfBrianB,
pubmed-author:QianDing-QuanDQ,
pubmed-author:ScherlePeggyP,
pubmed-author:ShiEricE,
pubmed-author:WynnRichardR,
pubmed-author:XuMeizhongM,
pubmed-author:YaoWenqingW,
pubmed-author:ZhangColinC,
pubmed-author:ZhuoJincongJ
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3525-30
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:19457660-ADAM Proteins,
pubmed-meshheading:19457660-Amyloid Precursor Protein Secretases,
pubmed-meshheading:19457660-Antineoplastic Agents,
pubmed-meshheading:19457660-Cell Line, Tumor,
pubmed-meshheading:19457660-Drug Design,
pubmed-meshheading:19457660-Humans,
pubmed-meshheading:19457660-Hydroxamic Acids,
pubmed-meshheading:19457660-Matrix Metalloproteinase 2,
pubmed-meshheading:19457660-Membrane Proteins,
pubmed-meshheading:19457660-Protein Binding,
pubmed-meshheading:19457660-Receptor, erbB-2,
pubmed-meshheading:19457660-Structure-Activity Relationship,
pubmed-meshheading:19457660-Substrate Specificity
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pubmed:year |
2009
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pubmed:articleTitle |
Compelling P1 substituent affect on metalloprotease binding profile enables the design of a novel cyclohexyl core scaffold with excellent MMP selectivity and HER-2 sheddase inhibition.
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pubmed:affiliation |
Incyte Corporation, Department of Medicinal Chemistry, Wilmington, DE 19880, USA. dburns@incyte.com
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pubmed:publicationType |
Journal Article
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