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18243695
Source:
http://linkedlifedata.com/resource/pubmed/id/18243695
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rdf:type
pubmed:Citation
lifeskim:mentions
umls-concept:C0014442
,
umls-concept:C0243077
,
umls-concept:C0392747
,
umls-concept:C1554963
,
umls-concept:C1710234
pubmed:issue
5
pubmed:dateCreated
2008-3-10
pubmed:abstractText
Explorations of the S(1') subsite of ACE2 via modifications of the P(1') methylene biphenyl moiety of thiol-based metalloprotease inhibitors led to improvements in ACE2 selectivity versus ACE and NEP, while maintaining potent ACE2 inhibition.
pubmed:language
eng
pubmed:journal
http://linkedlifedata.com/resource/pubmed/journal/9107377
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin-Converting Enzyme...
,
http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl-Dipeptidase A
,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfhydryl Compounds
,
http://linkedlifedata.com/resource/pubmed/chemical/angiotensin converting enzyme 2
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1464-3405
pubmed:author
pubmed-author:DeatonDavid NDN
,
pubmed-author:GrahamKevin PKP
,
pubmed-author:GrossJeffrey WJW
,
pubmed-author:MillerAaron BAB
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1681-7
pubmed:meshHeading
pubmed-meshheading:18243695-Angiotensin-Converting Enzyme Inhibitors
,
pubmed-meshheading:18243695-Binding Sites
,
pubmed-meshheading:18243695-Humans
,
pubmed-meshheading:18243695-Models, Molecular
,
pubmed-meshheading:18243695-Molecular Structure
,
pubmed-meshheading:18243695-Peptidyl-Dipeptidase A
,
pubmed-meshheading:18243695-Recombinant Proteins
,
pubmed-meshheading:18243695-Structure-Activity Relationship
,
pubmed-meshheading:18243695-Sulfhydryl Compounds
pubmed:year
2008
pubmed:articleTitle
Thiol-based angiotensin-converting enzyme 2 inhibitors: P1' modifications for the exploration of the S1' subsite.
pubmed:affiliation
Department of Medicinal Chemistry, GlaxoSmithKline, Research Triangle Park, NC 27709, USA. david.n.deaton@gsk.com
pubmed:publicationType
Journal Article