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http://purl.obolibrary.org/obo/RO_0002204
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http://www.tkuhn.ch/bel2nanopub/RAlowT5zANyJV68gcz46xMh4oCczyxM9lxDNamssW8Dzk#_4
http://purl.obolibrary.org/obo/BFO_0000066
http://purl.obolibrary.org/obo/CL_0000115
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http://www.selventa.com/vocabulary/increases
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http://www.w3.org/1999/02/22-rdf-syntax-ns#type
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http://www.w3.org/2000/01/rdf-schema#label
p(HGNC:TNF) -> cat(p(HGNC:MMP2))
http://www.tkuhn.ch/bel2nanopub/RAlowT5zANyJV68gcz46xMh4oCczyxM9lxDNamssW8Dzk#provenance
http://resource.belframework.org/belframework/20131211/knowledge/small_corpus.bel
http://purl.org/dc/elements/1.1/description
Approximately 2000 hand curated statements drawn from 57 PubMeds.
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Copyright (c) 2011-2012, Selventa. All Rights Reserved.
http://resource.belframework.org/belframework/20131211/knowledge/small_corpus.bel
http://purl.org/dc/elements/1.1/title
BEL Framework Small Corpus Document
http://resource.belframework.org/belframework/20131211/knowledge/small_corpus.bel
http://purl.org/dc/terms/license
Creative Commons Attribution-Non-Commercial-ShareAlike 3.0 Unported License
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http://www.w3.org/ns/prov#value
Incubation of medium conditioned by human smooth muscle cells that contained pro-MMP-2,
with plasma membrane extracts prepared from EC treated with TNF-α, interleukin-1β,
or OxLDL, increased the proteolytic conversion of 72-kDa proMMP-2 to new
gelatinolytic bands of 70- and 68-kDa corresponding to the processed active MMP-2
(Fig. 7A). Proteolytic processing of pro-MMP-2 was reduced in membrane extracts
incubated with anti-MT1-MMP antibody (Fig. 7A and B).
http://www.tkuhn.ch/bel2nanopub/RAlowT5zANyJV68gcz46xMh4oCczyxM9lxDNamssW8Dzk#_5
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http://www.ncbi.nlm.nih.gov/pubmed/10207013
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support@belframework.org
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Selventa
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2014-07-03T14:31:17.717+02:00
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