<HashMap><database>biostudies-other</database><scores/><additional><omics_type>Unknown</omics_type><submitter>Lucian Smith</submitter><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/MODEL1904020002</full_dataset_link><repository>biostudies-other</repository><additional_accession>10.1073/pnas.1816000116</additional_accession><pubmed_authors>Mohammad Umer Sharif Shohan</pubmed_authors><pubmed_authors>Lucian Smith</pubmed_authors><pubmed_authors>Simon Mitchell</pubmed_authors></additional><is_claimable>false</is_claimable><name>Simon2019 - NIK-dependent p100 processing into p52 and IkBd degradation, Michaelis-Menten, SBML 2v4</name><description>&lt;notes xmlns="http://www.sbml.org/sbml/level2/version4">      &lt;body xmlns="http://www.w3.org/1999/xhtml">        &lt;p>This model represents NIK-dependent p100 processing into p52  and NIK-dependent IkBd degradation with Michaelis-Menten kinetics. Compare this Michaelis-Menten representation to the mass action model in which the dose-response to increasing p100 mRNA is no longer monotonic due to substrate complex competition.&lt;/p>      &lt;/body>    &lt;/notes></description><dates><release>2019-04-02T00:00:00Z</release><modification>2025-07-15T09:49:05.205Z</modification><creation>2025-03-29T21:59:01.143Z</creation></dates><accession>MODEL1904020002</accession><cross_references><biomodels___db>BIOMD0000000869</biomodels___db><pubmed>31048505</pubmed><ensembl>ENSG00000077150</ensembl><ncit>NCIT:C18888</ncit><ncit>C97201</ncit><ncit>C61559</ncit><mamo>MAMO_0000046</mamo><go>GO:0006397</go><uniprot>Q00653</uniprot><uniprot>Q99558</uniprot><doi>10.1073/pnas.1816000116</doi></cross_references></HashMap>