<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Jin Y</submitter><funding>Ministry of Science and Technology of Guangdong Province, China</funding><funding>Science and Technology Program of Guangzhou, China</funding><funding>The Fundamental Research Funds for the Central Universities</funding><funding>National Natural Science Foundation of China</funding><funding>Guangdong Province Key Laboratory of Fermentation and Enzyme Engineering Open Fund, China</funding><pagination>1991-2001</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5157777</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>36(17)</volume><pubmed_abstract>Human bronchial smooth muscle cell soluble proteins were analyzed by a combined method of nondenaturing micro 2DE, grid gel-cutting, and quantitative LC-MS/MS and a native protein map was prepared for each of the identified 4323 proteins [1]. A method to evaluate the degree of similarity between the protein maps was developed since we expected the proteins comprising a protein complex would be separated together under nondenaturing conditions. The following procedure was employed using Excel macros; (i) maps that have three or more squares with protein quantity data were selected (2328 maps), (ii) within each map, the quantity values of the squares were normalized setting the highest value to be 1.0, (iii) in comparing a map with another map, the smaller normalized quantity in two correspo</pubmed_abstract><journal>Electrophoresis</journal><pubmed_title>Proteomic analysis of cellular soluble proteins from human bronchial smooth muscle cells by combining nondenaturing micro 2DE and quantitative LC-MS/MS. 2. Similarity search between protein maps for the analysis of protein complexes.</pubmed_title><pmcid>PMC5157777</pmcid><funding_grant_id>31400798</funding_grant_id><funding_grant_id>2012A080204001</funding_grant_id><funding_grant_id>2014J4100022</funding_grant_id><funding_grant_id>FJ2013002</funding_grant_id><funding_grant_id>2013ZM0048</funding_grant_id><pubmed_authors>Zhang J</pubmed_authors><pubmed_authors>Tan W</pubmed_authors><pubmed_authors>Yuan Q</pubmed_authors><pubmed_authors>Jin Y</pubmed_authors><pubmed_authors>Manabe T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Proteomic analysis of cellular soluble proteins from human bronchial smooth muscle cells by combining nondenaturing micro 2DE and quantitative LC-MS/MS. 2. Similarity search between protein maps for the analysis of protein complexes.</name><description>Human bronchial smooth muscle cell soluble proteins were analyzed by a combined method of nondenaturing micro 2DE, grid gel-cutting, and quantitative LC-MS/MS and a native protein map was prepared for each of the identified 4323 proteins [1]. A method to evaluate the degree of similarity between the protein maps was developed since we expected the proteins comprising a protein complex would be separated together under nondenaturing conditions. The following procedure was employed using Excel macros; (i) maps that have three or more squares with protein quantity data were selected (2328 maps), (ii) within each map, the quantity values of the squares were normalized setting the highest value to be 1.0, (iii) in comparing a map with another map, the smaller normalized quantity in two correspo</description><dates><release>2015-01-01T00:00:00Z</release><publication>2015 Sep</publication><modification>2026-05-04T13:21:52.069Z</modification><creation>2019-03-27T02:31:35Z</creation></dates><accession>S-EPMC5157777</accession><cross_references><pubmed>26031785</pubmed><doi>10.1002/elps.201400574</doi></cross_references></HashMap>