<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>8(11)</volume><submitter>Wang L</submitter><pubmed_abstract>FHL1 is multifunctional and serves as a modular protein binding interface to mediate protein-protein interactions. In skeletal muscle, FHL1 is involved in sarcomere assembly, differentiation, growth, and biomechanical stress. Muscle abnormalities may play a major role in congenital clubfoot (CCF) deformity during fetal development. Thus, identifying the interactions of FHL1 could provide important new insights into its functional role in both skeletal muscle development and CCF pathogenesis. Using proteins derived from rat L6GNR4 myoblastocytes, we detected FHL1 interacting proteins by immunoprecipitation. Samples were analyzed by liquid chromatography mass spectrometry (LC-MS). Dynamic gene expression of FHL1 was studied. Additionally, the expression of the possible interacting proteins g</pubmed_abstract><journal>PloS one</journal><pagination>e79551</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3827166</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Identification of an FHL1 protein complex containing gamma-actin and non-muscle myosin IIB by analysis of protein-protein interactions.</pubmed_title><pmcid>PMC3827166</pmcid><pubmed_authors>Zhang Y</pubmed_authors><pubmed_authors>Wu D</pubmed_authors><pubmed_authors>Zhang L</pubmed_authors><pubmed_authors>Li L</pubmed_authors><pubmed_authors>Miao J</pubmed_authors><pubmed_authors>Peng Z</pubmed_authors><pubmed_authors>Yuan Z</pubmed_authors><pubmed_authors>Wang L</pubmed_authors><pubmed_authors>Sun K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification of an FHL1 protein complex containing gamma-actin and non-muscle myosin IIB by analysis of protein-protein interactions.</name><description>FHL1 is multifunctional and serves as a modular protein binding interface to mediate protein-protein interactions. In skeletal muscle, FHL1 is involved in sarcomere assembly, differentiation, growth, and biomechanical stress. Muscle abnormalities may play a major role in congenital clubfoot (CCF) deformity during fetal development. Thus, identifying the interactions of FHL1 could provide important new insights into its functional role in both skeletal muscle development and CCF pathogenesis. Using proteins derived from rat L6GNR4 myoblastocytes, we detected FHL1 interacting proteins by immunoprecipitation. Samples were analyzed by liquid chromatography mass spectrometry (LC-MS). Dynamic gene expression of FHL1 was studied. Additionally, the expression of the possible interacting proteins g</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013</publication><modification>2025-04-04T12:17:58.434Z</modification><creation>2019-03-26T23:16:54Z</creation></dates><accession>S-EPMC3827166</accession><cross_references><pubmed>24265776</pubmed><doi>10.1371/journal.pone.0079551</doi></cross_references></HashMap>