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Faculty Profile Last Modified Time: 12:12:50 PM Mon, 20 Apr 2020   Contact Information Anna Malovannaya Associated Profiles  Assistant Professor, Biochemistry and Molecular Biology, Baylor College of Medicine   Mail Box: BCM125, BCM-Cullen Building, Room No.: 108CB    malovann@bcm.edu     (713) 798-8699    Web Link    Lab Webpage    Bioinformatics, Gene Expression and Regulation, Chromosomes, Chromatin, DNA Biology, Cancer, Genomics, Proteomics, Metabolomics, Mass Spectrometry, Protein Interaction Mapping, Immunoprecipitation    Associated Profiles Professional Preparation Research and Expertise Affiliations Appointments  Professional Preparation  Degree Major Institution Year  PhD Molecular and Cellular Biology Baylor College of Medicine 2009  BS Biology, Chemistry University of Wisconsin 2002  Research and Expertise Research Interests   EPICOME is an evolving resource for mass spectrometry-based analyses of human and murine proteomes and protein networks. Complex-Complex Interaction (CCI) Resource is currently available through msGPS (mass spectrometry gene products) portal. CCI Resource: Complex-Complex Interaction (CCI) resource hosts information on the analysis of the human endogenous complexome, based on >3,000 immunoprecipitation experiments that were sequenced with mass spectrometry. This web portal allows users to query CCI networks of interacting proteins grouped in minimal endogenous modules (MEMOs). Protein-protein interactions constitute the molecular backbone of cell biology, where select proteins assemble into meta-stable complexes to form bioactive units. These complexes then dynamically associate with each other in context of larger networks to carry out diverse biological functions. Thus, understanding the basic mechanisms of cell homeostasis requires both knowledge of the composition of protein complexes and the interactions between them. Here, we offer analyses that reveal the intrinsic tiered organization of the interactome in three discrete layers. These are (1) the minimal endogenous core complex modules ('MEMOs'), (2) the unique core complex isoforms ('uniCOREs'), and (3) the complex-complex interaction networks (CCIs). To better convey such modularity, we identified 'obligatory' protein modules in protein complexes (minimal endogenous core complex modules, or MEMOs). These modules represent complexes of proteins with stoichiometric interdependence across the entire IP/MS dataset and serve as the conceptual building blocks of the protein complexome. Each of the human protein-coding gene products is assigned to one MEMO only. MEMOs are then used to reconstitute all distinct protein complex 'isoforms', which we call unique cores (uniCOREs). The multi-subunit protein complexes conventionally described in the literature most closely correspond to uniCOREs in our resource and likely impart biological functional classification. Higher-order, weaker, and non-stoichiometric associations between different MEMOs/uniCOREs form the complex-complex interaction (CCI) networks. We suggest that CCIs represent the backbone of regulatory biology.  Publications/Creative Works Click here to search for this faculty member's publications on PubMed.  Affiliations  Research Consortia GCC Cluster for Cellular and Molecular Biophysics  Training Grants Houston Area Molecular Biophysics Training Program  Appointments Title Department / School Institution Assistant Professor Biochemistry and Molecular Biology Baylor College of Medicine

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