Javascript must be enabled to use this form.

View Profile	Home Browse Faculty Facility Research Consortia Training Grants Courses Search Support About rSp Help and FAQ's Contact Us	GCC Home
Faculty Profile Last Modified Time: 02:45:04 PM Thu, 16 Apr 2020   Contact Information Jun Qin Associated Profiles  Professor, Biochemistry & Molecular Biology and Molecular & Cellular Biology, Baylor College of Medicine   One Baylor Plaza, Room No.: 145E    jqin@bcm.edu     713-798-1507    Web Link    Lab Webpage    Mass Spectrometry, Proteomics, Cell Cycle, Protein Mass Spectrometry, Network Analysis Proteomics, Protein Interaction Landscape, Biological Mass Spectrometry, Protein Ubiquitination, Sister Chromatid Cohesion in Genome Maintenance    Associated Profiles Research and Expertise Appointments  Research and Expertise Research Interests   Network Analysis Proteomics: The Qin Laboratory is interested in understanding several intriguing biological processes, with a special emphasis on the development and application of cutting-edge mass spectrometry-based proteomics toolkits to untangle challenging biological problems. Protein Interaction Landscape: We have a long standing interest on a concept of "network analysis proteomics." Proteins tend to assemble into multi-subunit protein complexes as the minimal biologically functional units. The execution of biological processes in the cell can be viewed as a network of ordered interactions between different protein complexes. Thus, the understanding of the basic mechanisms of cellular homeostasis relies on our ability to determine the composition of protein complexes and to decipher the interactions between these protein complex modules. Likewise, the understanding of pathogenesis ultimately depends on the knowledge of global perturbations in the protein 'complexome', or a cellular network of protein complex interactions during disease development. Specifically, we are analyzing the endogenous protein complexome by immunoprecipitation (IP) with primary antibody and mass spectrometry. We aim at constructing a complete human protein interactome. Method Development for Biological Mass Spectrometry: As an important part of our research, we are continuously developing novel MS-based proteomic methods that will enable us to analyze dynamic changes of complex biological processes in a quantitative manner. Proteomic Analysis of Protein Ubiquitination: Protein ubiquitination is one of the major post translational modifications (PTMs) that regulate a very broad spectrum of cellular functions. Deregulation of ubiquitination is associated with many human diseases such as cancer and human neurodegenerative disorders. We are developing novel proteomics strategies to systematically profile ubiquitin proteome, and to study the regulation of such system in the biological contexts. Sister Chromatid Cohesion in Genome Maintenance: The cohesin complex plays a central role in genome maintenance by regulating chromosome segregation in mitosis and DNA damage response (DDR) in other phases of the cell cycle. Checkpoint kinas ATM/ATR phosphorylates SMC1 and SMC3, two core components of the cohesin complex. In addition, SMC3 is acetylated at two critical lysine residues and this modification is critical for sister chromatid cohesion and genome instability in both yeast and human. We recently showed that genome-wide binding of SMC1 and SMC3 after ionizing radiation (IR) is enhanced by reinforcing pre-existing cohesin binding sites in human cancer cells. We are now vigorously investigating the functions of sister chromatid cohesion using a combination of mass spectrometry, biochemistry and genetic manipulations.  Publications/Creative Works Click here to search for this faculty member's publications on PubMed.  Appointments Title Department / School Institution Professor Biochemistry and Molecular Biology Baylor College of Medicine

powering - The Partnership
Important Disclaimer: The responsibility for the accuracy of the information contained on these pages lies with the authors and user providing such information.