title: Studying of telomeric protein-protein interactions by Bi-molecular fluorescence complementation (BiFC) and peptide array-based assays.
abstract: Studying protein-protein interactions is critical to our understanding of the signaling pathways. The Telomere Interactome is assembled around the telomeres and consists of proteins and factors from diverse pathways. Dissecting how this protein network contributes to telomere protection and length regulation requires the elucidation of the complex and dynamic interactions between the proteins within the interactome. Here, we focus on the Bi-molecular fluorescence complementation (BiFC) and peptide array methods that have proven vital in our studies of telomere protein interaction networks.
authors: Department of Biochemistry, State Key Laboratory of Biocontrol, College of Life Sciences, Sun Yat-sen University, Guangzhou, China. mawenbin@mail.sysu.edu.cn
authors: Wenbin
authors: W
authors: Ma
authors: Hyeung
authors: H
authors: Kim
authors: Zhou
authors: Z
authors: Songyang
mesh_terms: D005453:Fluorescence; D005816:Genetic Complementation Test; D057809:HEK293 Cells; D006801:Humans; D008856:Microscopy, Fluorescence; D040081:Protein Array Analysis / Q000379:methods*; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000379:methods*; D015398:Signal Transduction; D034501:Telomere-Binding Proteins / Q000032:analysis* / Q000235:genetics / Q000378:metabolism*
chemical_list: D034501:Telomere-Binding Proteins