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This work provided a global view of the structural organization of the membrane proteome with respect to divergent functions, and built the foundation for future investigation of the dynamic membrane proteome reorganization in response to different environmental or internal stimuli."],"pubmed_title":["Systematically ranking the tightness of membrane association for peripheral membrane proteins (PMPs)."],"pubmed_authors":["Gao Liyan L,Ge Haitao H,Huang Xiahe X,Liu Kehui K,Zhang Yuanya Y,Xu Wu W,Wang Yingchun Y,","Gao Liyan L, Ge Haitao H, Huang Xiahe X, Liu Kehui K, Zhang Yuanya Y, Xu Wu W, Wang Yingchun Y"],"name_synonyms":["Integral Membrane Proteins, Cell Membrane, membrane, membrane of organ, Integral Membrane Protein, Associations, Protein, Surface, Proteins, Membrane-Associated, Surface Proteins, Membrane Proteins, Membrane Associated Proteins, Integral., Cell Surface, Cell Membrane Proteins, Membrane-Associated Proteins, membranous organ component, Integral, Membrane, Membrane Protein, Cell Surface Proteins, Integral Membrane"],"description_synonyms":["big, Integral Membrane Proteins, Signal Transduction Systems, scale tissue, Signal Transductions, multi-cellular organism, Synechocystis 6803, mol, GLM2, peltate hair, Surface Proteins, number, Receptor-Mediated, Gene, Signal Transduction System, Membrane-Associated Proteins, Aphanocapsa sp. 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File: GLY_M11_20140408.mzml. Published as part of Mol Cell Proteomics. 2014 Dec 13  . From the Abstract: {{i}} Large scale quantitative evaluation of the tightness of membrane association for non-transmembrane proteins is important for identifying true peripheral membrane proteins with functional significance. Herein, we simultaneously ranked more than 1,000 proteins of the photosynthetic model organism Synechocystis sp. PCC 6803 for their relative tightness of membrane association using a proteomic approach. Using multiple precisely ranked and experimentally verified peripheral subunits of photosynthetic protein complexes as the landmarks, we found that proteins involved in two-component signal transduction systems and transporters are overall tightly associated with the membranes, whereas the associations of ribosomal proteins are much weaker ... {{/i}}","dates":{"submission":"2015-01-21"},"accession":"GPM32320007112","cross_references":{"pubmed":["25505158"],"Pride":["PXD001246"],"pride":[],"Pride Archive":["PXD001246"]}}