Unknown

Dataset Information

0

Complexome Profiling: Assembly and Remodeling of Protein Complexes.


ABSTRACT: Many proteins have been found to operate in a complex with various biomolecules such as proteins, nucleic acids, carbohydrates, or lipids. Protein complexes can be transient, stable or dynamic and their association is controlled under variable cellular conditions. Complexome profiling is a recently developed mass spectrometry-based method that combines mild separation techniques, native gel electrophoresis, and density gradient centrifugation with quantitative mass spectrometry to generate inventories of protein assemblies within a cell or subcellular fraction. This review summarizes applications of complexome profiling with respect to assembly ranging from single subunits to large macromolecular complexes, as well as their stability, and remodeling in health and disease.

SUBMITTER: Wittig I 

PROVIDER: S-EPMC8346016 | biostudies-literature | 2021 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Complexome Profiling: Assembly and Remodeling of Protein Complexes.

Wittig Ilka I   Malacarne Pedro Felipe PF  

International journal of molecular sciences 20210721 15


Many proteins have been found to operate in a complex with various biomolecules such as proteins, nucleic acids, carbohydrates, or lipids. Protein complexes can be transient, stable or dynamic and their association is controlled under variable cellular conditions. Complexome profiling is a recently developed mass spectrometry-based method that combines mild separation techniques, native gel electrophoresis, and density gradient centrifugation with quantitative mass spectrometry to generate inven  ...[more]

Similar Datasets

| S-EPMC6735710 | biostudies-literature
| S-EPMC8790184 | biostudies-literature
| S-EPMC10602928 | biostudies-literature
| S-EPMC6372068 | biostudies-literature
2018-07-05 | GSE116570 | GEO
| S-EPMC8047798 | biostudies-literature
| S-EPMC8561636 | biostudies-literature
| S-EPMC6791824 | biostudies-literature
| S-EPMC2658002 | biostudies-literature
| S-EPMC6561273 | biostudies-literature