Structure, dynamics, assembly, and evolution of protein complexes.
By Joseph A. Marsh, Sarah A. Teichmann. 2015
415 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Materials Chemistry
In Molecular Biology
- Peer Bork
- C. von Mering
- Lars Juhl Jensen
- Damian Szklarczyk
- Jaime Huerta-Cepas
- Ivica Letunic
- Milan Simonovic
- Nadezhda T. Doncheva
Citations in the corpus
- SWISS-MODEL: homology modelling of protein structures and complexes (2018, neutral): “A significant contribution to this trend originates from the continuous progress of structure determination technologies, including recent developments of Electron Microscopy (EM) based methods, which are particularly suited for large macromolecular assemblies (4).”
- CORUM: the comprehensive resource of mammalian protein complexes—2019 (2018, background): “According to Teichmann (11), the majority of (known) protein complexes in PDB are homomers.”
- STRING v11: protein–protein association networks with increased coverage, supporting functional discovery in genome-wide experimental datasets (2018, background): “Some interactions are quite well documented and understood, for example in the context of three-dimensional reconstructions of large cellular machineries (4–6), while others are only hinted at so far, through indirect evidence such as genetic observations or statistical predictions.”
- Symmetry and simplicity spontaneously emerge from the algorithmic nature of evolution (2021, background): “This higher compressibility reduces constraints on genotypes, implying that more genotypes will map to simpler, more symmetric phenotypes than to more complex asymmetric ones [2, 3].”