An intrinsically disordered protein, CP12: jack of all trades and master of the Calvin cycle.
By B. Gontero, S. Maberly. 2012
71 citations recorded by the source corpus.
Subfields: Inorganic 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 Molecular Biology
- Gábor Erdös
- Zsuzsanna Dosztányi
- Bálint Mészáros
- Ursula Jakob
- Dana Reichmann
- Vladimir N Uversky
- Lukasz Kurgan
- Fanchi Meng
Citations in the corpus
- IUPred2A: context-dependent prediction of protein disorder as a function of redox state and protein binding (2018, background): “Fasci-nating examples, such as Hsp33(9), COX17(38) or CP12 (39) indicate that redox sensing can be coupled to disorder-to-order or order-to-disorder transitions.”
- The roles of conditional disorder in redox proteins (2013, background): “One type of post-translational folding switch is constituted by redox-sensitive cysteine thiols, whose capacity to form reversible disulfide bonds promotes order , disorder transitions that reversibly alter the function of the protein depending on the redox environment [10–14].”